|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5354 |
| Enzyme 1 Name |
Peroxisomal sarcosine oxidase |
| Enzyme 1 Synonyms |
- PSO
- L-pipecolate oxidase
- L-pipecolic acid oxidase
|
| Enzyme 1 Gene Name |
PIPOX |
| Enzyme 1 Protein Sequence |
>Peroxisomal sarcosine oxidase
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
|
| Enzyme 1 Number of Residues |
390 |
| Enzyme 1 Molecular Weight |
44067 |
| Enzyme 1 Theoretical pI |
8.54 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
- sarcosine oxidase activity
|
| Process |
- aromatic compound metabolism
- cellular metabolism
- electron transport
- folic acid and derivative metabolism
- generation of precursor metabolites and energy
- metabolism
- physiological process
- tetrahydrofolate metabolism
|
| Component |
| — |
|
| Enzyme 1 General Function |
Amino acid transport and metabolism |
| Enzyme 1 Specific Function |
Metabolizes sarcosine, L-pipecolic acid and L-proline |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
7157903  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9P0Z9  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
SOX_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1173 bp
ATGGCGGCTCAGAAAGATCTCTGGGACGCCATTGTGATTGGGGCGGGGATCCAGGGCTGC
TTCACTGCATACCACCTCGCCAAACACAGGAAGAGGATCCTCCTGCTGGAGCAGTTCTTT
CTACCACACTCCCGAGGAAGCTCCCATGGACAAAGCCGGATAATCCGAAAGGCGTACCTG
GAAGACTTTTACACCCGGATGATGCATGAGTGCTATCAGATATGGGCCCAGCTGGAGCAC
GAGGCTGGAACCCAATTGCACAGGCAGACTGGATTACTGCTGCTGGGAATGAAAGAGAAT
CAAGAATTAAAGACAATCCAGGCCAATCTGTCGAGGCAGAGGGTAGAACACCAGTGTCTT
TCATCTGAGGAACTGAAGCAACGTTTCCCAAATATTCGGTTGCCCAGGGGAGAAGTGGGG
CTCTTGGACAATTCCGGAGGAGTTATCTATGCATATAAGGCCCTCAGAGCCCTGCAGGAT
GCAATTCGACAGCTAGGAGGCATAGTGCGTGACGGAGAGAAGGTGGTGGAGATAAACCCA
GGGCTACTGGTCACGGTGAAAACCACCTCCAGGAGCTACCAAGCTAAGAGCTTGGTCATC
ACAGCAGGTCCTTGGACCAACCAGCTCCTCCGTCCCCTGGGCATTGAGATGCCTCTCCAG
ACCCTGCGGATCAACGTGTGTTACTGGCGAGAGATGGTTCCTGGGAGCTATGGTGTGTCC
CAGGCCTTTCCGTGCTTCCTGTGGCTGGGCTTGTGTCCCCACCACATCTACGGACTGCCC
ACAGGAGAGTACCCAGGGCTGATGAAGGTCAGCTATCACCACGGCAACCACGCAGACCCT
GAGGAGCGGGACTGCCCCACAGCACGCACAGACATCGGAGACGTCCAGATCCTGAGCAGC
TTTGTCAGAGATCACTTACCTGATCTGAAGCCCGAGCCTGCTGTCATTGAGAGCTGCATG
TACACGAATACCCCTGATGAGCAGTTCATTCTCGATCGCCACCCAAAGTATGACAACATT
GTCATTGGTGCTGGATTCTCTGGGCACGGGTTCAAGCTGGCCCCTGTGGTGGGGAAGATC
CTGTATGAATTAAGCATGAAATTAACACCATCTTATGACTTGGCACCTTTTCGAATCAGC
CGTTTCCCAAGCCTGGCCAAAGCCCACCTGTGA
|
| Enzyme 1 GenBank Gene ID |
AF134593  |
| Enzyme 1 GeneCard ID |
PIPOX  |
| Enzyme 1 GenAtlas ID |
PIPOX  |
| Enzyme 1 HGNC ID |
HGNC:17804  |
| Enzyme 1 Chromosome Location |
17 |
| Enzyme 1 Locus |
17q11.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ: L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem J. 2000 Feb 1;345 Pt 3:487-94. [PubMed
]
- Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5435 |
| Enzyme 2 Name |
Dimethylglycine dehydrogenase, mitochondrial precursor |
| Enzyme 2 Synonyms |
- ME2GLYDH
|
| Enzyme 2 Gene Name |
DMGDH |
| Enzyme 2 Protein Sequence |
>Dimethylglycine dehydrogenase, mitochondrial precursor
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCV
GVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLE
EETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNK
VLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMR
ANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYL
RQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLK
KADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEP
PFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLES
KCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVGVTDLSPFGKF
NIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSE
LHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTPEDLSDDVFKFLQTK
SLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRL
EKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATD
DVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPA
VIIQEPLVLTEPTRNRLQKKGGKDKT
|
| Enzyme 2 Number of Residues |
866 |
| Enzyme 2 Molecular Weight |
96808 |
| Enzyme 2 Theoretical pI |
7.69 |
| Enzyme 2 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- oxidoreductase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- glycine catabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Amino acid transport and metabolism |
| Enzyme 2 Specific Function |
N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor |
| Enzyme 2 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 2 Reactions |
- N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
6650622  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9UI17  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
M2GD_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2601 bp
ATGCTCCGTCCCGGCGCGCAGCTGCTGCGGGGCCTCCTGCTGCGGAGCTGCCCGCTGCAG
GGCTCCCCCGGGCGCCCGCGCTCTGTCTGCGGCCGGGAAGGAGAGGAAAAACCACCCTTA
TCTGCAGAAACACAATGGAAAGACAGAGCAGAAACAGTGATAATTGGAGGTGGCTGTGTT
GGTGTGAGTCTGGCTTATCACCTGGCCAAAGCAGGGATGAAAGATGTGGTCCTGCTGGAG
AAATCAGAGCTCACGGCTGGATCTACCTGGCACGCAGCAGGTTTAACAACTTACTTTCAT
CCTGGAATAAACTTGAAGAAAATACATTATGATAGCATCAAACTTTATGAGAAACTGGAA
GAAGAAACTGGTCAGGTGGTGGGATTCCATCAGCCAGGTAGTATCAGACTTGCTACCACC
CCTGTAAGGGTAGATGAATTTAAATATCAAATGACTCGGACTGGCTGGCATGCAACAGAA
CAGTATCTCATTGAACCTGAAAAAATTCAAGAGATGTTCCCTTTACTCAACATGAATAAG
GTTTTAGCTGGATTGTATAATCCTGGAGATGGTCACATTGATCCTTATTCTCTAACTATG
GCACTGGCTGCTGGGGCTAGGAAATGTGGTGCCCTTTTAAAATATCCTGCACCAGTAACT
TCTCTGAAAGCCAGGTCAGATGGAACATGGGACGTTGAAACACCACAGGGGTCTATGAGA
GCAAATAGAATTGTGAATGCTGCAGGATTTTGGGCTCGTGAAGTAGGTAAAATGATTGGA
CTAGAACATCCTCTCATTCCGGTTCAACATCAATATGTTGTTACATCGACTATATCTGAA
GTGAAAGCTTTGAAACGAGAACTGCCTGTGCTCCGTGACCTGGAAGGATCATATTATCTC
CGACAGGAAAGGGATGGGCTTTTGTTTGGTCCATATGAAAGTCAAGAGAAAATGAAAGTT
CAGGACTCCTGGGTCACCAATGGAGTTCCTCCAGGTTTTGGAAAGGAACTCTTTGAGTCT
GATCTAGATCGAATCATGGAACACATCAAAGCTGCCATGGAAATGGTTCCTGTCTTGAAA
AAGGCTGACATCATCAATGTTGTCAATGGTCCTATCACGTATTCTCCTGACATTCTGCCT
ATGGTGGGGCCCCATCAGGGGGTCAGAAACTACTGGGTGGCTATAGGCTTTGGATATGGC
ATAATCCACGCTGGTGGGGTAGGGAAATATCTCAGTGACTGGATCCTGCATGGAGAACCT
CCTTTTGATCTGATAGAATTGGATCCTAATCGCTATGGCAAATGGACAACAACCCAGTAC
ACTGAGGCCAAAGCAAGAGAATCATATGGATTCAACAATATTGTTGGTTATCCTAAAGAA
GAACGGTTTGCTGGGAGGCCGACTCAACGAGTCAGTGGGCTCTATCAAAGGCTGGAGTCT
AAGTGTTCCATGGGGTTCCATGCTGGCTGGGAGCAGCCGCACTGGTTCTACAAACCAGGC
CAGGACACTCAGTACAGGCCAAGTTTTCGCCGCACAAACTGGTTTGAGCCTGTGGGCTCG
GAGTATAAACAGGTTATGCAAAGAGTAGGGGTAACTGACCTATCACCATTTGGCAAGTTT
AACATCAAAGGCCAAGATTCCATTAGACTACTGGACCATCTCTTTGCAAATGTCATTCCA
AAGGTGGGTTTTACAAATATAAGTCACATGTTAACACCCAAGGGTCGAGTGTATGCTGAG
CTGACTGTTTCTCACCAATCTCCTGGGGAGTTTCTTTTAATTACTGGCTCTGGATCAGAA
CTTCATGATCTTAGATGGATTGAAGAAGAAGCAGTCAAAGGTGGATATGATGTTGAAATT
AAAAACATAACTGATGAGCTTGGAGTTCTTGGAGTTGCTGGGCCACAGGCAAGAAAGGTC
CTTCAGAAACTGACCCCTGAAGATCTTAGTGATGATGTTTTCAAGTTTCTTCAAACCAAG
TCCTTAAAGGTTTCCAACATTCCTGTCACTGCTATTAGGATATCTTATACTGGTGAGCTG
GGTTGGGAGCTGTATCACAGAAGAGAAGATTCTGTGGCGCTGTATGACGCTATCATGAAT
GCAGGCCAGGAGGAGGGAATCGACAATTTTGGAACCTATGCCATGAATGCCTTACGCCTG
GAGAAAGCCTTCAGAGCCTGGGGGTTAGAGATGAACTGTGATACAAATCCTTTGGAAGCT
GGACTGGAATATTTTGTGAAGTTAAATAAGCCAGCAGACTTCATAGGAAAGCAAGCACTG
AAACAGATTAAAGCCAAGGGGCTGAAACGAAGACTGGTCTGCCTCACCTTGGCAACGGAT
GATGTTGATCCAGAGGGAAATGAAAGCATCTGGTACAATGGCAAGGTGGTTGGCAACACG
ACATCTGGAAGCTATAGCTACAGCATCCAGAAGAGTCTGGCTTTCGCATATGTCCCTGTA
CAACTAAGTGAAGTGGGACAGCAAGTGGAAGTTGAACTATTAGGCAAAAATTACCCAGCA
GTCATCATACAAGAACCTTTGGTATTGACCGAACCAACCAGAAACCGGCTTCAGAAAAAA
GGTGGAAAGGACAAAACTTGA
|
| Enzyme 2 GenBank Gene ID |
AF111858  |
| Enzyme 2 GeneCard ID |
DMGDH  |
| Enzyme 2 GenAtlas ID |
DMGDH  |
| Enzyme 2 HGNC ID |
HGNC:24475  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5q14.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Binzak BA, Vockley JG, Jenkins RB, Vockley J: Structure and analysis of the human dimethylglycine dehydrogenase gene. Mol Genet Metab. 2000 Mar;69(3):181-7. [PubMed
]
- Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J: Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency. Am J Hum Genet. 2001 Apr;68(4):839-47. Epub 2001 Feb 28. [PubMed
]
- Moolenaar SH, Poggi-Bach J, Engelke UF, Corstiaensen JM, Heerschap A, de Jong JG, Binzak BA, Vockley J, Wevers RA: Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism: NMR spectroscopy study. Clin Chem. 1999 Apr;45(4):459-64. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5511 |
| Enzyme 3 Name |
Lactoperoxidase precursor |
| Enzyme 3 Synonyms |
- LPO
- Salivary peroxidase
- SPO
|
| Enzyme 3 Gene Name |
LPO |
| Enzyme 3 Protein Sequence |
>Lactoperoxidase precursor
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAM
SSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLE
VGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP
GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSE
YSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINAL
TSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTT
ARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAF
VQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE
NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQ
PTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGL
YGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDS
LQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
|
| Enzyme 3 Number of Residues |
712 |
| Enzyme 3 Molecular Weight |
80289 |
| Enzyme 3 Theoretical pI |
8.76 |
| Enzyme 3 GO Classification |
| Function |
- antioxidant activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Donor + H(2)O(2) = oxidized donor + 2 H(2)O |
| Enzyme 3 Pathways |
- Arachidonic acid metabolism (map00590
)
- Methane metabolism (map00680
)
- Phenylalanine Metabolism (map00360
)
- Stilbene, coumarine and lignin biosynthesis (map00940
)
|
| Enzyme 3 Reactions |
- donor + H2O2 = oxidized donor + 2 H2O
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1209685  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22079  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PERL_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2139 bp
ATGAGGGTCCTTCTCCATCTCCCAGCCCTCCTGGCTTCCCTCATCTTGCTTCAGGCTGCA
GCATCTACCACAAGAGCGCAGACTACCAGAACCTCTGCCATCTCCGATACTGTGAGTCAG
GCCAAGGTCCAAGTCAACAAGGCCTTCCTGGACTCCCGAACCAGGCTGAAGACCGCCATG
AGCTCTGAGACTCCCACCAGCCGACAGCTCTCAGAATACCTCAAGCATGCCAAAGGCCGG
ACGCGCACAGCCATCCGCAATGGACAGGTGTGGGAGGAGTCTTTAAAGAGACTGAGGCAG
AAGGCATCCTTGACCAATGTCACAGATCCCAGCCTGGACTTGACTTCACTGTCTCTGGAG
GTGGGCTGTGGTGCTCCTGCTCCCGTGGTGAGATGCGACCCGTGCAGCCCTTACCGCACC
ATTACGGGAGACTGCAATAACAGGAGGAAGCCTGCGCTGGGCGCCGCCAACAGGGCTCTG
GCGCGCTGGCTGCCCGCGGAGTACGAGGACGGGCTCTCCCTGCCCTTCGGCTGGACGCCG
GGGAAGACGCGCAACGGCTTCCCTCTCCCGCTGGCCCGGGAGGTATCTAACAAGATTGTT
GGCTATCTGAATGAGGAGGGTGTTCTGGACCAAAACAGGTCCCTGCTCTTCATGCAGTGG
GGTCAGATTGTGGATCATGACCTGGACTTTGCCCCTGACACCGAGCTGGGGAGTAGCGAG
TACTCCAAAGCCCAGTGTGATGAGTACTGTATCCAGGGAGACAACTGCTTCCCCATCATG
TTCCCACCCAATGACCCCAAGGCGGGGACTCAAGGGAAATGCATGCCTTTCTTCCGAGCT
GGGTTCGTCTGCCCCACTCCACCCTACAAGTCCCTGGCCCGAGAGCAGATCAACGCTCTG
ACCTCCTTCCTGGATGCCAGCTTTGTGTACAGCTCCGAGCCAAGCCTGGCCAGCCGCCTC
CGCAACCTCAGCAGCCCCCTGGGCCTCATGGCTGTCAACCAGGAGGTCTCAGACCATGGA
CTACCCTACCTGCCCTATGACAGCAAGAAGCCAAGCCCCTGTGAGTTCATCAACACCACT
GCCCGTGTGCCCTGCTTCCTGGCAGGAGATTCTCGAGCCTCAGAGCATATTCTGCTGGCC
ACATCCCACACCCTCTTTCTCCGCGAGCATAACCGGCTGGCCAGAGAACTAAAGAGACTC
AACCCTCAGTGGGATGGAGAGAAGCTCTACCAGGAAGCCCGGAAAATCCTGGGAGCCTTC
GTGCAGATTATCACCTTTAGGGACTACCTACCCATTTTGCTAGGTGACCACATGCAGAAG
TGGATACCCCCATATCAAGGCTACAGTGAATCTGTGGATCCCAGAATTTCCAATGTCTTC
ACCTTCGCCTTCCGCTTTGGCCACTTGGAGGTCCCCTCTAGTATGTTCCGCCTGGATGAG
AATTATCAGCCATGGGGGCCAGAACCAGAACTCCCCCTCCACACCCTCTTCTTCAACACT
TGGAGGATGGTCAAAGATGGTGGAATTGATCCTCTGGTGCGGGGCCTGCTGGCCAAGAAA
TCCAAGCTGATGAAACAGAATAAAATGATGACTGGAGAGCTGCGCAACAAGCTTTTCCAG
CCAACTCACAGGATCCATGGCTTTGACCTGGCTGCCATCAACACACAGCGTTGCCGGGAC
CATGGGCAACCTGGGTACAATTCCTGGAGAGCCTTCTGTGACCTCTCACAGCCGCAGACA
CTAGAGGAGTTGAACACAGTGCTGAAGAGCAAGATGCTGGCCAAGAAGTTACTGGGTCTC
TACGGGACCCCTGACAACATCGACATCTGGATAGGGGCCATTGCTGAGCCGCTGGTGGAA
AGGGGTCGGGTGGGGCCTCTCCTGGCCTGCCTCTTGGGCAAGCAGTTCCAGCAGATCCGT
GATGGAGACAGGTTCTGGTGGGAAAACCCTGGGGTCTTCACGAACGAGCAGAAGGACTCT
CTACAGAAAATGTCCTTCTCACGCCTTGTCTGTGACAACACCCGCATCACCAAGGTCCCA
CGGGACCCATTCTGGGCCAACAGCTACCCCTATGACTTCGTGGATTGCTCAGCCATCGAC
AAGCTGGACCTGTCACCCTGGGCCTCAGTGAAGAATTAG
|
| Enzyme 3 GenBank Gene ID |
U39573  |
| Enzyme 3 GeneCard ID |
LPO  |
| Enzyme 3 GenAtlas ID |
LPO  |
| Enzyme 3 HGNC ID |
HGNC:6678  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q23.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F: Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA. Gene. 1996 Sep 16;173(2):261-4. [PubMed
]
- Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ: Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990 Sep;9(7):499-509. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5517 |
| Enzyme 4 Name |
Eosinophil peroxidase precursor |
| Enzyme 4 Synonyms |
- EPO[Contains: Eosinophil peroxidase light chain
- Eosinophil peroxidase heavy chain]
|
| Enzyme 4 Gene Name |
EPX |
| Enzyme 4 Protein Sequence |
>Eosinophil peroxidase precursor
MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQ
RLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTE
PQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLS
LPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPE
SPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRN
QINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCL
LTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARK
IMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPF
MFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDEL
RDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLAR
KFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTK
RQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT
|
| Enzyme 4 Number of Residues |
715 |
| Enzyme 4 Molecular Weight |
81042 |
| Enzyme 4 Theoretical pI |
10.81 |
| Enzyme 4 GO Classification |
| Function |
- antioxidant activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Donor + H(2)O(2) = oxidized donor + 2 H(2)O |
| Enzyme 4 Pathways |
- Arachidonic acid metabolism (map00590
)
- Methane metabolism (map00680
)
- Phenylalanine Metabolism (map00360
)
- Stilbene, coumarine and lignin biosynthesis (map00940
)
|
| Enzyme 4 Reactions |
- donor + H2O2 = oxidized donor + 2 H2O
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
182146  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P11678  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PERE_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2148 bp
ATGCATCTGCTCCCAGCCCTGGCAGGGGTCCTGGCCACACTCGTCCTCGCCCAGCCCTGT
GAGGGCACTGACCCAGCCTCCCCTGGGGCAGTGGAGACCTCGGTCCTGCGAGACTGCATA
GCAGAGGCCAAGTTGCTGGTGGATGCTGCCTACAATTGGACCCAGAAGAGCATCAAGCAG
CGGCTTCGCAGCGGTTCAGCCAGCCCCATGGACCTCCTGTCCTACTTCAAACAACCGGTA
GCAGCCACCAGGACAGTTGTTCGGGCCGCAGATTATATGCATGTGGCTTTGGGGCTGCTT
GAAGAGAAGTTACAACCCCAGCGGTCCGGACCCTTCAATGTCACTGATGTGCTAACAGAA
CCACAGCTGCGGCTGCTGTCCCAGGCCAGTGGCTGTGCTCTCCGGGACCAGGCCGAGCGC
TGCAGCGACAAGTACCGCACCATCACTGGACGGTGCAACAACAAGAGGAGACCCTTGCTA
GGGGCCTCCAACCAGGCTCTGGCTCGCTGGCTGCCCGCCGAGTATGAGGATGGGCTGTCG
CTCCCCTTCGGCTGGACCCCCAGCAGGAGGCGCAATGGCTTCCTTCTCCCTCTTGTCCGG
GCTGTCTCCAACCAGATTGTGCGCTTCCCCAATGAGAGACTGACCTCCGACCGTGGCCGA
GCCCTCATGTTCATGCAGTGGGGCCAGTTCATTGACCATGACCTGGACTTCTCCCCGGAG
TCCCCGGCCAGAGTGGCCTTCACTGCAGGCGTTGACTGTGAGAGGACCTGCGCCCAGCTG
CCCCCCTGCTTTCCCATCAAGATCCCACCCAATGACCCCCGCATCAAGAACCAGCGTGAC
TGCATCCCTTTCTTCCGCTCGGCACCCTCATGCCCCCAAAACAAGAACAGAGTCCGCAAC
CAGATCAACGCGCTCACCTCCTTTGTGGACGCCAGCATGGTGTATGGCAGTGAGGTCTCC
CTCTCGCTGCGGCTCCGCAACCGGACCAACTACCTGGGGCTGCTGGCCATCAACCAGCGC
TTTCAAGACAACGGCCGGGCCCTGCTGCCCTTCGACAACCTGCACGATGACCCCTGTCTC
CTCACCAACCGCTCGGCGCGCATCCCCTGCTTCCTGGCAGGTGACACCCGATCAACGGAA
ACCCCCAAACTGGCAGCCATGCACACCCTCTTTATGCGAGAGCACAACCGGCTGGCCACC
GAGCTGAGACGCCTGAATCCCCGGTGGAATGGAGACAAACTGTACAATGAGGCTCGGAAG
ATCATGGGGGCCATGGTCCAGATCATCACCTACCGAGACTTTCTGCCCCTGGTTCTGGGC
AAGGCCCGGGCCAGGAGAACCCTGGGGCACTACAGGGGGTACTGCTCCAATGTGGACCCA
CGGGTGGCCAATGTCTTCACCCTGGCCTTCCGCTTTGGCCACACAATGCTCCAGCCCTTC
ATGTTCCGCTTGGACAGTCAGTACCGGGCCTCCGCACCCAACTCGCATGTCCCACTTAGC
TCTGCCTTCTTTGCCAGCTGGCGGATCGTGTATGAAGGGGGCATCGACCCCATCCTCCGG
GGCCTCATGGCCACCCCTGCCAAGCTGAACCGTCAGGATGCCATGTTAGTGGATGAGCTC
CGGGACCGGCTGTTTCGGCAAGTGAGGAGGATTGGGCTGGACCTGGCAGCTCTCAACATG
CAACGAAGCCGGGACCACGGCCTTCCAGGGTACAATGCTTGGAGGCGCTTCTGTGGGCTC
TCCCAGCCCCGGAATTTGGCACAGCTTAGCCGGGTGCTGAAAAACCAGGACTTGGCAAGG
AAGTTCCTGAATTTGTATGGAACACCTGACAACATTGACATCTGGATTGGGGCCATCGCT
GAGCCTCTTTTGCCGGGGGCTCGAGTGGGGCCTCTTCTGGCTTGTCTGTTCGAGAACCAG
TTCAGAAGAGCCCGAGACGGAGACAGGTTCTGGTGGCAGAAACGAGGTGTTTTCACCAAA
AGACAGCGCAAGGCCCTGAGCAGAATTTCCTTGTCTCGAATTATATGTGACAATACCGGT
ATCACCACGGTTTCAAGGGACATCTTCAGAGCCAACATCTACCCTCGGGGCTTTGTGAAC
TGCAGCCGTATCCCCAGGTTGAACCTATCAGCCTGGCGAGGGACATGA
|
| Enzyme 4 GenBank Gene ID |
M29913  |
| Enzyme 4 GeneCard ID |
EPX  |
| Enzyme 4 GenAtlas ID |
EPX  |
| Enzyme 4 HGNC ID |
HGNC:3423  |
| Enzyme 4 Chromosome Location |
17 |
| Enzyme 4 Locus |
17q23.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Sakamaki K, Tomonaga M, Tsukui K, Nagata S: Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem. 1989 Oct 5;264(28):16828-36. [PubMed
]
- Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ: Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J Exp Med. 1989 May 1;169(5):1757-69. [PubMed
]
- Oxvig C, Thomsen AR, Overgaard MT, Sorensen ES, Hojrup P, Bjerrum MJ, Gleich GJ, Sottrup-Jensen L: Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo. J Biol Chem. 1999 Jun 11;274(24):16953-8. [PubMed
]
- Romano M, Patriarca P, Melo C, Baralle FE, Dri P: Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12496-500. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5630 |
| Enzyme 5 Name |
Membrane copper amine oxidase |
| Enzyme 5 Synonyms |
- Semicarbazide-sensitive amine oxidase
- SSAO
- Vascular adhesion protein 1
- VAP-1
- HPAO
|
| Enzyme 5 Gene Name |
AOC3 |
| Enzyme 5 Protein Sequence |
>Membrane copper amine oxidase
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
|
| Enzyme 5 Number of Residues |
763 |
| Enzyme 5 Molecular Weight |
84623 |
| Enzyme 5 Theoretical pI |
6.51 |
| Enzyme 5 GO Classification |
| Function |
- binding
- cation binding
- copper ion binding
- ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 5 Specific Function |
Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin- independent fashion. Has a monoamine oxidase activity |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
1399032  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q16853  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
AOC3_HUMAN  |
| Enzyme 5 PDB ID |
1PU4  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2292 bp
ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG
|
| Enzyme 5 GenBank Gene ID |
U39447  |
| Enzyme 5 GeneCard ID |
AOC3  |
| Enzyme 5 GenAtlas ID |
AOC3  |
| Enzyme 5 HGNC ID |
HGNC:550  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed
]
- Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5631 |
| Enzyme 6 Name |
Retina-specific copper amine oxidase precursor |
| Enzyme 6 Synonyms |
- RAO
- Amine oxidase [copper-containing]
|
| Enzyme 6 Gene Name |
AOC2 |
| Enzyme 6 Protein Sequence |
>Retina-specific copper amine oxidase precursor
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
|
| Enzyme 6 Number of Residues |
756 |
| Enzyme 6 Molecular Weight |
83674 |
| Enzyme 6 Theoretical pI |
7.03 |
| Enzyme 6 GO Classification |
| Function |
- binding
- cation binding
- copper ion binding
- ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 6 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 6 Specific Function |
May be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1906806  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O75106  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
AOC2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2190 bp
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATTGGCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGATACCAG
CTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGCAGTAGCATCTATCACCAGAAT
GACATCTGGACACCCACAGTTACCTTTGCTGACTTCATCAACAATGAAACCCTCTTAGGA
GAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCACATTCCCCATGCCGAGGACATC
CCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTGCTCCGACCCTATAACTTCTTT
GATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTACTTTGAGAAGGGCCAGGATGCT
GGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGACCTGGCAGCCTGTGTCCCGGAC
TTACCCCCTTTCTCTTACCACGGCTTCTAG
|
| Enzyme 6 GenBank Gene ID |
D88213  |
| Enzyme 6 GeneCard ID |
AOC2  |
| Enzyme 6 GenAtlas ID |
AOC2  |
| Enzyme 6 HGNC ID |
HGNC:549  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed
]
- Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6073 |
| Enzyme 7 Name |
Sarcosine dehydrogenase, mitochondrial precursor |
| Enzyme 7 Synonyms |
- SarDH
- BPR-2
|
| Enzyme 7 Gene Name |
SARDH |
| Enzyme 7 Protein Sequence |
>Sarcosine dehydrogenase, mitochondrial precursor
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
|
| Enzyme 7 Number of Residues |
918 |
| Enzyme 7 Molecular Weight |
101038 |
| Enzyme 7 Theoretical pI |
7.26 |
| Enzyme 7 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- oxidoreductase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- glycine catabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 7 General Function |
Amino acid transport and metabolism |
| Enzyme 7 Specific Function |
Sarcosine + acceptor + H(2)O = glycine + formaldehyde + reduced acceptor |
| Enzyme 7 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 7 Reactions |
- sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
5902974  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9UL12  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
SARDH_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2757 bp
ATGGCCTCACTGAGCCGAGCCCTACGTGTGGCTGCTGCCCACCCTCGCCAGAGCCCTACC
CGGGGCATGGGGCCATGCAACCTGTCCAGCGCAGCTGGCCCCACAGCCGAGAAGAGTGTG
CCATATCAGCGGACCCTGAAGGAGGGACAGGGCACCTCGGTGGTGGCCCAAGGCCCAAGC
CGGCCCCTGCCCAGCACGGCCAACGTGGTGGTCATTGGTGGAGGCAGCTTGGGCTGCCAG
ACCCTGTACCACCTGGCCAAGCTGGGCATGAGTGGGGCGGTGCTGCTGGAGCGGGAGCGG
CTGACCTCCGGGACCACCTGGCACACGGCAGGCCTGCTGTGGCAGCTGCGGCCCAGTGAC
GTGGAGGTGGAGCTTCTGGCCCACACTCGGCGGGTGGTGAGCCGGGAGCTGGAGGAGGAG
ACGGGACTACACACGGGCTGGATCCAGAATGGGGGCCTCTTCATCGCGTCCAACCGGCAG
CGCCTGGACGAGTACAAGAGGCTCATGTCGCTGGGCAAGGCGTATGGTGTGGAATCCCAT
GTGCTGAGCCCGGCAGAGACCAAGACTCTGTACCCGCTGATGAATGTGGACGACCTCTAC
GGGACCCTGTATGTGCCGCACGACGGTACCATGGACCCCGCTGGCACCTGTACCACCCTC
GCCAGGGCAGCTTCTGCCCGAGGAGCACAGGTCATTGAGAACTGCCCAGTGACCGGCATT
CGTGTGTGGACGGATGATTTTGGGGTGCGGCGGGTCGCGGGTGTGGAGACTCAGCATGGT
TCCATCCAGACACCCTGCGTGGTCAACTGTGCAGGAGTGTGGGCAAGTGCTGTGGGCCGG
ATGGCTGGAGTCAAGGTCCCGCTGGTGGCCATGCACCATGCCTATGTCGTCACCGAGCGC
ATCGAGGGGATTCAGAACATGCCCAATGTCCGTGATCATGATGCCTCTGTCTACCTCCGC
CTCCAAGGGGATGCCTTGTCTGTGGGTGGCTATGAGGCCAACCCCATCTTTTGGGAGGAG
GTGTCAGACAAGTTTGCCTTCGGCCTCTTTGACCTGGACTGGGAGGTGTTCACCCAGCAC
ATTGAAGGCGCCATCAACAGGGTCCCCGTGCTGGAGAAGACAGGAATCAAGTCCACGGTC
TGCGGCCCTGAATCCTTCACGCCCGACCACAAGCCCCTGATGGGGGAGGCACCTGAGCTC
CGAGGGTTCTTCCTGGGCTGTGGCTTCAACAGCGCAGGAATGATGCTGGGTGGTGGCTGT
GGGCAGGAGCTGGCCCACTGGATCATCCATGGGCGCCCGGAGAAGGACATGCATGGCTAT
GACATCAGGCGCTTCCATCACTCGCTCACGGACCACCCCCGCTGGATCCGAGAGCGAAGC
CATGAGTCCTACGCCAAGAACTACTCCGTCGTCTTCCCCCACGATGAGCCGCTGGCCGGG
CGCAACATGAGGAGAGACCCGCTGCATGAGGAACTCCTTGGACAAGGCTGCGTGTTCCAG
GAGCGGCATGGCTGGGAGCGACCGGGATGGTTTCATCCCCGAGGCCCAGCTCCGGTCCTC
GAGTACGACTACTACGGGGCTTACGGGAGCCGCGCGCACGAGGACTACGCCTACCGCAGG
CTGCTGGCAGACGAGTACACCTTCGCCTTCCCGCCCCACCACGACACGATCAAGAAGGAG
TGCCTGGCCTGCAGAGGGGCCGCCGCTGTGTTTGACATGTCCTACTTCGGGAAGTTCTAC
CTGGTGGGGCTGGATGCAAGGAAGGCTGCCGACTGGCTCTTCTCCGCAGATGTCAGCCGA
CCCCCAGGCTCCACCGTGTACACGTGCATGCTCAACCACCGTGGGGGCACCGAGAGTGAC
CTGACTGTCAGCCGCCTGGCACCCAGCCACCAGGCCTCCCCGCTGGCCCCCGCCTTTGAA
GGGGACGGTTACTACCTGGCCATGGGCGGGGCCGTGGCCCAGCACAACTGGTCCCACATC
ACCACCGTGCTGCAGGACCAGAAGTCCCAGTGCCAGCTCATCGACAGCTCCGAGGACCTG
GGTATGATCAGTATCCAGGGCCCAGCCAGCCGAGCCATTTTGCAGGAGGTGCTGGACGCA
GACCTGAGCAACGAGGCCTTCCCGTTCTCCACCCACAAGCTACTGAGAGCCGCAGGGCAC
CTGGTCCGAGCCATGCGGCTGTCCTTTGTGGGGGAGCTGGGCTGGGAGCTGCACATTCCA
AAGGCGTCCTGCGTGCCTGTGTACCGGGCTGTGATGGCCGCGGGTGCCAAGCACGGCCTC
ATCAACGCAGGGTACCGCGCCATCGACTCCCTGAGCATTGAGAAAGGCTACCGGCACTGG
CACGCGGACCTGCGGCCAGACGACAGCCCCCTGGAGGCAGGCCTGGCCTTCACCTGCAAG
CTCAAGTCGCCGGTGCCCTTCCTGGGGAGGGAGGCCCTGGAGCAGCAGCGGGCCGCAGGC
CTCCGCCGGCGCCTGGTGTGCTTCACCATGGAGGACAAAGTACCCATGTTTGGCCTGGAG
GCCATCTGGAGGAACGGCCAAGTGGTGGGCCATGTCCGGAGGGCTGACTTTGGGTTCGCC
ATCGACAAGACCATCGCCTACGGTTACATCCATGACCCCAGCGGTGGGCCGGTCTCGCTG
GACTTTGTGAAGAGCGGGGACTATGCCCTGGAGAGAATGGGGGTGACCTATGGTGCCCAG
GCTCACCTGAAGTCGCCCTTCGACCCCAACAACAAGAGGGTGAAGGGAATCTACTGA
|
| Enzyme 7 GenBank Gene ID |
AF095735  |
| Enzyme 7 GeneCard ID |
SARDH  |
| Enzyme 7 GenAtlas ID |
SARDH  |
| Enzyme 7 HGNC ID |
HGNC:10536  |
| Enzyme 7 Chromosome Location |
9 |
| Enzyme 7 Locus |
9q33-q34 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Eschenbrenner M, Jorns MS: Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia. Genomics. 1999 Aug 1;59(3):300-8. [PubMed
]
- Gilbert JR, Kumar A, Newey S, Rao N, Ioannou P, Qiu H, Lin D, Xu P, Pettenati MJ, Pericak-Vance MA: Physical and cDNA mapping in the DBH region of human chromosome 9q34. Hum Hered. 2000 May-Jun;50(3):151-7. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6306 |
| Enzyme 8 Name |
Cytochrome P450 3A4 |
| Enzyme 8 Synonyms |
- Quinine 3-monooxygenase
- CYPIIIA4
- Nifedipine oxidase
- Taurochenodeoxycholate 6-alpha- hydroxylase
- NF-25
- P450-PCN1
|
| Enzyme 8 Gene Name |
CYP3A4 |
| Enzyme 8 Protein Sequence |
>Cytochrome P450 3A4
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
|
| Enzyme 8 Number of Residues |
503 |
| Enzyme 8 Molecular Weight |
57344 |
| Enzyme 8 Theoretical pI |
8.25 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 8 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. The enzyme also hydroxylates etoposide |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
- quinine + NADPH + H+ + O2 = 3-hydroxyquinine + NADP+ + H2O
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
181374  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P08684  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
CP3A4_HUMAN  |
| Enzyme 8 PDB ID |
1TQN  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1512 bp
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACCCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTATGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
|
| Enzyme 8 GenBank Gene ID |
M18907  |
| Enzyme 8 GeneCard ID |
CYP3A4  |
| Enzyme 8 GenAtlas ID |
CYP3A4  |
| Enzyme 8 HGNC ID |
HGNC:2637  |
| Enzyme 8 Chromosome Location |
7 |
| Enzyme 8 Locus |
7q21.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Gonzalez FJ, Schmid BJ, Umeno M, Mcbride OW, Hardwick JP, Meyer UA, Gelboin HV, Idle JR: Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase. DNA. 1988 Mar;7(2):79-86. [PubMed
]
- Beaune PH, Umbenhauer DR, Bork RW, Lloyd RS, Guengerich FP: Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8064-8. [PubMed
]
- Spurr NK, Gough AC, Stevenson K, Wolf CR: The human cytochrome P450 CYP3 locus: assignment to chromosome 7q22-qter. Hum Genet. 1989 Jan;81(2):171-4. [PubMed
]
- Bork RW, Muto T, Beaune PH, Srivastava PK, Lloyd RS, Guengerich FP: Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity. J Biol Chem. 1989 Jan 15;264(2):910-9. [PubMed
]
- Chen Q, Wu J, Yu Y: [Establishment of transgenic cell line CHL-3A4 and its metabolic activation] Zhonghua Yu Fang Yi Xue Za Zhi. 1998 Sep;32(5):281-4. [PubMed
]
- Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed
]
- Hsieh KP, Lin YY, Cheng CL, Lai ML, Lin MS, Siest JP, Huang JD: Novel mutations of CYP3A4 in Chinese. Drug Metab Dispos. 2001 Mar;29(3):268-73. [PubMed
]
- Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed
]
- Zhang H, Coville PF, Walker RJ, Miners JO, Birkett DJ, Wanwimolruk S: Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br J Clin Pharmacol. 1997 Mar;43(3):245-52. [PubMed
]
- Zhao XJ, Kawashiro T, Ishizaki T: Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab Dispos. 1998 Feb;26(2):188-91. [PubMed
]
- Sata F, Sapone A, Elizondo G, Stocker P, Miller VP, Zheng W, Raunio H, Crespi CL, Gonzalez FJ: CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: evidence for an allelic variant with altered catalytic activity. Clin Pharmacol Ther. 2000 Jan;67(1):48-56. [PubMed
]
- Dai D, Tang J, Rose R, Hodgson E, Bienstock RJ, Mohrenweiser HW, Goldstein JA: Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos. J Pharmacol Exp Ther. 2001 Dec;299(3):825-31. [PubMed
]
- Eiselt R, Domanski TL, Zibat A, Mueller R, Presecan-Siedel E, Hustert E, Zanger UM, Brockmoller J, Klenk HP, Meyer UA, Khan KK, He YA, Halpert JR, Wojnowski L: Identification and functional characterization of eight CYP3A4 protein variants. Pharmacogenetics. 2001 Jul;11(5):447-58. [PubMed
]
- Lamba JK, Lin YS, Thummel K, Daly A, Watkins PB, Strom S, Zhang J, Schuetz EG: Common allelic variants of cytochrome P4503A4 and their prevalence in different populations. Pharmacogenetics. 2002 Mar;12(2):121-32. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6324 |
| Enzyme 9 Name |
Cytochrome P450 2C9 |
| Enzyme 9 Synonyms |
- (R-limonene 6-monooxygenase
- (S-limonene 6-monooxygenase
- (S- limonene 7-monooxygenase
- CYPIIC9
- P450 PB-1
- P450 MP-4/MP-8
- S- mephenytoin 4-hydroxylase
- P-450MP
|
| Enzyme 9 Gene Name |
CYP2C9 |
| Enzyme 9 Protein Sequence |
>Cytochrome P450 2C9
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
|
| Enzyme 9 Number of Residues |
490 |
| Enzyme 9 Molecular Weight |
55629 |
| Enzyme 9 Theoretical pI |
7.99 |
| Enzyme 9 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 9 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan |
| Enzyme 9 Pathways |
- Limonene and pinene degradation (map00903
)
- Monoterpenoid biosynthesis (map00902
)
|
| Enzyme 9 Reactions |
- (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
181366  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P11712  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
CP2C9_HUMAN  |
| Enzyme 9 PDB ID |
1R9O  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1152 bp
AGAGGATTTGGAATTGTTTTCAGCAATGGAAAGAAATGGAAGGAGATCCGGCGTTTCTCC
CTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGCATTGAGGACCGTGTTCAAGAG
GAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAGGCCTCACCCTGTGATCCCACT
TTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCCATTATTTTCCATAAACGTTTT
GATTATAAAGATCAGCAATTTCTTAACTTAATGGAAAAGTTGAATGAAAACATCAAGATT
TTGAGCAGCCCCTGGATCCAGATCTGCAATAATTTTTCTCCTATCATTGATTACTTCCCG
GGAACTCACAACAAATTACTTAAAAACGTTGCTTTTATGAAAAGTTATATTTTGGAAAAA
GTAAAAGAACACCAAGAATCAATGGACATGAACAACCCTCAGGACTTTATTGATTGCTTC
CTGATGAAAATGGAGAAGGAAAAGCACAACCAACCATCAGAATTTACTATTGAAAGCTTG
GAAAACACTGCAGTTGACTTGTTTGGAGCTGGGACAGAGACGACAAGCACAACCCTGAGA
TATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACAGCTAAAGTCCAGGAAGAGATT
GAACGTGTGATTGGCAGAAACCGGAGCCCCTGCATGCAAGACAGGAGCCACATGCCCTAC
ACAGATGCTGTGGTGCACGAGGTCCAGAGATGCATTGACCTTCTCCCCACCAGCCTGCCC
CATGCAGTGACCTGTGACATTAAATTCAGAAACTATCTCATTCCCAAGGGCACAACCATA
TTAATTTCCCTGACTTCTGTGCTACATGACAACAAAGAATTTCCCAACCCAGAGATGTTT
GACCCTCATCACTTTCTGGATGAAGGTGGCAATTTTAAGAAAAGTAAATACTTCATGCCT
TTCTCAGCAGGAAAACGGATTTGTGTGGGAGAAGCCCTGGCCGGCATGGAGCTGTTTTTA
TTCCTGACCTCCATTTTACAGAACTTTAACCTGAAATCTCTGGTTGACCCAAAGAACCTT
GACACCACTCCAGTTGTCAATGGATTTGCCTCTGTGCCGCCCTTCTACCAGCTGTGCTTC
ATTCCTGTCTGA
|
| Enzyme 9 GenBank Gene ID |
M21940  |
| Enzyme 9 GeneCard ID |
CYP2C9  |
| Enzyme 9 GenAtlas ID |
CYP2C9  |
| Enzyme 9 HGNC ID |
HGNC:2623  |
| Enzyme 9 Chromosome Location |
10 |
| Enzyme 9 Locus |
10q24 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Meehan RR, Gosden JR, Rout D, Hastie ND, Friedberg T, Adesnik M, Buckland R, van Heyningen V, Fletcher J, Spurr NK, et al.: Human cytochrome P-450 PB-1: a multigene family involved in mephenytoin and steroid oxidations that maps to chromosome 10. Am J Hum Genet. 1988 Jan;42(1):26-37. [PubMed
]
- Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed
]
- Yasumori T, Kawano S, Nagata K, Shimada M, Yamazoe Y, Kato R: Nucleotide sequence of a human liver cytochrome P-450 related to the rat male specific form. J Biochem (Tokyo). 1987 Nov;102(5):1075-82. [PubMed
]
- Umbenhauer DR, Martin MV, Lloyd RS, Guengerich FP: Cloning and sequence determination of a complementary DNA related to human liver microsomal cytochrome P-450 S-mephenytoin 4-hydroxylase. Biochemistry. 1987 Feb 24;26(4):1094-9. [PubMed
]
- Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed
]
- Ohgiya S, Komori M, Ohi H, Shiramatsu K, Shinriki N, Kamataki T: Six-base deletion occurring in messages of human cytochrome P-450 in the CYP2C subfamily results in reduction of tolbutamide hydroxylase activity. Biochem Int. 1992 Sep;27(6):1073-81. [PubMed
]
- Shimada T, Misono KS, Guengerich FP: Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J Biol Chem. 1986 Jan 15;261(2):909-21. [PubMed
]
- Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed
]
- Srivastava PK, Yun CH, Beaune PH, Ged C, Guengerich FP: Separation of human liver microsomal tolbutamide hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes. Mol Pharmacol. 1991 Jul;40(1):69-79. [PubMed
]
- Haining RL, Hunter AP, Veronese ME, Trager WF, Rettie AE: Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms. Arch Biochem Biophys. 1996 Sep 15;333(2):447-58. [PubMed
]
- Sandhu P, Baba T, Guengerich FP: Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity. Arch Biochem Biophys. 1993 Nov 1;306(2):443-50. [PubMed
]
- Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed
]
- Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H: Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. [PubMed
]
- Stubbins MJ, Harries LW, Smith G, Tarbit MH, Wolf CR: Genetic analysis of the human cytochrome P450 CYP2C9 locus. Pharmacogenetics. 1996 Oct;6(5):429-39. [PubMed
]
- Bhasker CR, Miners JO, Coulter S, Birkett DJ: Allelic and functional variability of cytochrome P4502C9. Pharmacogenetics. 1997 Feb;7(1):51-8. [PubMed
]
- Imai J, Ieiri I, Mamiya K, Miyahara S, Furuumi H, Nanba E, Yamane M, Fukumaki Y, Ninomiya H, Tashiro N, Otsubo K, Higuchi S: Polymorphism of the cytochrome P450 (CYP) 2C9 gene in Japanese epileptic patients: genetic analysis of the CYP2C9 locus. Pharmacogenetics. 2000 Feb;10(1):85-9. [PubMed
]
- Dickmann LJ, Rettie AE, Kneller MB, Kim RB, Wood AJ, Stein CM, Wilkinson GR, Schwarz UI: Identification and functional characterization of a new CYP2C9 variant (CYP2C9*5) expressed among African Americans. Mol Pharmacol. 2001 Aug;60(2):382-7. [PubMed
]
- Higashi MK, Veenstra DL, Kondo LM, Wittkowsky AK, Srinouanprachanh SL, Farin FM, Rettie AE: Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy. JAMA. 2002 Apr 3;287(13):1690-8. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6326 |
| Enzyme 10 Name |
Cytochrome P450 2C19 |
| Enzyme 10 Synonyms |
- (R-limonene 6-monooxygenase
- (S-limonene 6-monooxygenase
- (S- limonene 7-monooxygenase
- CYPIIC19
- P450-11A
- Mephenytoin 4- hydroxylase
- CYPIIC17
- P450-254C
|
| Enzyme 10 Gene Name |
CYP2C19 |
| Enzyme 10 Protein Sequence |
>Cytochrome P450 2C19
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
|
| Enzyme 10 Number of Residues |
490 |
| Enzyme 10 Molecular Weight |
55932 |
| Enzyme 10 Theoretical pI |
7.42 |
| Enzyme 10 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 10 Specific Function |
Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine |
| Enzyme 10 Pathways |
- Limonene and pinene degradation (map00903
)
- Monoterpenoid biosynthesis (map00902
)
|
| Enzyme 10 Reactions |
- (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
181344  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P33261  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
CP2CJ_HUMAN  |
| Enzyme 10 PDB ID |
1R9O  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1473 bp
ATGGATCCTTTTGTGGTCCTTGTGCTCTGTCTCTCATGTTTGCTTCTCCTTTCAATCTGG
AGACAGAGCTCTGGGAGAGGAAAACTCCCTCCTGGCCCCACTCCTCTCCCAGTGATTGGA
AATATCCTACAGATAGATATTAAGGATGTCAGCAAATCCTTAACCAATCTCTCAAAAATC
TATGGCCCTGTGTTCACTCTGTATTTTGGCCTGGAACGCATGGTGGTGCTGCATGGATAT
GAAGTGGTGAAGGAAGCCCTGATTGATCTTGGAGAGGAGTTTTCTGGAAGAGGCCATTTC
CCACTGGCTGAAAGAGCTAACAGAGGATTTGGAATCGTTTTCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
ATTATTTTCCAGAAACGTTTCGATTATAAAGATCAGCAATTTCTTAACTTGATGGAAAAA
TTGAATGAAAACATCAGGATTGTAAGCACCCCCTGGATCCAGATATGCAATAATTTTCCC
ACTATCATTGATTATTTCCCGGGAACCCATAACAAATTACTTAAAAACCTTGCTTTTATG
GAAAGTGATATTTTGGAGAAAGTAAAAGAACACCAAGAATCGATGGACATCAACAACCCT
CGGGACTTTATTGATTGCTTCCTGATCAAAATGGAGAAGGAAAAGCAAAACCAACAGTCT
GAATTCACTATTGAAAACTTGGTAATCACTGCAGCTGACTTACTTGGAGCTGGGACAGAG
ACAACAAGCACAACCCTGAGATATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAACGTGTCATTGGCAGAAACCGGAGCCCCTGCATGCAG
GACAGGGGCCACATGCCCTACACAGATGCTGTGGTGCACGAGGTCCAGAGATACATCGAC
CTCATCCCCACCAGCCTGCCCCATGCAGTGACCTGTGACGTTAAATTCAGAAACTACCTC
ATTCCCAAGGGCACAACCATATTAACTTCCCTCACTTCTGTGCTACATGACAACAAAGAA
TTTCCCAACCCAGAGATGTTTGACCCTCGTCACTTTCTGGATGAAGGTGGAAATTTTAAG
AAAAGTAACTACTTCATGCCTTTCTCAGCAGGAAAACGGATTTGTGTGGGAGAGGGCCTG
GCCCGCATGGAGCTGTTTTTATTCCTGACCTTCATTTTACAGAACTTTAACCTGAAATCT
CTGATTGACCCAAAGGACCTTGACACAACTCCTGTTGTCAATGGATTTGCTTCTGTCCCG
CCCTTCTATCAGCTGTGCTTCATTCCTGTCTGA
|
| Enzyme 10 GenBank Gene ID |
M61854  |
| Enzyme 10 GeneCard ID |
CYP2C19  |
| Enzyme 10 GenAtlas ID |
CYP2C19  |
| Enzyme 10 HGNC ID |
HGNC:2621  |
| Enzyme 10 Chromosome Location |
10 |
| Enzyme 10 Locus |
10q24.1-q24.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed
]
- Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. Biochemistry. 1993 Feb 9;32(5):1390. [PubMed
]
- Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed
]
- de Morais SM, Wilkinson GR, Blaisdell J, Nakamura K, Meyer UA, Goldstein JA: The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans. J Biol Chem. 1994 Jun 3;269(22):15419-22. [PubMed
]
- De Morais SM, Wilkinson GR, Blaisdell J, Meyer UA, Nakamura K, Goldstein JA: Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese. Mol Pharmacol. 1994 Oct;46(4):594-8. [PubMed
]
- Xiao ZS, Goldstein JA, Xie HG, Blaisdell J, Wang W, Jiang CH, Yan FX, He N, Huang SL, Xu ZH, Zhou HH: Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele. J Pharmacol Exp Ther. 1997 Apr;281(1):604-9. [PubMed
]
- Ibeanu GC, Goldstein JA, Meyer U, Benhamou S, Bouchardy C, Dayer P, Ghanayem BI, Blaisdell J: Identification of new human CYP2C19 alleles (CYP2C19*6 and CYP2C19*2B) in a Caucasian poor metabolizer of mephenytoin. J Pharmacol Exp Ther. 1998 Sep;286(3):1490-5. [PubMed
]
- Ibeanu GC, Blaisdell J, Ghanayem BI, Beyeler C, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Daly AK, Goldstein JA: An additional defective allele, CYP2C19*5, contributes to the S-mephenytoin poor metabolizer phenotype in Caucasians. Pharmacogenetics. 1998 Apr;8(2):129-35. [PubMed
]
- Ibeanu GC, Blaisdell J, Ferguson RJ, Ghanayem BI, Brosen K, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Goldstein JA: A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin. J Pharmacol Exp Ther. 1999 Aug;290(2):635-40. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6840 |
| Enzyme 11 Name |
Cytochrome P450 2E1 |
| Enzyme 11 Synonyms |
- CYPIIE1
- P450-J
|
| Enzyme 11 Gene Name |
CYP2E1 |
| Enzyme 11 Protein Sequence |
>Cytochrome P450 2E1
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
|
| Enzyme 11 Number of Residues |
493 |
| Enzyme 11 Molecular Weight |
56850 |
| Enzyme 11 Theoretical pI |
8.22 |
| Enzyme 11 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 11 Specific Function |
Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
Not Available |
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
181360  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P05181  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
CP2E1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1482 bp
ATGTCTGCCCTCGGAGTGACCGTGGCCCTGCTGGTGTGGGCGGCCTTCCTCCTGCTGGTG
TCCATGTGGAGGCAGGTGCACAGCAGCTGGAATCTGCCCCCAGGTCCTTTCCCGCTTCCC
ATCATCGGGAACCTCTTCCAGTTGGAATTGAAGAATATTCCCAAGTCCTTCACCCGGTTG
GCCCAGCGCTTCGGGCCGGTGTTCACGCTGTACGTGGGCTCGCAGCGCATGGTGGTGATG
CACGGCTACAAGGCGGTGAAGGAAGCGCTGCTGGACTACAAGGACGAGTTCTCGGGCAGA
GGCGACCTCCCCGCGTTCCATGCGCACAGGGACAGGGGAATCATTTTTAATAATGGACCT
ACCTGGAAGGACATCCGGCGGTTTTCCCTGACCACCCTCCGGAACTATGGGATGGGGAAA
CAGGGCAATGAGAGCCGGATCCAGAGGGAGGCCCACTTCCTGCTGGAAGCACTCAGGAAG
ACCCAAGGCCAGCCTTTCGACCCCACCTTCCTCATCGGCTGCGCGCCCTGCAACGTCATA
GCCGACATCCTCTTCCGCAAGCATTTTGACTACAATGATGAGAAGTTTCTAAGGCTGATG
TATTTGTTTAATGAGAACTTCCACCTACTCAGCACTCCCTGGCTCCAGCTTTACAATAAT
TTTCCCAGCTTTCTACACTACTTGCCTGGAAGCCACAGAAAAGTCATAAAAAATGTGGCT
GAAGTAAAAGAGTATGTGTCTGAAAGGGTGAAGGAGCACCATCAATCTCTGGACCCCAAC
TGTCCCCGGGACCTCACCGACTGCCTGCTCGTGGAAATGGAGAAGGAAAAGCACAGTGCA
GAGCGCTTGTACACAATGGACGGTATCACCGTGACTGTGGCCGACCTGTTCTTTGCGGGG
ACAGAGACCACCAGCACAACTCTGAGATATGGGCTCCTGATTCTCATGAAATACCCTGAG
ATCGAAGAGAAGCTCCATGAAGAAATTGACAGGGTGATTGGGCCAAGCCGAATCCCTGCC
ATCAAGGATAGGCAAGAGATGCCCTACATGGATGCTGTGGTGCATGAGATTCAGCGGTTC
ATCACCCTCGTGCCCTCCAACCTGCCCCATGAAGCAACCCGAGACACCATTTTCAGAGGA
TACCTCATCCCCAAGGGCACAGTCGTAGTGCCAACTCTGGACTCTGTTTTGTATGACAAC
CAAGAATTTCCTGATCCAGAAAAGTTTAAGCCAGAACACTTCCTGAATGAAAATGGAAAG
TTCAAGTACAGTGACTATTTCAAGCCATTTTCCACAGGAAAACGAGTGTGTGCTGGAGAA
GGCCTGGCTCGCATGGAGTTGTTTCTTTTGTTGTGTGCCATTTTGCAGCATTTTAATTTG
AAGCCTCTCGTTGACCCAAAGGATATCGACCTCAGCCCTATACATATTGGGTTTGGCTGT
ATCCCACCACGTTACAAACTCTGTGTCATTCCCCGCTCATGA
|
| Enzyme 11 GenBank Gene ID |
J02625  |
| Enzyme 11 GeneCard ID |
CYP2E1  |
| Enzyme 11 GenAtlas ID |
CYP2E1  |
| Enzyme 11 HGNC ID |
HGNC:2631  |
| Enzyme 11 Chromosome Location |
10 |
| Enzyme 11 Locus |
10q24.3-qter |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Song BJ, Gelboin HV, Park SS, Yang CS, Gonzalez FJ: Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme. J Biol Chem. 1986 Dec 15;261(35):16689-97. [PubMed
]
- Umeno M, McBride OW, Yang CS, Gelboin HV, Gonzalez FJ: Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry. 1988 Dec 13;27(25):9006-13. [PubMed
]
- Lasker JM, Raucy J, Kubota S, Bloswick BP, Black M, Lieber CS: Purification and characterization of human liver cytochrome P-450-ALC. Biochem Biophys Res Commun. 1987 Oct 14;148(1):232-8. [PubMed
]
- Robinson RC, Shorr RG, Varrichio A, Park SS, Gelboin HV, Miller H, Friedman FK: Human liver cytochrome P-450 related to a rat acetone-inducible, nitrosamine-metabolizing cytochrome P-450: identification and isolation. Pharmacology. 1989;39(3):137-44. [PubMed
]
- Gillam EM, Guo Z, Guengerich FP: Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties. Arch Biochem Biophys. 1994 Jul;312(1):59-66. [PubMed
]
- Hu Y, Oscarson M, Johansson I, Yue QY, Dahl ML, Tabone M, Arinco S, Albano E, Ingelman-Sundberg M: Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol. 1997 Mar;51(3):370-6. [PubMed
]
- Fairbrother KS, Grove J, de Waziers I, Steimel DT, Day CP, Crespi CL, Daly AK: Detection and characterization of novel polymorphisms in the CYP2E1 gene. Pharmacogenetics. 1998 Dec;8(6):543-52. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6843 |
| Enzyme 12 Name |
Cytochrome P450 1B1 |
| Enzyme 12 Synonyms |
- CYPIB1
|
| Enzyme 12 Gene Name |
CYP1B1 |
| Enzyme 12 Protein Sequence |
>Cytochrome P450 1B1
MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI
GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF
ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL
LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL
VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA
EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL
DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV
FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL
FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE
TCQ
|
| Enzyme 12 Number of Residues |
543 |
| Enzyme 12 Molecular Weight |
60847 |
| Enzyme 12 Theoretical pI |
9.23 |
| Enzyme 12 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 12 Specific Function |
Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
501031  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q16678  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
CP1B1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1632 bp
ATGGGCACCAGCCTCAGCCCGAACGACCCTTGGCCGCTAAACCCGCTGTCCATCCAGCAG
ACCACGCTCCTGCTACTCCTGTCGGTGCTGGCCACTGTGCATGTGGGCCAGCGGCTGCTG
AGGCAACGGAGGCGGCAGCTCCGGTCCGCGCCCCCGGGCCCGTTTGCGTGGCCACTGATC
GGAAACGCGGCGGCGGTGGGCCAGGCGGCTCACCTCTCGTTCGCTCGCCTGGCGCGGCGC
TACGGCGACGTTTTCCAGATCCGCCTGGGCAGCTGCCCCATAGTGGTGCTGAATGGCGAG
CGCGCCATCCACCAGGCCCTGGTGCAGCAGGGCTCGGCCTTCGCCGACCGGCCGGCCTTC
GCCTCCTTCCGTGTGGTGTCCGGCGGCCGCAGCATGGCTTTCGGCCACTACTCGGAGCAC
TGGAAGGTGCAGCGGCGCGCAGCCCACAGCATGATGCGCAACTTCTTCACGCGCCAGCCG
CGCAGCCGCCAAGTCCTCGAGGGCCACGTGCTGAGCGAGGCGCGCGAGCTGGTGGCGCTG
CTGGTGCGCGGCAGCGCGGACGGCGCCTTCCTCGACCCGAGGCCGCTGACCGTCGTGGCC
GTGGCCAACGTCATGAGTGCCGTGTGTTTCGGCTGCCGCTACAGCCACGACGACCCCGAG
TTCCGTGAGCTGCTCAGCCACAACGAAGAGTTCGGGCGCACGGTGGGCGCGGGCAGCCTG
GTGGACGTGATGCCCTGGCTGCAGTACTTCCCCAACCCGGTGCGCACCGTTTTCCGCGAA
TTCGAGCAGCTCAACCGCAACTTCAGCAACTTCATCCTGGACAAGTTCTTGAGGCACTGC
GAAAGCCTTCGGCCCGGGGCCGCCCCCCGCGACATGATGGACGCCTTTATCCTCTCTGCG
GAAAAGAAGGCGGCCGGGGACTCGCACGGTGGTGGCGCGCGGCTGGATTTGGAGAACGTA
CCGGCCACTATCACTGACATCTTCGGCGCCAGCCAGGACACCCTGTCCACCGCGCTGCAG
TGGCTGCTCCTCCTCTTCACCAGGTATCCTGATGTGCAGACTCGAGTGCAGGCAGAATTG
GATCAGGTCGTGGGGAGGGACCGTCTGCCTTGTATGGGTGACCAGCCCAACCTGCCCTAT
GTCCTGGCCTTCCTTTATGAAGCCATGCGCTTCTCCAGCTTTGTGCCTGTCACTATTCCT
CATGCCACCACTGCCAACACCTCTGTCTTGGGCTACCACATTCCCAAGGACACTGTGGTT
TTTGTCAACCAGTGGTCTGTGAATCATGACCCAGTGAAGTGGCCTAACCCGGAGAACTTT
GATCCAGCTCGATTCTTGGACAAGGATGGCCTCATCAACAAGGACCTGACCAGCAGAGTG
ATGATTTTTTCAGTGGGCAAAAGGCGGTGCATTGGCGAAGAACTTTCTAAGATGCAGCTT
TTTCTCTTCATCTCCATCCTGGCTCACCAGTGCGATTTCAGGGCCAACCCAAATGAGCCT
GCGAAAATGAATTTCAGTTATGGTCTAACCATTAAACCCAAGTCATTTAAAGTCAATGTC
ACTCTCAGAGAGTCCATGGAGCTCCTTGATAGTGCTGTCCAAAATTTACAAGCCAAGGAA
ACTTGCCAATAA
|
| Enzyme 12 GenBank Gene ID |
U03688  |
| Enzyme 12 GeneCard ID |
CYP1B1  |
| Enzyme 12 GenAtlas ID |
CYP1B1  |
| Enzyme 12 HGNC ID |
HGNC:2597  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
2p21 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Sutter TR, Tang YM, Hayes CL, Wo YY, Jabs EW, Li X, Yin H, Cody CW, Greenlee WF: Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. J Biol Chem. 1994 May 6;269(18):13092-9. [PubMed
]
- Tang YM, Wo YY, Stewart J, Hawkins AL, Griffin CA, Sutter TR, Greenlee WF: Isolation and characterization of the human cytochrome P450 CYP1B1 gene. J Biol Chem. 1996 Nov 8;271(45):28324-30. [PubMed
]
- Bejjani BA, Lewis RA, Tomey KF, Anderson KL, Dueker DK, Jabak M, Astle WF, Otterud B, Leppert M, Lupski JR: Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia. Am J Hum Genet. 1998 Feb;62(2):325-33. [PubMed
]
- Stoilov I, Akarsu AN, Alozie I, Child A, Barsoum-Homsy M, Turacli ME, Or M, Lewis RA, Ozdemir N, Brice G, Aktan SG, Chevrette L, Coca-Prados M, Sarfarazi M: Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1. Am J Hum Genet. 1998 Mar;62(3):573-84. [PubMed
]
- Bailey LR, Roodi N, Dupont WD, Parl FF: Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer. Cancer Res. 1998 Nov 15;58(22):5038-41. [PubMed
]
- Vincent AL, Billingsley G, Buys Y, Levin AV, Priston M, Trope G, Williams-Lyn D, Heon E: Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. Am J Hum Genet. 2002 Feb;70(2):448-60. Epub 2002 Jan 3. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6847 |
| Enzyme 13 Name |
Cytochrome P450 2F1 |
| Enzyme 13 Synonyms |
- CYPIIF1
|
| Enzyme 13 Gene Name |
CYP2F1 |
| Enzyme 13 Protein Sequence |
>Cytochrome P450 2F1
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSK
EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDR
WKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLADVRKTEGEPFDPTFVLSRSVSNIIC
SVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDILDPRFPSLLDWVPGPHQRIFQ
NFKCLRDLIAHSVHDHQASSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGT
KTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA
DIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF
KKSPAFMPFSAGRRLCLGELLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNL
PRPFQLCLRPR
|
| Enzyme 13 Number of Residues |
491 |
| Enzyme 13 Molecular Weight |
55500 |
| Enzyme 13 Theoretical pI |
7.40 |
| Enzyme 13 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 13 Specific Function |
Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene- indolenine |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
181358  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P24903  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CP2F1_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1476 bp
ATGGACAGCATAAGCACAGCCATCTTACTCCTGCTCCTGGCTCTCGTCTGTCTGCTCCTG
ACCCTAAGCTCAAGAGATAAGGGAAAGCTGCCTCCGGGACCCAGACCCCTCTCAATCCTG
GGAAACCTGCTGCTGCTTTGCTCCCAAGACATGCTGACTTCTCTCACTAAGCTGAGCAAG
GAGTATGGCTCCATGTACACAGTGCACCTGGGACCCAGGCGGGTGGTGGTCCTCAGCGGG
TACCAAGCTGTGAAGGAGGCCCTGGTGGACCAGGGAGAGGAGTTTAGTGGCCGCGGTGAC
TACCCTGCCTTTTTCAACTTTACCAAGGGCAATGGCATCGCCTTCTCCAGTGGGGATCGA
TGGAAGGTCCTGAGACAGTTCTCTATCCAGATTCTACGGAATTTCGGGATGGGGAAGAGA
AGCATTGAGGAGCGAATCCTAGAGGAGGGCAGCTTCCTGCTGGCGGACGTGCGGAAAACT
GAAGGCGAGCCCTTTGACCCCACGTTTGTGCTGAGTCGCTCAGTGTCCAACATTATCTGT
TCCGTGCTCTTCGGCAGCCGCTTCGACTATGATGATGAGCGTCTGCTCACCATTATCCGC
CTTATCAATGACAACTTCCAAATCATGAGCAGCCCCTGGGGCGAGTTGTACGACATCCTA
GACCCCAGATTCCCGAGCCTCCTGGACTGGGTGCCTGGGCCGCACCAACGCATCTTCCAG
AACTTCAAGTGCCTGAGAGACCTCATCGCCCACAGCGTCCACGACCACCAGGCCTCGTCT
CCCCGGGACTTCATCCAGTGCTTCCTCACCAAGATGGCAGAGGAGAAGGAGGACCCACTG
AGCCACTTCCACATGGATACCCTGCTGATGACCACACATAACCTGCTCTTTGGCGGCACC
AAGACGGTGAGCACCACGCTGCACCACGCCTTCCTGGCACTCATGAAGTACCCAAAAGTT
CAAGCCCGCGTGCAGGAGGAGATCGACCTCGTGGTGGGACGCGCGCGGCTGCCGGCGCTG
AAGGACCGCGCGGCCATGCCTTACACAGACGCGGTGATCCACGAGGTGCAGCGCTTTGCA
GACATCATCCCCATGAACTTGCCGCACCGCGTCACTAGGGACACGGCCTTTCGCGGCTTC
CTGATACCCAAGGGCACCGATGTCATCACCCTCCTTAACACCGTCCACTACGACCCCAGC
CAGTTCCTGACGCCCCAGGAGTTCAACCCCGAGCATTTTTTGGATGCCAATCAGTCCTTC
AAGAAGAGTCCAGCCTTCATGCCCTTCTCAGCTGGGCGCCGTCTGTGCCTGGGAGAGCTG
CTGGCGCGCATGGAGCTCTTTCTGTACCTCACCGCCATCCTGCAGAGCTTTTCGCTGCAG
CCGCTGGGTGCGCCCGAGGACATCGACCTGACCCCACTCAGCTCAGGTCTTGGCAATTTG
CCGCGGCCTTTCCAGCTGTGCCTGCGCCCGCGCTAA
|
| Enzyme 13 GenBank Gene ID |
J02906  |
| Enzyme 13 GeneCard ID |
CYP2F1  |
| Enzyme 13 GenAtlas ID |
CYP2F1  |
| Enzyme 13 HGNC ID |
HGNC:2632  |
| Enzyme 13 Chromosome Location |
19 |
| Enzyme 13 Locus |
19q13.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Nhamburo PT, Kimura S, McBride OW, Kozak CA, Gelboin HV, Gonzalez FJ: The human CYP2F gene subfamily: identification of a cDNA encoding a new cytochrome P450, cDNA-directed expression, and chromosome mapping. Biochemistry. 1990 Jun 12;29(23):5491-9. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6849 |
| Enzyme 14 Name |
Cytochrome P450 2B6 |
| Enzyme 14 Synonyms |
- CYPIIB6
- P450 IIB1
|
| Enzyme 14 Gene Name |
CYP2B6 |
| Enzyme 14 Protein Sequence |
>Cytochrome P450 2B6
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
|
| Enzyme 14 Number of Residues |
491 |
| Enzyme 14 Molecular Weight |
56279 |
| Enzyme 14 Theoretical pI |
8.44 |
| Enzyme 14 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 14 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
181296  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P20813  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
CP2B6_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1476 bp
ATGGAACTCAGCGTCCTCCTCTTCCTTGCACTCCTCACAGGACTCTTGCTACTCCTGGTT
CAGCGCCACCCTAACACCCATGACCGCCTCCCACCAGGGCCCCGCCCTCTGCCCCTTTTG
GGAAACCTTCTGCAGATGGATAGAAGAGGCCTACTCAAATCCTTTCTGAGGTTCCGAGAG
AAATATGGGGACGTCTTCACGGTACACCTGGGACCGAGGCCCGTGGTCATGCTGTGTGGA
GTAGAGGCCATACGGGAGGCCCTTGTGGACAAGGCTGAGGCCTTCTCTGGCCGGGGAAAA
ATCGCCATGGTCGACCCATTCTTCCGGGGATATGGTGTGATCTTTGCCAATGGAAACCGC
TGGAAGGTGCTTCGGCGATTCTCTGTGACCACTATGAGGGACTTCGGGATGGGAAAGCGG
AGTGTGGAGGAGCGGATTCAGGAGGAGGCTCAGTGTCTGATAGAGGAGCTTCGGAAATCC
AAGGGGGCCCTCATGGACCCCACCTTCCTCTTCCAGTCCATTACCGCCAACATCATCTGC
TCCATCGTCTTTGGAAAACGATTCCACTACCAAGATCAAGAGTTCCTGAAGATGCTGAAC
TTGTTCTACCAGACTTTTTCACTCATCAGCTCTGTATTCGGCCAGCTGTTTGAGCTCTTC
TCTGGCTTCTTGAAATACTTTCCTGGGGCACACAGGCAAGTTTACAAAAACCTGCAGGAA
ATCAATGCTTACATTGGCCACAGTGTGGAGAAGCACCGTGAAACCCTGGACCCCAGCGCC
CCCAAGGACCTCATCGACACCTACCTGCTCCACATGGAAAAAGAGAAATCCAACGCACAC
AGTGAATTCAGCCACCAGAACCTCAACCTCAACACGCTCTCGCTCTTCTTTGCTGGCACT
GAGACCACCAGCACCACTCTCCGCTACGGCTTCCTGCTCATGCTCAAATACCCTCATGTT
GCAGAGAGAGTCTACAGGGAGATTGAACAGGTGATTGGCCCACATCGCCCTCCAGAGCTT
CATGACCGAGCCAAAATGCCATACACAGAGGCAGTCATCTATGAGATTCAGAGATTTTCC
GACCTTCTCCCCATGGGTGTGCCCCACATTGTCACCCAACACACCAGCTTCCGAGGGTAC
ATCATCCCCAAGGACACAGAAGTATTTCTCATCCTGAGCACTGCTCTCCATGACCCACAC
TACTTTGAAAAACCAGACGCCTTCAATCCTGACCACTTTCTGGATGCCAATGGGGCACTG
AAAAAGACTGAAGCTTTTATCCCCTTCTCCTTAGGGAAGCGGATTTGTCTTGGTGAAGGC
ATCGCCCGTGCGGAATTGTTCCTCTTCTTCACCACCATCCTCCAGAACTTCTCCATGGCC
AGCCCCGTGGCCCCAGAAGACATCGATCTGACACCCCAGGAGTGTGGTGTGGGCAAAATA
CCCCCAACATACCAGATCCGCTTCCTGCCCCGCTGA
|
| Enzyme 14 GenBank Gene ID |
M29874  |
| Enzyme 14 GeneCard ID |
CYP2B6  |
| Enzyme 14 GenAtlas ID |
CYP2B6  |
| Enzyme 14 HGNC ID |
HGNC:2615  |
| Enzyme 14 Chromosome Location |
19 |
| Enzyme 14 Locus |
19q13.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Yamano S, Nhamburo PT, Aoyama T, Meyer UA, Inaba T, Kalow W, Gelboin HV, McBride OW, Gonzalez FJ: cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver. Biochemistry. 1989 Sep 5;28(18):7340-8. [PubMed
]
- Miles JS, McLaren AW, Wolf CR: Alternative splicing in the human cytochrome P450IIB6 gene generates a high level of aberrant messages. Nucleic Acids Res. 1989 Oct 25;17(20):8241-55. [PubMed
]
- Thum T, Borlak J: Gene expression in distinct regions of the heart. Lancet. 2000 Mar 18;355(9208):979-83. [PubMed
]
- Ariyoshi N, Miyazaki M, Toide K, Sawamura Yi, Kamataki T: A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation. Biochem Biophys Res Commun. 2001 Mar;281(5):1256-60. [PubMed
]
- Lang T, Klein K, Fischer J, Nussler AK, Neuhaus P, Hofmann U, Eichelbaum M, Schwab M, Zanger UM: Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver. Pharmacogenetics. 2001 Jul;11(5):399-415. [PubMed
]
- Jinno H, Tanaka-Kagawa T, Ohno A, Makino Y, Matsushima E, Hanioka N, Ando M: Functional characterization of cytochrome P450 2B6 allelic variants. Drug Metab Dispos. 2003 Apr;31(4):398-403. [PubMed
]
- Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6852 |
| Enzyme 15 Name |
Cytochrome P450 2A13 |
| Enzyme 15 Synonyms |
- CYPIIA13
|
| Enzyme 15 Gene Name |
CYP2A13 |
| Enzyme 15 Protein Sequence |
>Cytochrome P450 2A13
MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN
GERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKE
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFF
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQ
RFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
|
| Enzyme 15 Number of Residues |
494 |
| Enzyme 15 Molecular Weight |
56688 |
| Enzyme 15 Theoretical pI |
9.78 |
| Enzyme 15 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 15 Specific Function |
Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N- dimethylaniline, 2'-methoxyacetophenone, N- nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4- (methylnitrosamino)-1-(3-pyridyl)-1-butanone |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
Not Available |
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
1777437  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q16696  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
CP2AD_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGACCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCAGTCTGGCGGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCTGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGCGGACATGATGCCGTCAAGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAGGCCACCTTCGACTGGCTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTAAGGGGTTTTGGCGTG
GGCAAGCGCGGCATCGAGGAACGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTGGGAAGGTTCCAGTTCACGGGAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGGAG
CTGCAAGGGCTGGAGGACTTCATCGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATCGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACAGAGTTCTACTTGAAGAACCTGGTGATGACCACCCTGAACCTCTTCTTT
GCGGGCACTGAGACCGTGAGCACCACCCTGCGCTACGGTTTCCTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACACAGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACATGCTCCCCATGGGTTTGGCCCACAGGGTCAACAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACTGAAGTGTTCCCTATGCTGGGCTCCGAGCTGAGA
GACCCCAGGTTCTTCTCCAACCCCCAGGACTGCAGTCCCCAGCACTTCCTGGATGAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTT
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCATCATGCAGAACTTT
CGCTTCAAGTCCCCTCAGTCGCCTAAGGATATCGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
|
| Enzyme 15 GenBank Gene ID |
U22028  |
| Enzyme 15 GeneCard ID |
CYP2A13  |
| Enzyme 15 GenAtlas ID |
CYP2A13  |
| Enzyme 15 HGNC ID |
HGNC:2608  |
| Enzyme 15 Chromosome Location |
19 |
| Enzyme 15 Locus |
19q13.2 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed
]
- Su T, Bao Z, Zhang QY, Smith TJ, Hong JY, Ding X: Human cytochrome P450 CYP2A13: predominant expression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Cancer Res. 2000 Sep 15;60(18):5074-9. [PubMed
]
- Zhang X, Su T, Zhang QY, Gu J, Caggana M, Li H, Ding X: Genetic polymorphisms of the human CYP2A13 gene: identification of single-nucleotide polymorphisms and functional characterization of an Arg257Cys variant. J Pharmacol Exp Ther. 2002 Aug;302(2):416-23. [PubMed
]
- Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6854 |
| Enzyme 16 Name |
Cytochrome P450 4B1 |
| Enzyme 16 Synonyms |
- CYPIVB1
- P450-HP
|
| Enzyme 16 Gene Name |
CYP4B1 |
| Enzyme 16 Protein Sequence |
>Cytochrome P450 4B1
MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE
IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ
WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI
FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT
PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL
SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL
GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP
DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP
SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
|
| Enzyme 16 Number of Residues |
511 |
| Enzyme 16 Molecular Weight |
58992 |
| Enzyme 16 Theoretical pI |
8.39 |
| Enzyme 16 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 16 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
Not Available |
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
180969  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P13584  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
CP4B1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1536 bp
ATGGTGCCCAGCTTCCTCTCCCTGAGCTTCTCCTCCTTGGGCCTGTGGGCTTCTGGGCTG
ATCTTGGTCTTAGGCTTTCTCAAGCTCATCCACCTGCTGCTGCGGAGGCGAACGTTGGCT
AAGGCTATGGACAAATTCCCAGGGCCTCCCACCCACTGGCTTTTTGGACATGCCCTCGAG
ATCCAGGAGACGGGGAGCCTGGACAAAGTGGTGTCCTGGGCCCACCAGTTCCCGTATGCC
CACCCACTCTGGTTCGGACAGTTCATTGGCTTCCTGAACATCTATGAGCCTGACTATGCC
AAAGCTGTGTACAGCCGTGGGGACCCTAAGGCCCCTGATGTGTATGACTTCTTCCTCCAG
TGGATTGGGAGAGGCCTGCTGGTTCTTGAGGGGCCCAAGTGGTTGCAGCACCGCAAGCTG
CTCACACCTGGCTTTCATTATGATGTGCTGAAGCCCTATGTGGCCGTGTTCACTGAGTCT
ACACGTATCATGCTGGACAAGTGGGAAGAGAAAGCTCGGGAGGGTAAGTCCTTTGACATC
TTCTGCGATGTGGGTCACATGGCGCTGAACACACTCATGAAGTGCACCTTTGGAAGAGGA
GACACCGGCCTGGGCCACAGGGACAGCAGCTACTACCTTGCAGTCAGCGATCTCACTCTG
TTGATGCAGCAGCGCCTTGTGTCCTTCCAGTACCATAATGACTTCATCTACTGGCTCACC
CCACATGGCCGCCGCTTCCTGCGGGCCTGCCAGGTGGCCCATGACCATACAGACCAGGTC
ATCAGGGAGCGGAAGGCAGCCCTGCAGGATGAGAAGGTGCGGAAGAAGATCCAGAACCGG
AGGCACCTGGACTTCCTGGACATTCTCCTGGGTGCCCGGGATGAAGATGACATCAAACTG
TCAGATGCAGACCTCCGGGCTGAAGTGGACACATTCATGTTTGAAGGCCATGACACCACC
ACCAGTGGTATCTCCTGGTTTCTCTACTGCATGGCCCTGTACCCTGAGCACCAGCATCGT
TGTAGAGAGGAGGTCCGCGAGATCCTAGGGGACCAGGACTTCTTCCAGTGGGATGATCTG
GGCAAAATGACTTATCTGACCATGTGCATCAAGGAGAGCTTCCGCCTCTACCCACCTGTG
CCCCAGGTGTACCGCCAGCTCAGCAAGCCTGTCACCTTTGTGGATGGCCGGTCTCTACCT
GCAGGAAGCCTGATCTCTATGCATATCTATGCCCTCCATAGGAACAGTGCTGTATGGCCC
GACCCTGAGGTCTTTGACTCTCTGCGCTTTTCCACTGAGAATGCATCCAAACGCCATCCC
TTTGCCTTTATGCCCTTCTCTGCTGGGCCCAGGAACTGCATTGGGCAGCAGTTTGCCATG
AGTGAGATGAAGGTGGTCACAGCCATGTGCTTGCTCCGCTTTGAGTTCTCTCTGGACCCC
TCACGGCTGCCCATCAAGATGCCCCAGCTTGTCCTGCGCTCCAAGAATGGCTTTCACCTC
CACCTGAAGCCACTGGGCCCTGGGTCTGGGAAGTAG
|
| Enzyme 16 GenBank Gene ID |
J02871  |
| Enzyme 16 GeneCard ID |
CYP4B1  |
| Enzyme 16 GenAtlas ID |
CYP4B1  |
| Enzyme 16 HGNC ID |
HGNC:2644  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
1p34-p12 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Nhamburo PT, Gonzalez FJ, McBride OW, Gelboin HV, Kimura S: Identification of a new P450 expressed in human lung: complete cDNA sequence, cDNA-directed expression, and chromosome mapping. Biochemistry. 1989 Oct 3;28(20):8060-6. [PubMed
]
- Yokotani N, Sogawa K, Matsubara S, Gotoh O, Kusunose E, Kusunose M, Fujii-Kuriyama Y: cDNA cloning of cytochrome P-450 related to P-450p-2 from the cDNA library of human placenta. Gene structure and expression. Eur J Biochem. 1990 Jan 12;187(1):23-9. [PubMed
]
- Lo-Guidice JM, Allorge D, Cauffiez C, Chevalier D, Lafitte JJ, Lhermitte M, Broly F: Genetic polymorphism of the human cytochrome P450 CYP4B1: evidence for a non-functional allelic variant. Pharmacogenetics. 2002 Jul;12(5):367-74. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6855 |
| Enzyme 17 Name |
Cytochrome P450 4Z1 |
| Enzyme 17 Synonyms |
- CYPIVZ1
|
| Enzyme 17 Gene Name |
CYP4Z1 |
| Enzyme 17 Protein Sequence |
>Cytochrome P450 4Z1
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEF
YPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESW
VGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELF
QHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFS
SQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFS
EADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLS
QMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWED
PQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHS
RPPQPVRQVVLKSKNGIHVFAKKVC
|
| Enzyme 17 Number of Residues |
505 |
| Enzyme 17 Molecular Weight |
59087 |
| Enzyme 17 Theoretical pI |
9.63 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 17 Specific Function |
RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
29690384  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q86W10  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
CP4Z1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1518 bp
ATGGAGCCCTCCTGGCTTCAGGAACTCATGGCTCACCCCTTCTTGCTGCTGATCCTCCTC
TGCATGTCTCTGCTGCTGTTTCAGGTAATCAGGTTGTACCAGAGGAGGAGATGGATGATC
AGAGCCCTGCACCTGTTTCCTGCACCCCCTGCCCACTGGTTCTATGGCCACAAGGAGTTT
TACCCAGTAAAGGAGTTTGAGGTGTATCATAAGCTGATGGAAAAATACCCATGTGCTGTT
CCCTTGTGGGTTGGACCCTTTACGATGTTCTTCAGTGTCCATGACCCAGACTATGCCAAG
ATTCTCCTGAAAAGACAAGATCCCAAAAGTGCTGTTAGCCACAAAATCCTTGAATCCTGG
GTTGGTCGAGGACTTGTGACCCTGGATGGTTCTAAATGGAAAAAGCACCGCCAGATTGTG
AAACCTGGCTTCAACATCAGCATTCTGAAAATATTCATCACCATGATGTCTGAGAGTGTT
CGGATGATGCTGAACAAATGGGAGGAACACATTGCCCAAAACTCACGTCTGGAGCTCTTT
CAACATGTCTCCCTGATGACCCTGGACAGCATCATGAAGTGTGCCTTCAGCCACCAGGGC
AGCATCCAGTTGGACAGTACCCTGGACTCATACCTGAAAGCAGTGTTCAACCTTAGCAAA
ATCTCCAACCAGCGCATGAACAATTTTCTACATCACAACGACCTGGTTTTCAAATTCAGC
TCTCAAGGCCAAATCTTTTCTAAATTTAACCAAGAACTTCATCAGTTCACAGAGAAAGTA
ATCCAGGACCGGAAGGAGTCTCTTAAGGATAAGCTAAAACAAGATACTACTCAGAAAAGG
CGCTGGGATTTTCTGGACATACTTTTGAGTGCCAAAAGCGAAAACACCAAAGATTTCTCT
GAAGCAGATCTCCAGGCTGAAGTGAAAACGTTCATGTTTGCAGGACATGACACCACATCC
AGTGCTATCTCCTGGATCCTTTACTGCTTGGCAAAGTACCCTGAGCATCAGCAGAGATGC
CGAGATGAAATCAGGGAACTCCTAGGGGATGGGTCTTCTATTACCTGGGAACACCTGAGC
CAGATGCCTTACACCACGATGTGCATCAAGGAATGCCTCCGCCTCTACGCACCGGTAGTA
AACATATCCCGGTTACTCGACAAACCCATCACCTTTCCAGATGGACGCTCCTTACCTGCA
GGAATAACTGTGTTTATCAATATTTGGGCTCTTCACCACAACCCCTATTTCTGGGAAGAC
CCTCAGGTCTTTAACCCCTTGAGATTCTCCAGGGAAAATTCTGAAAAAATACATCCCTAT
GCCTTCATACCATTCTCAGCTGGATTAAGGAACTGCATTGGGCAGCATTTTGCCATAATT
GAGTGTAAAGTGGCAGTGGCATTAACTCTGCTCCGCTTCAAGCTGGCTCCAGACCACTCA
AGGCCTCCCCAGCCTGTTCGTCAAGTTGTCCTCAAGTCCAAGAATGGAATCCATGTGTTT
GCAAAAAAAGTTTGCTAA
|
| Enzyme 17 GenBank Gene ID |
AY262056  |
| Enzyme 17 GeneCard ID |
CYP4Z1  |
| Enzyme 17 GenAtlas ID |
CYP4Z1  |
| Enzyme 17 HGNC ID |
HGNC:20583  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1p33 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6856 |
| Enzyme 18 Name |
Cytochrome P450 1A2 |
| Enzyme 18 Synonyms |
- CYPIA2
- P450-P3
- P(3450
- P450 4
|
| Enzyme 18 Gene Name |
CYP1A2 |
| Enzyme 18 Protein Sequence |
>Cytochrome P450 1A2
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
|
| Enzyme 18 Number of Residues |
515 |
| Enzyme 18 Molecular Weight |
58295 |
| Enzyme 18 Theoretical pI |
9.43 |
| Enzyme 18 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 18 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
30339  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P05177  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
CP1A2_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1548 bp
ATGGCATTGTCCCAGTCTGTTCCCTTCTCGGCCACAGAGCTTCTCCTGGCCTCTGCCATC
TTCTGCCTGGTATTCTGGGTGCTCAAGGGTTTGAGGCCTCGGGTCCCCAAAGGCCTGAAA
AGTCCACCAGAGCCATGGGGCTGGCCCTTGCTCGGGCATGTGCTGACCCTGGGGAAGAAC
CCGCACCTGGCACTGTCAAGGATGAGCCAGCGCTACGGGGACGTCCTGCAGATCCGCATT
GGCTCCACGCCCGTGCTGGTGCTGAGCCGCCTGGACACCATCCGGCAGGCCCTGGTGCGG
CAGGGCGACGATTTCAAGGGCCGGCCTGACCTCTACACCTCCACCCTCATCACTGATGGC
CAGAGCTTGACCTTCAGCACAGACTCTGGACCGGTGTGGGCTGCCCGCCGGCGCCTGGCC
CAGAATGCCCTCAACACCTTCTCCATCGCCTCTGACCCAGCTTCCTCATCCTCCTGCTAC
CTGGAGGAGCATGTGAGCAAGGAGGCTAAGGCCCTGATCAGCAGGTTGCAGGAGCTGATG
GCAGGGCCTGGGCACTTCGACCCTTACAATCAGGTGGTGGTGTCAGTGGCCAACGTCATT
GGTGCCATGTGCTTCGGACAGCACTTCCCTGAGAGTAGCGATGAGATGCTCAGCCTCGTG
AAGAACACTCATGAGTTCGTGGAGACTGCCTCCTCCGGGAACCCCCTGGACTTCTTCCCC
ATCCTTCGCTACCTGCCTAACCCTGCCCTGCAGAGGTTCAAGGCCTTCAACCAGAGGTTC
CTGTGGTTCCTGCAGAAAACAGTCCAGGAGCACTATCAGGACTTTGACAAGAACAGTGTC
CGGGACATCACGGGTGCCCTGTTCAAGCACAGCAAGAAGGGGCCTAGAGCCAGCGGCAAC
CTCATCCCACAGGAGAAGATTGTCAACCTTGTCAATGACATCTTTGGAGCAGGATTTGAC
ACAGTCACCACAGCCATCTCCTGGAGCCTCATGTACCTTGTGACCAAGCCTGAGATACAG
AGGAAGATCCAGAAGGAGCTGGACACTGTGATTGGCAGGGAGCGGCGGCCCCGGCTCTCT
GACAGACCCCAGCTGCCCTACTTGGAGGCCTTCATCCTGGAGACCTTCCGACACTCCTCC
TTCTTGCCCTTCACCATCCCCCACAGCACAACAAGGGACACAACGCTGAATGGCTTCTAC
ATCCCCAAGAAATGCTGTGTCTTCGTAAACCAGTGGCAGGTCAACCATGACCCAGAGCTG
TGGGAGGACCCCTCTGAGTTCCGGCCTGAGCGGTTCCTCACCGCCGATGGCACTGCCATT
AACAAGCCCTTGAGTGAGAAGATGATGCTGTTTGGCATGGGCAAGCGCCGGTGTATCGGG
GAAGTCCTGGCCAAGTGGGAGATCTTCCTCTTCCTGGCCATCCTGCTACAGCAACTGGAG
TTCAGCGTGCCGCCGGGCGTGAAAGTCGACCTGACCCCCATCTACGGGCTGACCATGAAG
CACGCCCGCTGTGAACATGTCCAGGCGCGGCGCTTCTCCATCAATTGA
|
| Enzyme 18 GenBank Gene ID |
Z00036  |
| Enzyme 18 GeneCard ID |
CYP1A2  |
| Enzyme 18 GenAtlas ID |
CYP1A2  |
| Enzyme 18 HGNC ID |
HGNC:2596  |
| Enzyme 18 Chromosome Location |
15 |
| Enzyme 18 Locus |
15q24 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Jaiswal AK, Nebert DW, Gonzalez FJ: Human P3(450): cDNA and complete amino acid sequence. Nucleic Acids Res. 1986 Aug 26;14(16):6773-4. [PubMed
]
- Quattrochi LC, Pendurthi UR, Okino ST, Potenza C, Tukey RH: Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6731-5. [PubMed
]
- Ikeya K, Jaiswal AK, Owens RA, Jones JE, Nebert DW, Kimura S: Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Mol Endocrinol. 1989 Sep;3(9):1399-408. [PubMed
]
- Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ: Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. J Exp Pathol. 1987 Winter;3(1):1-17. [PubMed
]
- Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed
]
- Wrighton SA, Campanile C, Thomas PE, Maines SL, Watkins PB, Parker G, Mendez-Picon G, Haniu M, Shively JE, Levin W, et al.: Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. Mol Pharmacol. 1986 Apr;29(4):405-10. [PubMed
]
- Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed
]
- Huang JD, Guo WC, Lai MD, Guo YL, Lambert GH: Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese. Drug Metab Dispos. 1999 Jan;27(1):98-101. [PubMed
]
- Chevalier D, Cauffiez C, Allorge D, Lo-Guidice JM, Lhermitte M, Lafitte JJ, Broly F: Five novel natural allelic variants-951A>C, 1042G>A (D348N), 1156A>T (I386F), 1217G>A (C406Y) and 1291C>T (C431Y)-of the human CYP1A2 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355-6. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6857 |
| Enzyme 19 Name |
Cytochrome P450 19A1 |
| Enzyme 19 Synonyms |
- Aromatase
- CYPXIX
- Estrogen synthetase
- P-450AROM
|
| Enzyme 19 Gene Name |
CYP19A1 |
| Enzyme 19 Protein Sequence |
>Cytochrome P450 19A1
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI
SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL
GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN
ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL
YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI
LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI
YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK
NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH
PDETKNMLEMIFTPRNSDRCLEH
|
| Enzyme 19 Number of Residues |
503 |
| Enzyme 19 Molecular Weight |
57884 |
| Enzyme 19 Theoretical pI |
7.56 |
| Enzyme 19 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 19 Specific Function |
Catalyzes the formation of aromatic C18 estrogens from C19 androgens |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
179002  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
P11511  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
CP19A_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1512 bp
ATGGTTTTGGAAATGCTGAACCCGATACATTATAACATCACCAGCATCGTGCCTGAAGCC
ATGCCTGCTGCCACCATGCCAGTCCTGCTCCTCACTGGCCTTTTTCTCTTGGTGTGGAAT
TATGAGGGCACATCCTCAATACCAGGTCCTGGCTACTGCATGGGAATTGGACCCCTCATC
TCCCACGGCAGATTCCTGTGGATGGGGATCGGCAGTGCCTGCAACTACTACAACCGGGTA
TATGGAGAATTCATGCGAGTCTGGATCTCTGGAGAGGAAACACTCATTATCAGCAAGTCC
TCAAGTATGTTCCACATAATGAAGCACAATCATTACAGCTCTCGATTCGGCAGCAAACTT
GGGCTGCAGTGCATCGGTATGCATGAGAAAGGCATCATATTTAACAACAATCCAGAGCTC
TGGAAAACAACTCGACCCTTCTTTATGAAAGCTCTGTCAGGCCCCGGCCTTGTTCGTATG
GTCACAGTCTGTGCTGAATCCCTCAAAACACATCTGGACAGGTTGGAGGAGGTGACCAAT
GAATCGGGCTATGTGGACGTGTTGACCCTTCTGCGTCGTGTCATGCTGGACACCTCTAAC
ACGCTCTTCTTGAGGATCCCTTTGGACGAAAGTGCTATCGTGGTTAAAATCCAAGGTTAT
TTTGATGCATGGCAAGCTCTCCTCATCAAACCAGACATCTTCTTTAAGATTTCTTGGCTA
TACAAAAAGTATGAGAAGTCTGTCAAGGATTTGAAAGATGCCATAGAAGTTCTGATAGCA
GAAAAAAGACGCAGGATTTCCACAGAAGAGAAACTGGAAGAATGTATGGACTTTGCCACT
GAGTTGATTTTAGCAGAGAAACGTGGTGACCTGACAAGAGAGAATGTGAACCAGTGCATA
TTGGAAATGCTGATCGCAGCTCCTGACACCATGTCTGTCTCTTTGTTCTTCATGCTATTT
CTCATTGCAAAGCACCCTAATGTTGAAGAGGCAATAATAAAGGAAATCCAGACTGTTATT
GGTGAGAGAGACATAAAGATTGATGATATACAAAAATTAAAAGTGATGGAAAACTTCATT
TATGAGAGCATGCGGTACCAGCCTGTCGTGGACTTGGTCATGCGCAAAGCCTTAGAAGAT
GATGTAATCGATGGCTACCCAGTGAAAAAGGGGACAAACATTATCCTGAATATTGGAAGG
ATGCACAGACTCGAGTTTTTCCCCAAACCCAATGAATTTACTCTTGAAAATTTTGCAAAG
AATGTTCCTTATAGGTACTTTCAGCCATTTGGCTTTGGGCCCCGTGGCTGTGCAGGAAAG
TACATCGCCATGGTGATGATGAAAGCCATCCTCGTTACACTTCTGAGACGATTCCACGTG
AAGACATTGCAAGGACAGTGTGTTGAGAGCATACAGAAGATACACGACTTGTCCTTGCAC
CCAGATGAGACTAAAAACATGCTGGAAATGATCTTTACCCCAAGAAGCTCAGACAGGTGT
CTGGAACACTAG
|
| Enzyme 19 GenBank Gene ID |
M22246  |
| Enzyme 19 GeneCard ID |
CYP19A1  |
| Enzyme 19 GenAtlas ID |
CYP19A1  |
| Enzyme 19 HGNC ID |
HGNC:2594  |
| Enzyme 19 Chromosome Location |
15 |
| Enzyme 19 Locus |
15q21.1 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Harada N: Cloning of a complete cDNA encoding human aromatase: immunochemical identification and sequence analysis. Biochem Biophys Res Commun. 1988 Oct 31;156(2):725-32. [PubMed
]
- Chen SA, Besman MJ, Sparkes RS, Zollman S, Klisak I, Mohandas T, Hall PF, Shively JE: Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15. DNA. 1988 Jan-Feb;7(1):27-38. [PubMed
]
- Corbin CJ, Graham-Lorence S, McPhaul M, Mason JI, Mendelson CR, Simpson ER: Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8948-52. [PubMed
]
- Toda K, Terashima M, Mitsuuchi Y, Yamasaki Y, Yokoyama Y, Nojima S, Ushiro H, Maeda T, Yamamoto Y, Sagara Y, et al.: Alternative usage of different poly(A) addition signals for two major species of mRNA encoding human aromatase P-450. FEBS Lett. 1989 Apr 24;247(2):371-6. [PubMed
]
- Means GD, Mahendroo MS, Corbin CJ, Mathis JM, Powell FE, Mendelson CR, Simpson ER: Structural analysis of the gene encoding human aromatase cytochrome P-450, the enzyme responsible for estrogen biosynthesis. J Biol Chem. 1989 Nov 15;264(32):19385-91. [PubMed
]
- Pompon D, Liu RY, Besman MJ, Wang PL, Shively JE, Chen S: Expression of human placental aromatase in Saccharomyces cerevisiae. Mol Endocrinol. 1989 Sep;3(9):1477-87. [PubMed
]
- Harada N, Ogawa H, Shozu M, Yamada K, Suhara K, Nishida E, Takagi Y: Biochemical and molecular genetic analyses on placental aromatase (P-450AROM) deficiency. J Biol Chem. 1992 Mar 5;267(7):4781-5. [PubMed
]
- Evans CT, Ledesma DB, Schulz TZ, Simpson ER, Mendelson CR: Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6387-91. [PubMed
]
- Simpson ER, Evans CT, Corbin CJ, Powell FE, Ledesma DB, Mendelson CR: Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-450AROM). Mol Cell Endocrinol. 1987 Aug;52(3):267-72. [PubMed
]
- Mahendroo MS, Means GD, Mendelson CR, Simpson ER: Tissue-specific expression of human P-450AROM. The promoter responsible for expression in adipose tissue is different from that utilized in placenta. J Biol Chem. 1991 Jun 15;266(17):11276-81. [PubMed
]
- Mahendroo MS, Mendelson CR, Simpson ER: Tissue-specific and hormonally controlled alternative promoters regulate aromatase cytochrome P450 gene expression in human adipose tissue. J Biol Chem. 1993 Sep 15;268(26):19463-70. [PubMed
]
- Chen S, Shively JE, Nakajin S, Shinoda M, Hall PF: Amino terminal sequence analysis of human placenta aromatase. Biochem Biophys Res Commun. 1986 Mar 28;135(3):713-9. [PubMed
]
- Honda S, Harada N, Takagi Y: Novel exon 1 of the aromatase gene specific for aromatase transcripts in human brain. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1153-60. [PubMed
]
- Ito Y, Fisher CR, Conte FA, Grumbach MM, Simpson ER: Molecular basis of aromatase deficiency in an adult female with sexual infantilism and polycystic ovaries. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11673-7. [PubMed
]
- Morishima A, Grumbach MM, Simpson ER, Fisher C, Qin K: Aromatase deficiency in male and female siblings caused by a novel mutation and the physiological role of estrogens. J Clin Endocrinol Metab. 1995 Dec;80(12):3689-98. [PubMed
]
- Carani C, Qin K, Simoni M, Faustini-Fustini M, Serpente S, Boyd J, Korach KS, Simpson ER: Effect of testosterone and estradiol in a man with aromatase deficiency. N Engl J Med. 1997 Jul 10;337(2):91-5. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6858 |
| Enzyme 20 Name |
Cytochrome P450 2C8 |
| Enzyme 20 Synonyms |
- CYPIIC8
- P450 form 1
- P450 MP- 12/MP-20
- P450 IIC2
- S-mephenytoin 4-hydroxylase
|
| Enzyme 20 Gene Name |
CYP2C8 |
| Enzyme 20 Protein Sequence |
>Cytochrome P450 2C8
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
|
| Enzyme 20 Number of Residues |
490 |
| Enzyme 20 Molecular Weight |
55825 |
| Enzyme 20 Theoretical pI |
8.62 |
| Enzyme 20 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 20 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol) |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
181326  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P10632  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
CP2C8_HUMAN  |
| Enzyme 20 PDB ID |
1PQ2  |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1473 bp
ATGGAACCTTTTGTGGTCCTGGTGCTGTGTCTCTCTTTTATGCTTCTCTTTTCACTCTGG
AGACAGAGCTGTAGGAGAAGGAAGCTCCCTCCTGGCCCCACTCCTCTTCCTATTATTGGA
AATATGCTACAGATAGATGTTAAGGACATCTGCAAATCTTTCACCAATTTCTCAAAAGTC
TATGGTCCTGTGTTCACCGTGTATTTTGGCATGAATCCCATAGTGGTGTTTCATGGATAT
GAGGCAGTGAAGGAAGCCCTGATTGATAATGGAGAGGAGTTTTCTGGAAGAGGCAATTCC
CCAATATCTCAAAGAATTACTAAAGGACTTGGAATCATTTCCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCACAAACTTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCTCACTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
GTTGTTTTCCAGAAACGATTTGATTATAAAGATCAGAATTTTCTCACCCTGATGAAAAGA
TTCAATGAAAACTTCAGGATTCTGAACTCCCCATGGATCCAGGTCTGCAATAATTTCCCT
CTACTCATTGATTGTTTCCCAGGAACTCACAACAAAGTGCTTAAAAATGTTGCTCTTACA
CGAAGTTACATTAGGGAGAAAGTAAAAGAACACCAAGCATCACTGGATGTTAACAATCCT
CGGGACTTTATGGATTGCTTCCTGATCAAAATGGAGCAGGAAAAGGACAACCAAAAGTCA
GAATTCAATATTGAAAACTTGGTTGGCACTGTAGCTGATCTATTTGTTGCTGGAACAGAG
ACAACAAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGATCATGTAATTGGCAGACACAGGAGCCCCTGCATGCAG
GATAGGAGCCACATGCCTTACACTGATGCTGTAGTGCACGAGATCCAGAGATACAGTGAC
CTTGTCCCCACCGGTGTGCCCCATGCAGTGACCACTGATACTAAGTTCAGAAACTACCTC
ATCCCCAAGGGCACAACCATAATGGCATTACTGACTTCCGTGCTACATGATGACAAAGAA
TTTCCTAATCCAAATATCTTTGACCCTGGCCACTTTCTAGATAAGAATGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGAATTTGTGCAGGAGAAGGACTT
GCCCGCATGGAGCTATTTTTATTTCTAACCACAATTTTACAGAACTTTAACCTGAAATCT
GTTGATGATTTAAAGAACCTCAATACTACTGCAGTTACCAAAGGGATTGTTTCTCTGCCA
CCCTCATACCAGATCTGCTTCATCCCTGTCTGA
|
| Enzyme 20 GenBank Gene ID |
M17397  |
| Enzyme 20 GeneCard ID |
CYP2C8  |
| Enzyme 20 GenAtlas ID |
CYP2C8  |
| Enzyme 20 HGNC ID |
HGNC:2622  |
| Enzyme 20 Chromosome Location |
10 |
| Enzyme 20 Locus |
10q23.33 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Okino ST, Quattrochi LC, Pendurthi UR, McBride OW, Tukey RH: Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing. J Biol Chem. 1987 Nov 25;262(33):16072-9. [PubMed
]
- Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed
]
- Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed
]
- Ged C, Beaune P: Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid responsive elements in the 5' region. Biochim Biophys Acta. 1991 Mar 26;1088(3):433-5. [PubMed
]
- Zeldin DC, DuBois RN, Falck JR, Capdevila JH: Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform. Arch Biochem Biophys. 1995 Sep 10;322(1):76-86. [PubMed
]
- Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed
]
- Shephard EA, Phillips IR, Santisteban I, Palmer CN, Povey S: Cloning, expression and chromosomal localization of a member of the human cytochrome P450IIC gene sub-family. Ann Hum Genet. 1989 Jan;53(Pt 1):23-31. [PubMed
]
- Kolyada AY: Sequence of a human liver cytochrome P-450 cDNA clone. Nucleic Acids Res. 1990 Sep 25;18(18):5550. [PubMed
]
- Dai D, Zeldin DC, Blaisdell JA, Chanas B, Coulter SJ, Ghanayem BI, Goldstein JA: Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid. Pharmacogenetics. 2001 Oct;11(7):597-607. [PubMed
]
- Bahadur N, Leathart JB, Mutch E, Steimel-Crespi D, Dunn SA, Gilissen R, Houdt JV, Hendrickx J, Mannens G, Bohets H, Williams FM, Armstrong M, Crespi CL, Daly AK: CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel 6alpha-hydroxylase activity in human liver microsomes. Biochem Pharmacol. 2002 Dec 1;64(11):1579-89. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6859 |
| Enzyme 21 Name |
Cytochrome P450 2S1 |
| Enzyme 21 Synonyms |
- CYPIIS1
|
| Enzyme 21 Gene Name |
CYP2S1 |
| Enzyme 21 Protein Sequence |
>Cytochrome P450 2S1
MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRL
SKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN
GERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSN
VVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH
VSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLL
FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA
QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA
DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSG
LFNIPPAFQLQVRPTDLHSTTQTR
|
| Enzyme 21 Number of Residues |
504 |
| Enzyme 21 Molecular Weight |
55818 |
| Enzyme 21 Theoretical pI |
8.84 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 21 Specific Function |
Has a potential importance for extrahepatic xenobiotic metabolism |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
13161184  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q96SQ9  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
CP2S1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1515 bp
ATGGAGGCGACCGGCACCTGGGCGCTGCTGCTGGCGCTGGCGCTGCTCCTGCTGCTGACG
CTGGCGCTGTCCGGGACCAGGGCCCGAGGCCACCTGCCCCCCGGGCCCACGCCGCTACCA
CTGCTGGGAAACCTCCTGCAGCTACGGCCCGGGGCGCTGTATTCAGGGCTCATGCGGCTG
AGTAAGAAGTACGGACCGGTGTTCACCATCTACCTGGGACCCTGGCGGCCTGTGGTGGTC
CTGGTTGGGCAGGAGGCTGTGCGGGAGGCCCTGGGAGGTCAGGCTGAGGAGTTCAGCGGC
CGGGGAACCGTAGCGATGCTGGAAGGGACTTTTGATGGCCATGGGGTTTTCTTCTCCAAC
GGGGAGCGGTGGAGGCAGCTGAGGAAGTTTACCATGCTTGCTCTGCGGGACCTGGGCATG
GGGAAGCGAGAAGGCGAGGAGCTGATCCAGGCGGAGGCCCGGTGTCTGGTGGAGACATTC
CAGGGGACAGAAGGACGCCCATTCGATCCCTCCCTGCTGCTGGCCCAGGCCACCTCCAAC
GTAGTCTGCTCCCTCCTCTTTGGCCTCCGCTTCTCCTATGAGGATAAGGAGTTCCAGGCC
GTGGTCCGGGCAGCTGGTGGTACCCTGCTGGGAGTCAGCTCCCAGGGGGGTCAGACCTAC
GAGATGTTCTCCTGGTTCCTGCGGCCCCTGCCAGGCCCCCACAAGCAGCTCCTCCACCAC
GTCAGCACCTTGGCTGCCTTCACAGTCCGGCAGGTGCAGCAGCACCAGGGGAACCTGGAT
GCTTCGGGCCCCGCACGTGACCTTGTCGATGCCTTCCTGCTGAAGATGGCACAGGAGGAA
CAAAACCCAGGCACAGAATTCACCAACAAGAACATGCTGATGACAGTCATTTATTTGCTG
TTTGCTGGGACGATGACGGTCAGCACCACGGTCGGCTATACCCTCCTGCTCCTGATGAAA
TACCCTCATGTCCAAAAGTGGGTACGTGAGGAGCTGAATCGGGAGCTGGGGGCTGGCCAG
GCACCAAGCCTAGGGGACCGTACCCGCCTCCCTTACACCGACGCGGTTCTGCATGAGGCG
CAGCGGCTGCTGGCGCTGGTGCCCATGGGAATACCCCGCACCCTCATGCGGACCACCCGC
TTCCGAGGGTACACCCTGCCCCAGGGCACGGAGGTCTTCCCCCTCCTTGGCTCCATCCTG
CATGACCCCAACATCTTCAAGCACCCAGAAGAGTTCAACCCAGACCGTTTCCTGGATGCA
GATGGACGGTTCAGGAAGCATGAGGCGTTCCTGCCCTTCTCCTTAGGGAAGCGTGTCTGC
CTTGGAGAGGGCCTGGCAAAAGCGGAGCTCTTCCTCTTCTTCACCACCATCCTACAAGCC
TTCTCCCTGGAGAGCCCGTGCCCGCCGGACACCCTGAGCCTCAAGCCCACCGTCAGTGGC
CTTTTCAACATTCCCCCAGCCTTCCAGCTGCAAGTCCGTCCCACTGACCTTCACTCCACC
ACGCAGACCAGATGA
|
| Enzyme 21 GenBank Gene ID |
AF335278  |
| Enzyme 21 GeneCard ID |
CYP2S1  |
| Enzyme 21 GenAtlas ID |
CYP2S1  |
| Enzyme 21 HGNC ID |
HGNC:15654  |
| Enzyme 21 Chromosome Location |
19 |
| Enzyme 21 Locus |
19q13.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6861 |
| Enzyme 22 Name |
Cytochrome P450 2J2 |
| Enzyme 22 Synonyms |
- CYPIIJ2
- Arachidonic acid epoxygenase
|
| Enzyme 22 Gene Name |
CYP2J2 |
| Enzyme 22 Protein Sequence |
>Cytochrome P450 2J2
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVD
FEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHI
FKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDP
HFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFL
PGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEEN
LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMP
YTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDT
FNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLS
LKFRMGITISPVSHRLCAVPQV
|
| Enzyme 22 Number of Residues |
502 |
| Enzyme 22 Molecular Weight |
57611 |
| Enzyme 22 Theoretical pI |
8.87 |
| Enzyme 22 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 22 Specific Function |
This enzyme metabolizes arachidonic acid predominantly via a NADPH-dependent olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
18254513  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P51589  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
CP2J2_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1509 bp
ATGCTCGCGGCGATGGGCTCTCTGGCGGCTGCCCTCTGGGCAGTGGTCCATCCTCGGACT
CTCCTACTGGGCACTGTCGCCTTTCTGCTCGCTGCTGACTTTCTCAAAAGACGGCGCCCA
AAGAACTACCCGCCGGGGCCCTGGCGCCTGCCCTTCCTTGGCAACTTCTTCCTTGTGGAC
TTCGAGCAGTCGCACCTGGAGGTTCAGCTGTTTGTGAAGAAATATGGGAACCTTTTTAGC
TTGGAGCTTGGTGACATATCTGCAGTTCTTATTACTGGCTTGCCCTTAATCAAAGAAGCC
CTTATCCACATGGACCAAAACTTTGGGAACCGCCCCGTGACCCCTATGCGAGAACATATC
TTTAAGAAAAATGGATTGATTATGTCAAGTGGCCAGGCATGGAAGGAGCAAAGAAGGTTC
ACTCTGACAGCACTAAGGAACTTTGGTTTAGGAAAGAAGAGCTTAGAGGAACGCATTCAG
GAGGAGGCCCAACACCTCACTGAAGCAATAAAAGAGGAGAACGGACAGCCTTTTGACCCT
CATTTCAAGATCAACAATGCAGTTTCCAATATCATTTGCTCCATCACCTTCGGAGAACGC
TTTGAGTACCAGGATAGTTGGTTTCAGCAGCTGCTGAAGTTACTAGATGAAGTCACATAC
TTGGAGGCTTCAAAGACATGCCAGCTCTACAATGTCTTTCCATGGATAATGAAATTCCTG
CCTGGACCCCACCAAACTCTCTTCAGCAACTGGAAAAAACTGAAATTGTTTGTTTCTCAT
ATGATTGACAAACACAGAAAGGATTGGAATCCTGCAGAAACAAGAGACTTTATTGATGCT
TACCTTAAAGAAATGTCAAAGCACACAGGCAATCCTACTTCAAGTTTCCATGAAGAAAAC
CTCATCTGCAGCACCCTGGACCTCTTCTTTGCCGGAACCGAGACAACTTCCACAACTCTG
CGATGGGCTCTGCTTTATATGGCCCTCTACCCAGAAATCCAAGAAAAAGTACAAGCTGAG
ATTGACAGAGTGATTGGCCAGGGGCAGCAGCCGAGCACAGCCGCCCGGGAGTCCATGCCC
TACACCAATGCTGTCATCCATGAGGTGCAGAGAATGGGCAACATCATCCCCCTGAACGTT
CCCAGGGAAGTGACAGTTGATACCACTTTGGCTGGGTACCACCTGCCCAAGGGTACCATG
ATCCTGACCAATTTGACGGCGCTGCACAGGGACCCCACAGAGTGGGCCACCCCTGACACA
TTCAATCCGGACCATTTTCTGGAGAATGGACAGTTTAAGAAAAGGGAAGCCTTTATGCCT
TTCTCAATAGGAAAGCGGGCATGCCTCGGAGAACAGTTGGCCAGGACTGAGCTGTTTATT
TTCTTCACTTCCCTTATGCAAAAATTTACCTTCAGGCCCCCAAACAATGAGAAGCTGAGC
CTGAAGTTTAGAATGGGTATCACCATTTCCCCAGTCAGTCACCGCCTCTGCGCTGTTCCT
CAGGTGTAA
|
| Enzyme 22 GenBank Gene ID |
U37143  |
| Enzyme 22 GeneCard ID |
CYP2J2  |
| Enzyme 22 GenAtlas ID |
CYP2J2  |
| Enzyme 22 HGNC ID |
HGNC:2634  |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
1p31.3-p31.2 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Wu S, Moomaw CR, Tomer KB, Falck JR, Zeldin DC: Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart. J Biol Chem. 1996 Feb 16;271(7):3460-8. [PubMed
]
- King LM, Ma J, Srettabunjong S, Graves J, Bradbury JA, Li L, Spiecker M, Liao JK, Mohrenweiser H, Zeldin DC: Cloning of CYP2J2 gene and identification of functional polymorphisms. Mol Pharmacol. 2002 Apr;61(4):840-52. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6862 |
| Enzyme 23 Name |
Cytochrome P450 2A7 |
| Enzyme 23 Synonyms |
- CYPIIA7
- P450-IIA4
|
| Enzyme 23 Gene Name |
CYP2A7 |
| Enzyme 23 Protein Sequence |
>Cytochrome P450 2A7
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMK
FSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSN
GERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSSHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKL
LQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFI
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSSKHVGF
ATIPRNYTMSFLPR
|
| Enzyme 23 Number of Residues |
494 |
| Enzyme 23 Molecular Weight |
56409 |
| Enzyme 23 Theoretical pI |
7.96 |
| Enzyme 23 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 23 Specific Function |
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
Not Available |
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
181270  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P20853  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
CP2A7_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGGCCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCTGTCTGGCAGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCACTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCACATATGTGACTCCATCATGAAG
TTCAGTGAGTGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCTGCGCTTTGCCATCGCCACCCTGAGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGTCGGGCTTCCTCATCGAGGCCATC
CGGAGCAGCCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGCTGAGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACAGGACTTCATCGACTCCTTTCTCATCCACATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAGAACCTGATGATGAGCACGTTGAACCTCTTCATT
GCAGGCACGGAGACCGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGACCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGAGTCAAAAAGGACACCAAGTTT
CGGGATTTTTTCCTCCCTAAGGGCACCGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGTTTCTTCTCCAACCCCCAGGACTTCAATCCCCAGCACTTCCTGGATGACAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCTCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
|
| Enzyme 23 GenBank Gene ID |
M33317  |
| Enzyme 23 GeneCard ID |
CYP2A7  |
| Enzyme 23 GenAtlas ID |
CYP2A7  |
| Enzyme 23 HGNC ID |
HGNC:2611  |
| Enzyme 23 Chromosome Location |
19 |
| Enzyme 23 Locus |
19q13.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Yamano S, Tatsuno J, Gonzalez FJ: The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry. 1990 Feb 6;29(5):1322-9. [PubMed
]
- Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6878 |
| Enzyme 24 Name |
Catalase |
| Enzyme 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
CAT |
| Enzyme 24 Protein Sequence |
>Catalase
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
|
| Enzyme 24 Number of Residues |
527 |
| Enzyme 24 Molecular Weight |
59757 |
| Enzyme 24 Theoretical pI |
7.41 |
| Enzyme 24 GO Classification |
| Function |
- antioxidant activity
- catalase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 24 General Function |
Inorganic ion transport and metabolism |
| Enzyme 24 Specific Function |
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
1228085  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P04040  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
CATA_HUMAN  |
| Enzyme 24 PDB ID |
1F4J  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>66 bp
ATGGCTGACAGCCGGGATCCCGCCAGCGACCAGATGCAGCACTGGAAGGAGCAGCGGGCC
GCGCAG
|
| Enzyme 24 GenBank Gene ID |
X04085  |
| Enzyme 24 GeneCard ID |
CAT  |
| Enzyme 24 GenAtlas ID |
CAT  |
| Enzyme 24 HGNC ID |
HGNC:1516  |
| Enzyme 24 Chromosome Location |
11 |
| Enzyme 24 Locus |
11p13 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Quan F, Korneluk RG, Tropak MB, Gravel RA: Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986 Jul 11;14(13):5321-35. [PubMed
]
- Bell GI, Najarian RC, Mullenbach GT, Hallewell RA: cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561-2. [PubMed
]
- Jin LH, Bahn JH, Eum WS, Kwon HY, Jang SH, Han KH, Kang TC, Won MH, Kang JH, Cho SW, Park J, Choi SY: Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic Biol Med. 2001 Dec 1;31(11):1509-19. [PubMed
]
- Yoo JH, Erzurum SC, Hay JG, Lemarchand P, Crystal RG: Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. J Clin Invest. 1994 Jan;93(1):297-302. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819-23. [PubMed
]
- Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ: Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. [PubMed
]
- Putnam CD, Arvai AS, Bourne Y, Tainer JA: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. [PubMed
]
- Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP: Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
13116 |
| Enzyme 25 Name |
Cytochrome P450, family 1, subfamily A, polypeptide 1 |
| Enzyme 25 Synonyms |
- Cytochrome P450, family 1, subfamily A, polypeptide 1, isoform CRA_a
|
| Enzyme 25 Gene Name |
CYP1A1 |
| Enzyme 25 Protein Sequence |
>Cytochrome P450, family 1, subfamily A, polypeptide 1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
|
| Enzyme 25 Number of Residues |
512 |
| Enzyme 25 Molecular Weight |
58166 |
| Enzyme 25 Theoretical pI |
8.47 |
| Enzyme 25 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
117606758  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
A0N0X8  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
A0N0X8_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
EF094025  |
| Enzyme 25 GeneCard ID |
A0N0X8  |
| Enzyme 25 GenAtlas ID |
Not Available |
| Enzyme 25 HGNC ID |
Not Available |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
14942 |
| Enzyme 26 Name |
JmjC domain-containing histone demethylation protein 1A |
| Enzyme 26 Synonyms |
- [Histone-H3]-lysine-36 demethylase 1A
- F-box/LRR-repeat protein 11
- F-box and leucine-rich repeat protein 11
- F-box protein FBL7
- F-box protein Lilina
- CXXC-type zinc finger protein 8
|
| Enzyme 26 Gene Name |
FBXL11 |
| Enzyme 26 Protein Sequence |
>JmjC domain-containing histone demethylation protein 1A
MEPEEERIRYSQRLRGTMRRRYEDDGISDDEIEGKRTFDLEEKLHTNKYNANFVTFMEGK
DFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNTQKGIE
MTMAQWTRYYETPEEEREKLYNVISLEFSHTRLENMVQRPSTVDFIDWVDNMWPRHLKES
QTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHN
LELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNFL
HSFNIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLERYVYCITNRSHLTKEFQKESLS
MDLELNGLESGNGDEEAVDREPRRLSSRRSVLTSPVANGVNLDYDGLGKTCRSLPSLKKT
LAGDSSSDCSRGSHNGQVWDPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPT
GIEDEDALIADVKILLEELANSDPKLALTGVPIVQWPKRDKLKFPTRPKVRVPTIPITKP
HTMKPAPRLTPVRPAAASPIVSGARRRRVRCRKCKACVQGECGVCHYCRDMKKFGGPGRM
KQSCVLRQCLAPRLPHSVTCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEG
LLNEELPNCWECPKCYQEDSSEKAQKRKMEESDEEAVQAKVLRPLRSCDEPLTPPPHSPT
SMLQLIHDPVSPRGMVTRSSPGAGPSDHHSASRDERFKRRQLLRLQATERTMVREKENNP
SGKKELSEVEKAKIRGSYLTVTLQRPTKELHGTSIVPKLQAITASSANLRHSPRVLVQHC
PARTPQRGDEEGLGGEEEEEEEEEEEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMS
VFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLS
WTNISKKQLTWLVNRLPGLKDLLLAGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIR
DLLTPPADKPGQDNRSKLRNMTDFRLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQ
SSNLLTAVGSSTRYSLTELNMAGCNKLTDQTLIYLRRIANVTLIDLRGCKQITRKACEHF
ISDLSINSLYCLSDEKLIQKIS
|
| Enzyme 26 Number of Residues |
1162 |
| Enzyme 26 Molecular Weight |
132794 |
| Enzyme 26 Theoretical pI |
7.61 |
| Enzyme 26 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
| — |
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Histone demethylase that specifically demethylates 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylted H3 'Lys- 36'. May also recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
20521722  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9Y2K7  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
JHD1A_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>3492 bp
GAGATGGAACCCGAAGAAGAAAGGATTCGTTACAGCCAGAGATTGCGTGGTACCATGCGA
CGACGCTATGAAGATGATGGCATTTCAGATGATGAAATTGAAGGAAAAAGAACTTTTGAC
TTGGAAGAGAAACTGCACACCAACAAATATAATGCCAATTTTGTTACTTTTATGGAAGGA
AAAGATTTTAATGTAGAGTATATTCAGCGGGGTGGCTTGAGAGATCCTCTGATTTTCAAG
AATTCTGATGGACTCGGAATAAAAATGCCGGATCCAGACTTCACTGTGAATGATGTCAAA
ATGTGTGTGGGGAGTCGTCGCATGGTGGATGTCATGGACGTGAACACACAGAAAGGCATT
GAAATGACCATGGCTCAGTGGACACGCTACTATGAGACCCCAGAGGAGGAGCGAGAGAAA
CTCTATAATGTCATCAGCCTCGAGTTTAGCCACACCAGGCTGGAGAATATGGTGCAGAGG
CCCTCCACGGTGGATTTCATTGACTGGGTAGACAACATGTGGCCAAGGCACTTGAAGGAA
AGCCAGACTGAATCAACAAATGCCATCTTGGAGATGCAGTACCCTAAAGTGCAGAAGTAC
TGTCTAATGAGTGTTCGAGGCTGCTATACTGACTTCCATGTGGACTTTGGTGGTACCTCT
GTTTGGTATCACATCCATCAAGGGGGAAAGGTCTTCTGGCTCATCCCCCCTACAGCCCAC
AACCTGGAGCTGTACGAGAATTGGCTGCTGTCAGGGAAACAGGGAGACATCTTTCTGGGT
GACCGGGTATCAGATTGTCAGCGCATTGAGCTCAAGCAGGGCTATACCTTCGTCATTCCC
TCAGGCTGGATTCATGCTGTGTATACTCCTACAGACACATTAGTGTTTGGGGGCAATTTT
TTGCATAGCTTCAACATCCCTATGCAGTTAAAAATATACAACATTGAAGATCGGACACGG
GTTCCAAATAAGTTTCGCTATCCATTCTACTATGAGATGTGTTGGTATGTGTTGGAGCGC
TATGTGTACTGCATAACCAACCGTTCCCACCTAACCAAGGAATTTCAGAAAGAGTCCCTC
AGCATGGATTTGGAGTTAAATGGGTTGGAGTCTGGGAATGGGGATGAGGAAGCAGTGGAT
CGAGAACCCCGACGCTTGAGCAGCAGGCGTTCTGTCCTCACTAGCCCTGTAGCGAATGGA
GTCAACCTGGATTATGATGGACTGGGCAAAACCTGCCGAAGTCTTCCAAGTCTGAAGAAA
ACTTTGGCTGGGGACTCATCTTCTGACTGTAGCCGGGGCTCCCACAATGGACAAGTGTGG
GATCCCCAGTGTGCTCCCCGAAAGGACAGGCAAGTGCATCTGACCCATTTTGAGCTTGAA
GGCCTTCGCTGCCTTGTAGATAAGTTGGAGTCTCTGCCACTGCACAAGAAATGTGTCCCC
ACAGGGATAGAAGATGAAGATGCTCTCATTGCTGATGTAAAGATTTTGCTGGAGGAGCTT
GCCAACAGCGATCCCAAGTTAGCCCTCACTGGAGTTCCTATAGTACAGTGGCCAAAAAGG
GATAAGCTTAAATTCCCCACTCGGCCAAAGGTGCGGGTTCCTACCATCCCCATTACGAAG
CCTCACACTATGAAACCAGCTCCACGGTTAACACCTGTGAGGCCAGCTGCTGCCTCCCCG
ATTGTGTCAGGAGCCAGACGGAGACGAGTGCGATGTCGAAAATGCAAAGCCTGTGTGCAA
GGAGAGTGTGGTGTTTGCCACTACTGCAGAGACATGAAGAAGTTTGGGGGGCCTGGACGC
ATGAAGCAGTCCTGTGTCCTCCGACAGTGCTTGGCACCCAGACTGCCTCACTCAGTCACA
TGTTCCCTCTGTGGAGAGGTGGATCAGAATGAAGAGACACAAGACTTTGAGAAGAAACTC
ATGGAATGCTGTATCTGCAATGAGATTGTTCATCCTGGCTGCCTCCAGATGGACGGAGAG
GGGTTGCTTAACGAAGAATTGCCAAATTGCTGGGAATGTCCAAAGTGCTACCAGGAGGAC
AGCTCGGAGAAAGCCCAGAAGCGGAAAATGGAAGAGAGTGACGAAGAAGCTGTGCAAGCC
AAAGTCCTGCGGCCCCTGCGGAGCTGCGATGAGCCTCTCACGCCCCCGCCTCATTCACCC
ACTTCCATGCTGCAGCTCATCCATGACCCGGTTTCCCCCCGGGGTATGGTGACTCGGTCA
TCCCCTGGGGCTGGCCCCAGCGACCACCACAGTGCCAGCCGCGATGAGCGCTTCAAACGG
CGGCAGTTGCTGCGGCTGCAGGCCACAGAGCGCACCATGGTACGGGAAAAGGAGAACAAT
CCCAGCGGCAAAAAGGAGCTGTCTGAAGTTGAGAAAGCCAAGATCCGGGGATCGTACCTC
ACTGTCACGCTACAGAGGCCCACCAAAGAGCTCCACGGGACATCCATTGTGCCCAAGCTG
CAGGCCATCACGGCCTCCTCTGCCAACCTTCGCCATTCCCCCCGTGTGCTAGTGCAGCAC
TGCCCAGCCCGAACCCCCCAGCGTGGGGATGAGGAGGGGCTGGGGGGAGAGGAGGAGGAA
GAGGAGGAGGAGGAGGAGGAAGATGACAGTGCAGAGGAGGGGGGTGCAGCCAGGCTGAAT
GGCCGGGGCAGTTGGGCTCAGGATGGAGACGAAAGCTGGATGCAGCGGGAGGTCTGGATG
TCTGTCTTCCGCTACCTCAGCCGCAGAGAACTTTGTGAATGTATGCGAGTGTGCAAGACG
TGGTATAAATGGTGCTGCGACAAGAGACTTTGGACAAAAATTGACTTGAGTAGGTGTAAG
GCCATTGTGCCCCAGGCCCTCAGTGGCATCATCAAGAGGCAGCCAGTCAGCCTTGACCTC
AGTTGGACCAACATCTCTAAAAAGCAACTGACATGGCTCGTCAATAGGCTGCCAGGACTG
AAAGACCTCCTCCTAGCAGGCTGCTCCTGGTCTGCAGTCTCTGCCCTCAGCACCTCCAGC
TGCCCCCTTCTCAGGACCCTTGATCTTCGGTGGGCAGTAGGAATCAAGGACCCTCAAATT
CGGGACTTGCTTACTCCACCGGCTGATAAACCAGGTCAGGACAATCGCAGCAAGCTCCGG
AACATGACCGACTTCCGGCTGGCAGGCCTTGACATCACAGATGCCACGCTTCGCCTCATA
ATTCGCCACATGCCCCTCCTGTCTCGACTCGACCTCAGTCACTGCAGCCACCTTACAGAT
CAGTCCTCCAATCTACTCACTGCTGTCGGGTCTTCCACTCGCTACTCTCTCACAGAGCTC
AATATGGCAGGTTGCAATAAATTGACAGACCAGACCCTGATCTACCTACGGCGCATTGCC
AACGTCACCTTGATCGACCTTCGAGGATGCAAGCAGATCACTCGAAAAGCCTGCGAGCAC
TTCATCTCAGACTTGTCCATCAACAGCCTCTACTGCCTGTCTGACGAGAAGCTGATACAG
AAGATCAGCTAA
|
| Enzyme 26 GenBank Gene ID |
AB023221  |
| Enzyme 26 GeneCard ID |
Q9Y2K7  |
| Enzyme 26 GenAtlas ID |
FBXL11  |
| Enzyme 26 HGNC ID |
HGNC:13606  |
| Enzyme 26 Chromosome Location |
11 |
| Enzyme 26 Locus |
11q13.1 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Ilyin GP, Rialland M, Pigeon C, Guguen-Guillouzo C: cDNA cloning and expression analysis of new members of the mammalian F-box protein family. Genomics. 2000 Jul 1;67(1):40-7. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Hattori A, Okumura K, Nagase T, Kikuno R, Hirosawa M, Ohara O: Characterization of long cDNA clones from human adult spleen. DNA Res. 2000 Dec 31;7(6):357-66. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
14943 |
| Enzyme 27 Name |
JmjC domain-containing histone demethylation protein 1B |
| Enzyme 27 Synonyms |
- [Histone-H3]-lysine-36 demethylase 1B
- F-box and leucine-rich repeat protein 10
- F-box/LRR-repeat protein 10
- F-box protein FBL10
- Jumonji domain-containing EMSY-interactor methyltransferase motif protein
- Protein JEMMA
- CXXC-type zinc finger protein 2
- Protein-containing CXXC domain 2
|
| Enzyme 27 Gene Name |
FBXL10 |
| Enzyme 27 Protein Sequence |
>JmjC domain-containing histone demethylation protein 1B
MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQRPIDRQRYDENEDLSDVE
EIVSVRGFSLEEKLRSQLYQGDFVHAMEGKDFNYEYVQREALRVPLIFREKDGLGIKMPD
PDFTVRDVKLLVGSRRLVDVMDVNTQKGTEMSMSQFVRYYETPEAQRDKLYNVISLEFSH
TKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNAIAEMKYPKVKKYCLMSVKGCFTD
FHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIEL
KQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIEDRTRVQPKFRYPFYY
EMCWYVLERYVYCVTQRSHLTQEYQRESMLIDAPRKPSIDGFSSDSWLEMEEEACDQQPQ
EEEEKDEEGEGRDRAPKPPTDGSTSPTSTPSEDQEALGKKPKAPALRFLKRTLSNESEES
VKSTTLAVDYPKTPTGSPATEVSAKWTHLTEFELKGLKALVEKLESLPENKKCVPEGIED
PQALLEGVKNVLKEHADDDPSLAITGVPVVTWPKKTPKNRAVGRPKGKLGPASAVKLAAN
RTTAGARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCIAPVLPHTA
VCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECP
KCNHAGKTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDE
HSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSS
LSPWWRSSLTYFQQQLKPGKEDKLFRKKRRSWKNAEDRMALANKPLRRFKQEPEDELPEA
PPKTRESDHSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLPNKELSRELSKELNHEIQR
TENSLANENQQPIKSEPESEGEEPKRPPGICERPHRFSKGLNGTPRELRHQLGPSLRSPP
RVISRPPPSVSPPKCIQMERHVIRPPPISPPPDSLPLDDGAAHVMHREVWMAVFSYLSHQ
DLCVCMRVCRTWNRWCCDKRLWTRIDLNHCKSITPLMLSGIIRRQPVSLDLSWTNISKKQ
LSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTD
NRPGQMDNRSKLRNIVELRLAGLDITDASLRLIIRHMPLLSKLHLSYCNHVTDQSINLLT
AVGTTTRDSLTEINLSDCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSV
SVQFGQVEEKLLQKLS
|
| Enzyme 27 Number of Residues |
1336 |
| Enzyme 27 Molecular Weight |
152616 |
| Enzyme 27 Theoretical pI |
8.68 |
| Enzyme 27 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Histone demethylase that specifically demethylates 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylted H3 'Lys- 36'. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
20451682  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q8NHM5  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
JHD1B_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>4011 bp
ATGGCGGGTCCGCAAATGGGGGGATCTGCAGAGGATCACCCCCCACGAAAAAGACATGCA
GCAGAAAAGCAAAAAAAGAAAACAGTTATATATACAAAATGCTTTGAATTTGAGTCGGCC
ACACAGCGCCCGATTGACCGCCAGCGATACGACGAGAACGAGGACTTGTCGGACGTGGAG
GAGATCGTCAGCGTCCGCGGCTTCAGCCTGGAGGAGAAGCTTCGCAGCCAGCTGTACCAG
GGGGACTTCGTGCACGCCATGGAGGGCAAAGATTTCAACTATGAGTACGTACAGAGAGAA
GCTCTCAGGGTTCCCCTGATATTTCGAGAAAAGGATGGACTGGGAATTAAGATGCCTGAC
CCTGATTTCACAGTCCGAGACGTCAAACTCCTAGTGGGGAGCCGGCGGCTTGTGGACGTG
ATGGATGTGAACACCCAGAAGGGCACGGAGATGAGCATGTCCCAGTTTGTGCGTTACTAC
GAGACGCCCGAGGCCCAGCGGGACAAGCTGTACAACGTCATCAGCCTAGAGTTCAGCCAC
ACCAAGCTGGAGCACTTGGTCAAGCGTCCGACTGTGGTAGACCTGGTGGACTGGGTGGAC
AACATGTGGCCCCAGCATCTGAAGGAGAAGCAGACAGAAGCCACGAACGCCATTGCAGAG
ATGAAGTACCCGAAAGTGAAAAAGTACTGTCTGATGAGCGTGAAAGGTTGTTTCACCGAC
TTCCACATCGACTTTGGAGGCACTTCCGTTTGGTACCATGTTTTCCGGGGTGGGAAGATT
TTTTGGCTGATTCCTCCAACGCTGCACAATTTGGCGCTGTACGAGGAGTGGGTGCTGTCA
GGCAAACAGAGTGACATCTTTCTGGGAGACCGTGTGGAACGATGCCAAAGAATTGAGCTG
AAGCAGGGCTACACATTTTTCATCCCTTCCGGTTGGATCCATGCCGTCTACACCCCTGTA
GACTCTTTGGTGTTCGGCGGAAACATCCTGCACAGCTTTAACGTGCCCATGCAGCTGCGG
ATCTACGAGATCGAGGACAGGACGCGGGTGCAGCCCAAATTCCGTTACCCCTTCTACTAT
GAGATGTGCTGGTATGTCCTGGAGAGATACGTGTACTGTGTGACCCAGCGCTCCCACCTC
ACTCAGGAATACCAGAGGGAGTCGATGCTTATTGATGCCCCGAGGAAGCCCAGCATAGAC
GGCTTCTCTTCGGATTCCTGGCTGGAGATGGAGGAGGAGGCCTGTGATCAGCAGCCTCAG
GAGGAGGAGGAGAAGGACGAGGAGGGCGAGGGCAGGGACAGGGCACCCAAACCGCCCACC
GATGGCTCCACTTCACCCACCAGCACGCCCTCTGAGGACCAGGAGGCCCTCGGGAAGAAG
CCCAAAGCACCTGCCCTGCGATTCCTCAAAAGGACTTTGTCTAATGAGTCGGAGGAAAGT
GTGAAGTCCACCACATTGGCCGTAGACTACCCCAAGACCCCCACCGGCTCTCCCGCCACG
GAGGTCTCTGCCAAATGGACCCATCTCACTGAGTTTGAACTGAAGGGCCTGAAAGCTCTG
GTGGAGAAACTGGAATCCCTCCCGGAGAACAAGAAGTGTGTCCCCGAGGGCATCGAGGAC
CCCCAGGCACTCCTGGAGGGTGTGAAGAACGTCCTGAAGGAGCACGCAGATGATGACCCT
AGTCTGGCCATCACTGGGGTCCCTGTGGTGACTTGGCCAAAGAAGACTCCAAAGAACCGG
GCTGTGGGTCGGCCCAAGGGGAAGCTGGGCCCGGCCTCCGCGGTGAAGTTGGCCGCCAAC
CGGACAACGGCAGGAGCTCGGCGGCGCCGGACGCGATGCCGCAAGTGCGAGGCCTGCCTG
CGGACCGAGTGCGGAGAGTGCCACTTCTGCAAGGACATGAAGAAGTTCGGGGGCCCCGGG
CGCATGAAGCAGAGCTGCATCATGCGGCAGTGCATCGCGCCAGTGCTGCCCCACACCGCC
GTGTGCCTTGTGTGTGGCGAGGCGGGGAAGGAAGACACGGTGGAAGAGGAGGAAGGCAAG
TTTAACCTCATGCTCATGGAGTGCTCCATCTGCAATGAAATCATCCACCCTGGATGCCTT
AAGATTAAGGAGTCAGAGGGTGTGGTCAACGACGAGCTTCCAAACTGCTGGGAGTGTCCG
AAGTGTAACCACGCCGGCAAGACCGGGAAGCAAAAGCGTGGCCCTGGCTTTAAGTACGCC
TCCAACCTGCCCGGCTCCCTGCTCAAGGAGCAGAAGATGAACCGGGACAACAAGGAAGGG
CAGGAACCTGCCAAGCGGAGGAGTGAGTGTGAGGAGGCGCCCCGGCGCAGGTCGGATGAG
CACTCGAAGAAGGTGCCGCCGGACGGCCTTCTGCGCAGAAAGTCTGACGACGTGCACCTG
AGGAAGAAGCGGAAATACGAGAAGCCCCAGGAGCTGAGTGGACGCAAGCGGGCCTCATCG
CTTCAAACGTCCCCCGGTTCCTCCTCTCACCTCTCGCCGAGGCCCCCTCTAGGCAGCAGC
CTCAGCCCCTGGTGGAGATCCAGTCTCACTTACTTCCAGCAGCAGCTCAAACCTGGCAAA
GAAGATAAGCTTTTCAGGAAAAAGCGGCGGTCCTGGAAGAACGCCGAGGACCGCATGGCG
CTGGCCAACAAGCCCCTCCGGCGCTTCAAGCAGGAACCCGAGGACGAACTGCCCGAGGCG
CCCCCCAAGACCAGGGAGAGCGACCACTCCCGCTCCAGCTCCCCCACCGCGGGACCCAGC
ACCGAAGGGGCCGAGGGCCCGGAGGAGAAGAAGAAGGTGAAGATGCGCCGGAAGCGGCGG
CTTCCCAACAAGGAGCTGAGCAGGGAGCTGAGCAAGGAGCTCAACCACGAGATCCAGAGG
ACGGAGAACAGCCTGGCCAACGAGAACCAGCAGCCCATCAAGTCGGAGCCTGAGAGCGAG
GGCGAGGAGCCCAAGCGGCCCCCGGGCATCTGCGAGCGTCCCCACCGCTTCAGCAAGGGG
CTCAACGGCACCCCCCGGGAGCTGCGGCACCAGCTGGGGCCCAGCCTGCGCAGCCCGCCC
CGTGTCATCTCCCGGCCCCCACCCTCCGTGTCCCCGCCCAAGTGTATCCAGATGGAGCGC
CATGTGATCCGGCCACCCCCCATCAGCCCCCCGCCTGACTCGCTACCCCTGGACGATGGG
GCAGCCCACGTCATGCACAGGGAGGTGTGGATGGCCGTCTTCAGCTACCTCAGCCACCAA
GACCTGTGTGTGTGCATGCGGGTCTGCAGGACCTGGAACCGCTGGTGCTGCGATAAGCGG
TTGTGGACCCGCATTGACCTGAACCACTGCAAGTCTATCACACCCCTGATGCTGAGTGGC
ATCATCCGGCGACAGCCCGTCTCCCTCGACCTCAGCTGGACCAATATCTCCAAGAAGCAG
CTGAGCTGGCTCATCAACCGGCTGCCTGGGCTCCGGGACTTGGTGCTGTCAGGCTGCTCA
TGGATCGCGGTCTCGGCCCTTTGCAGCTCCAGTTGTCCGCTGCTCCGGACCCTGGATGTC
CAGTGGGTGGAGGGACTAAAGGATGCCCAGATGCGGGATCTCCTGTCCCCGCCCACAGAC
AACAGGCCAGGTCAGATGGACAATCGGAGCAAGCTCCGGAACATCGTGGAGCTGCGCCTG
GCAGGCCTGGACATCACAGATGCCTCCCTGCGGCTCATCATCCGCCACATGCCCCTGCTC
TCCAAGCTCCACCTCAGTTACTGTAACCACGTCACCGACCAGTCTATCAACCTGCTCACT
GCTGTTGGCACCACCACCCGAGACTCCTTAACCGAGATCAACCTGTCTGACTGCAATAAG
GTCACTGATCAGTGCCTGTCCTTCTTCAAACGCTGTGGAAACATCTGTCATATTGACCTG
AGGTACTGCAAGCAAGTCACCAAGGAAGGCTGTGAGCAGTTCATAGCCGAGATGTCTGTG
AGTGTCCAGTTTGGGCAAGTAGAAGAAAAACTCCTGCAAAAACTGAGTTAG
|
| Enzyme 27 GenBank Gene ID |
AJ459424  |
| Enzyme 27 GeneCard ID |
Q8NHM5  |
| Enzyme 27 GenAtlas ID |
FBXL10  |
| Enzyme 27 HGNC ID |
HGNC:13610  |
| Enzyme 27 Chromosome Location |
12 |
| Enzyme 27 Locus |
12q24.31 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
15174 |
| Enzyme 28 Name |
Cytochrome P450, family 3, subfamily A, polypeptide 7 |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
CYP3A7 |
| Enzyme 28 Protein Sequence |
>Cytochrome P450, family 3, subfamily A, polypeptide 7
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
|
| Enzyme 28 Number of Residues |
503 |
| Enzyme 28 Molecular Weight |
57471 |
| Enzyme 28 Theoretical pI |
9.52 |
| Enzyme 28 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 28 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
Not Available |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
A4D288  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
A4D288_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
Not Available |
| Enzyme 28 GenBank Gene ID |
CH236956  |
| Enzyme 28 GeneCard ID |
A4D288  |
| Enzyme 28 GenAtlas ID |
Not Available |
| Enzyme 28 HGNC ID |
Not Available |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
15175 |
| Enzyme 29 Name |
Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6) |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
CYP2D6 |
| Enzyme 29 Protein Sequence |
>Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLCIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVTPSPYELCAVPR
|
| Enzyme 29 Number of Residues |
497 |
| Enzyme 29 Molecular Weight |
55731 |
| Enzyme 29 Theoretical pI |
7.09 |
| Enzyme 29 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
45768272  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q6NWU0  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
Q6NWU0_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1494 bp
ATGGGGCTAGAAGCACTGGTGCCCCTGGCCGTGATAGTGGCCATCTTCCTGCTCCTGGTG
GACCTGATGCACCGGCGCCAACGCTGGGCTGCACGCTACCCACCAGGCCCCCTGCCACTG
CCCGGGCTGGGCAACCTGCTGCATGTGGACTTCCAGAACACACCATACTGCTTCGACCAG
TTGCGGCGCCGCTTCGGGGACGTGTTCAGCCTGCAGCTGGCCTGGACGCCGGTGGTCGTG
CTCAATGGGCTGGCGGCCGTGCGCGAGGCGCTGGTGACCCACGGCGAGGACACCGCCGAC
CGCCCGCCTGTGCCCATCACCCAGATCCTGGGTTTCGGGCCGCGTTCCCAAGGGGTGTTC
CTGGCGCGCTATGGGCCCGCGTGGCGCGAGCAGAGGCGCTTCTCCGTCTCCACCTTGCGC
AACTTGGGCCTGGGCAAGAAGTCGCTGGAGCAGTGGGTGACCGAGGAGGCCGCCTGCCTT
TGTGCCGCCTTCGCCAACCACTCCGGACGCCCCTTTCGCCCCAACGGTCTCTTGGACAAA
GCCGTGAGCAACGTGATCGCCTCCCTCACCTGCGGGCGCCGCTTCGAGTACGACGACCCT
CGCTTCCTCAGGCTGCTGGACCTAGCTCAGGAGGGACTGAAGGAGGAGTCGGGCTTTCTG
CGCGAGGTGCTGAATGCTGTCCCCGTCCTCCTGCATATCCCAGCGCTGGCTGGCAAGGTC
CTACGCTTCCAAAAGGCTTTCCTGACCCAGCTGGATGAGCTGCTAACTGAGCACAGGATG
ACCTGGGACCCAGCCCAGCCCCCCCGAGACCTGACTGAGGCCTTCCTGGCAGAGATGGAG
AAGGCCAAGGGGAACCCTGAGAGCAGCTTCAATGATGAGAACCTGTGCATAGTGGTGGCT
GACCTGTTCTCTGCCGGGATGGTGACCACCTCGACCACGCTGGCCTGGGGCCTCCTGCTC
ATGATCCTACATCCGGATGTGCAGCGCCGTGTCCAACAGGAGATCGACGACGTGATAGGG
CAGGTGCGGCGACCAGAGATGGGTGACCAGGCTCACATGCCCTACACCACTGCCGTGATT
CATGAGGTGCAGCGCTTTGGGGACATCGTCCCCCTGGGTGTGACCCATATGACATCCCGT
GACATCGAAGTACAGGGCTTCCGCATCCCTAAGGGAACGACACTCATCACCAACCTGTCA
TCGGTGCTGAAGGATGAGGCCGTCTGGGAGAAGCCCTTCCGCTTCCACCCCGAACACTTC
CTGGATGCCCAGGGCCACTTTGTGAAGCCGGAGGCCTTCCTGCCTTTCTCAGCAGGCCGC
CGTGCATGCCTCGGGGAGCCCCTGGCCCGCATGGAGCTCTTCCTCTTCTTCACCTCCCTG
CTGCAGCACTTCAGCTTCTCGGTGCCCACTGGACAGCCCCGGCCCAGCCACCATGGTGTC
TTTGCTTTCCTGGTGACCCCATCCCCCTATGAGCTTTGTGCTGTGCCCCGCTAG
|
| Enzyme 29 GenBank Gene ID |
BC067432  |
| Enzyme 29 GeneCard ID |
Q6NWU0  |
| Enzyme 29 GenAtlas ID |
CYP2D6  |
| Enzyme 29 HGNC ID |
HGNC:2625  |
| Enzyme 29 Chromosome Location |
22 |
| Enzyme 29 Locus |
22q13.1 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
15176 |
| Enzyme 30 Name |
Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a) |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
CYP3A5 |
| Enzyme 30 Protein Sequence |
>Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
|
| Enzyme 30 Number of Residues |
502 |
| Enzyme 30 Molecular Weight |
57109 |
| Enzyme 30 Theoretical pI |
9.09 |
| Enzyme 30 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
Not Available |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
A4D289  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
A4D289_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
Not Available |
| Enzyme 30 GenBank Gene ID |
CH236956  |
| Enzyme 30 GeneCard ID |
A4D289  |
| Enzyme 30 GenAtlas ID |
Not Available |
| Enzyme 30 HGNC ID |
Not Available |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
15177 |
| Enzyme 31 Name |
Cytochrome P450, family 4, subfamily X, polypeptide 1 (Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b) (Cytochrome P450) |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
CYP4X1 |
| Enzyme 31 Protein Sequence |
>Cytochrome P450, family 4, subfamily X, polypeptide 1 (Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b) (Cytochrome P450)
MEFSWLETRWARPFYLAFVFCLALGLLQAIKLYLRRQRLLRDLRPFPAPPTHWFLGHQKF
IQDDNMEKLEEIIEKYPRAFPFWIGPFQAFFCIYDPDYAKTLLSRTDPKSQYLQKFSPPL
LGKGLAALDGPKWFQHRRLLTPGFHFNILKAYIEVMAHSVKMMLDKWEKICSTQDTSVEV
YEHINSMSLDIIMKCAFSKETNCQTNSTHDPYAKAIFELSKIIFHRLYSLLYHSDIIFKL
SPQGYRFQKLSRVLNQYTDTIIQERKKSLQAGVKQDNTPKRKYQDFLDIVLSAKDESGSS
FSDIDVHSEVSTFLLAGHDTLAASISWILYCLALNPEHQERCREEVRGILGDGSSITWDQ
LGEMSYTTMCIKETCRLIPAVPSISRDLSKPLTFPDGCTLPAGITVVLSIWGLHHNPAVW
KNPKVFDPLRFSQENSDQRHPYAYLPFSAGSRNCIGQEFAMIELKVTIALILLHFRVTPD
PTRPLTFPNHFILKPKNGMYLHLKKLSEC
|
| Enzyme 31 Number of Residues |
509 |
| Enzyme 31 Molecular Weight |
58876 |
| Enzyme 31 Theoretical pI |
8.62 |
| Enzyme 31 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 31 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
55664877  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q5VVE5  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
Q5VVE5_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1530 bp
ATGGAATTCTCCTGGCTGGAGACGCGCTGGGCGCGGCCCTTTTACCTGGCGTTCGTGTTC
TGCCTGGCCCTGGGGCTGCTGCAGGCCATTAAGCTGTACCTGCGGAGGCAGCGGCTGCTG
CGGGACCTGCGCCCCTTCCCAGCGCCCCCCACCCACTGGTTCCTTGGGCACCAGAAGTTT
ATTCAGGATGATAACATGGAGAAGCTTGAGGAAATTATTGAAAAATACCCTCGTGCCTTC
CCTTTCTGGATTGGGCCCTTTCAGGCATTTTTCTGTATCTATGACCCAGACTATGCAAAG
ACACTTCTGAGCAGAACAGATCCCAAGTCCCAGTACCTGCAGAAATTCTCACCTCCACTT
CTTGGAAAAGGACTAGCGGCTCTAGACGGACCCAAGTGGTTCCAGCATCGTCGCCTACTA
ACTCCTGGATTCCATTTTAACATCCTGAAAGCATACATTGAGGTGATGGCTCATTCTGTG
AAAATGATGCTGGATAAGTGGGAGAAGATTTGCAGCACTCAGGACACAAGCGTGGAGGTC
TATGAGCACATCAACTCGATGTCTCTGGATATAATCATGAAATGCGCTTTCAGCAAGGAG
ACCAACTGCCAGACAAACAGCACCCATGATCCTTATGCAAAAGCCATATTTGAACTCAGC
AAAATCATATTTCACCGCTTGTACAGTTTGTTGTATCACAGTGACATAATTTTCAAACTC
AGCCCTCAGGGCTACCGCTTCCAGAAGTTAAGCCGAGTGTTGAATCAGTACACAGATACA
ATAATCCAGGAAAGAAAGAAATCCCTCCAGGCTGGGGTAAAGCAGGATAACACTCCGAAG
AGGAAGTACCAGGATTTTCTGGATATTGTCCTTTCTGCCAAGGATGAAAGTGGTAGCAGC
TTCTCAGATATTGATGTACACTCTGAAGTGAGCACATTCCTGTTGGCAGGACATGACACC
TTGGCAGCAAGCATCTCCTGGATCCTTTACTGCCTGGCTCTGAACCCTGAGCATCAAGAG
AGATGCCGGGAGGAGGTCAGGGGCATCCTGGGGGATGGGTCTTCTATCACTTGGGACCAG
CTGGGTGAGATGTCGTACACCACAATGTGCATCAAGGAGACGTGCCGATTGATTCCTGCA
GTCCCGTCCATTTCCAGAGATCTCAGCAAGCCACTTACCTTCCCAGATGGATGCACATTG
CCTGCAGGGATCACCGTGGTTCTTAGTATTTGGGGTCTTCACCACAACCCTGCTGTCTGG
AAAAACCCAAAGGTCTTTGACCCCTTGAGGTTCTCTCAGGAGAATTCTGATCAGAGACAC
CCCTATGCCTACTTACCATTCTCAGCTGGATCAAGGAACTGCATTGGGCAGGAGTTTGCC
ATGATTGAGTTAAAGGTAACCATTGCCTTGATTCTGCTCCACTTCAGAGTGACTCCAGAC
CCCACCAGGCCTCTTACTTTCCCCAACCATTTTATCCTCAAGCCCAAGAATGGGATGTAT
TTGCACCTGAAGAAACTCTCTGAATGTTAG
|
| Enzyme 31 GenBank Gene ID |
AL450996  |
| Enzyme 31 GeneCard ID |
Q5VVE5  |
| Enzyme 31 GenAtlas ID |
CYP4X1  |
| Enzyme 31 HGNC ID |
HGNC:20244  |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
15178 |
| Enzyme 32 Name |
Putative uncharacterized protein CYP3A43 (Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e) |
| Enzyme 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
CYP3A43 |
| Enzyme 32 Protein Sequence |
>Putative uncharacterized protein CYP3A43 (Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e)
MDLIPNFAMETWVLVATSLVLLYIYGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNF
DRECNEKYGEMWGLYEGQQPMLVIMDPDMIKTVLVKECYSVFTNQMPLGPMGFLKSALSF
AEDEEWKRIRTLLSPAFTSVKFKEMVPIISQCGDMLVRSLRQEAENSKSINLKDFFGAYT
MDVITGTLFGVNLDSLNNPQDPFLKNMKKLLKLDFLDPFLLLISLFPFLTPVFEALNIGL
FPKDVTHFLKNSIERMKESRLKDKQKHRVDFFQQMIDSQNSKETKSHKALSDLELVAQSI
IIIFAAYDTTSTTLPFIMYELATHPDVQQKLQEEIDAVLPNKAPVTYDALVQMEYLDMVV
NETLRLFPVVSRVTRVCKKDIEINGVFIPKGLAVMVPIYALHHDPKYWTEPEKFCPESRF
SKKNKDSIDLYRYIPFGAGPRNCIGMRFALTNIKLAVIRALQNFSFKPCKETQIPLKLDN
LPILQPEKPIVLKVHLRDGITSGP
|
| Enzyme 32 Number of Residues |
504 |
| Enzyme 32 Molecular Weight |
57758 |
| Enzyme 32 Theoretical pI |
8.25 |
| Enzyme 32 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 32 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
41471313  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q75MK2  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
Q75MK2_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1512 bp
ATGGATCTCATTCCAAACTTTGCCATGGAAACATGGGTTCTTGTGGCTACCAGCCTGGTA
CTCCTCTATATTTATGGGACCCATTCACATAAACTTTTTAAGAAGCTGGGAATTCCTGGG
CCAACCCCTCTGCCTTTTCTGGGAACTATTTTGTTCTACCTTAGGGGTCTTTGGAATTTT
GACAGAGAATGTAATGAAAAATACGGAGAAATGTGGGGGCTGTATGAGGGGCAACAGCCC
ATGCTGGTCATCATGGATCCCGACATGATCAAAACAGTGTTAGTGAAAGAATGTTACTCT
GTCTTCACAAACCAGATGCCTTTAGGTCCAATGGGATTTCTGAAAAGTGCCTTAAGTTTT
GCTGAAGATGAAGAATGGAAGAGAATACGAACATTGCTATCTCCAGCTTTCACCAGTGTA
AAATTCAAGGAAATGGTCCCCATCATTTCCCAATGTGGAGATATGTTGGTGAGAAGCCTG
AGGCAGGAAGCAGAGAACAGCAAGTCCATCAACTTGAAAGATTTCTTTGGGGCCTACACC
ATGGATGTAATCACTGGCACATTATTTGGAGTGAACTTGGATTCTCTCAACAATCCACAA
GATCCCTTTCTGAAAAATATGAAGAAGCTTTTAAAATTGGATTTTTTGGATCCCTTTTTA
CTCTTAATATCACTCTTTCCATTTCTTACCCCAGTTTTTGAAGCCCTAAATATCGGTTTG
TTTCCAAAAGATGTTACCCATTTTTTAAAAAATTCCATTGAAAGGATGAAAGAAAGTCGC
CTCAAAGATAAACAAAAGCATCGAGTAGATTTCTTTCAACAGATGATCGACTCCCAGAAT
TCCAAAGAAACAAAGTCCCATAAAGCTCTGTCTGATCTGGAGCTTGTGGCCCAGTCAATT
ATCATCATTTTTGCTGCCTATGACACAACTAGCACCACTCTCCCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAGATTGACGCAGTTTTACCC
AATAAGGCACCTGTCACCTACGATGCCCTGGTACAGATGGAGTACCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAGTTGTTAGTAGAGTTACGAGAGTCTGCAAGAAAGAT
ATTGAAATCAATGGAGTGTTCATTCCCAAAGGGTTAGCAGTGATGGTTCCAATCTATGCT
CTTCACCATGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCTGCCCTGAAAGGTTCAGT
AAGAAGAACAAGGACAGCATAGATCTTTACAGATACATACCTTTTGGAGCTGGACCCCGA
AACTGCATTGGCATGAGGTTTGCTCTCACAAACATAAAACTTGCTGTCATTAGAGCACTG
CAGAACTTCTCCTTCAAACCTTGTAAAGAGACTCAGATCCCACTGAAATTAGACAATCTA
CCAATTCTTCAACCAGAAAAACCTATTGTTCTAAAAGTGCACTTAAGAGATGGGATTACA
AGTGGACCCTGA
|
| Enzyme 32 GenBank Gene ID |
AC011904  |
| Enzyme 32 GeneCard ID |
Q75MK2  |
| Enzyme 32 GenAtlas ID |
CYP3A43  |
| Enzyme 32 HGNC ID |
HGNC:17450  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
15226 |
| Enzyme 33 Name |
Myeloperoxidase (Myeloperoxidase, isoform CRA_a) |
| Enzyme 33 Synonyms |
Not Available |
| Enzyme 33 Gene Name |
MPO |
| Enzyme 33 Protein Sequence |
>Myeloperoxidase (Myeloperoxidase, isoform CRA_a)
MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS
|
| Enzyme 33 Number of Residues |
745 |
| Enzyme 33 Molecular Weight |
83870 |
| Enzyme 33 Theoretical pI |
9.14 |
| Enzyme 33 GO Classification |
| Function |
- antioxidant activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 33 General Function |
Not Available |
| Enzyme 33 Specific Function |
Not Available |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
120660232  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
A1L4B8  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
A1L4B8_HUMAN  |
| Enzyme 33 PDB ID |
1MYP  |
| Enzyme 33 PDB File |
Show |
| Enzyme 33 3D Structure |
|
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>2238 bp
ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT
GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG
GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG
TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG
CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC
TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC
GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC
ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC
CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC
AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG
GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC
GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT
CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC
CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC
TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC
CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC
GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC
ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG
GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC
AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG
GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT
CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG
AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG
GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT
TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC
GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA
CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA
GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG
AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG
CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT
GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG
CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC
GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC
CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG
GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC
CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC
AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC
TGGAGGGAAGCCTCCTAG
|
| Enzyme 33 GenBank Gene ID |
BC130476  |
| Enzyme 33 GeneCard ID |
A1L4B8  |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
17 |
| Enzyme 33 Locus |
17q23.1 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
15227 |
| Enzyme 34 Name |
cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a) |
| Enzyme 34 Synonyms |
Not Available |
| Enzyme 34 Gene Name |
PRDX6 |
| Enzyme 34 Protein Sequence |
>cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a)
MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPE
FAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPA
EKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVD
WKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
|
| Enzyme 34 Number of Residues |
224 |
| Enzyme 34 Molecular Weight |
25035 |
| Enzyme 34 Theoretical pI |
6.29 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 34 Specific Function |
Not Available |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
Not Available |
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
158259727  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
A8JZY7  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
A8JZY7_HUMAN  |
| Enzyme 34 PDB ID |
1PRX  |
| Enzyme 34 PDB File |
Show |
| Enzyme 34 3D Structure |
|
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>675 bp
ATGCCCGGAGGTCTGCTTCTCGGGGACGTGGCTCCCAACTTTGAGGCCAATACCACCGTC
GGCCGCATCCGTTTCCACGACTTTCTGGGAGACTCATGGGGCATTCTCTTCTCCCACCCT
CGGGACTTTACCCCAGTGTGCACCACAGAGCTTGGCAGAGCTGCAAAGCTGGCACCAGAA
TTTGCCAAGAGGAATGTTAAGTTGATTGCCCTTTCAATAGACAGTGTTGAGGACCATCTT
GCCTGGAGCAAGGATATCAATGCTTACAATTGTGAAGAGCCCACAGAAAAGTTACCTTTT
CCCATCATCGATGATAGGAATCGGGAGCTTGCCATCCTGTTGGGCATGCTGGATCCAGCA
GAGAAGGATGAAAAGGGCATGCCTGTGACAGCTCGTGTGGTGTTTGTTTTTGGTCCTGAT
AAGAAGCTGAAGCTGTCTATCCTCTACCCAGCTACCACTGGCAGGAACTTTGATGAGATT
CTCAGGGTAGTCATCTCTCTCCAGCTGACAGCAGAAAAAAGGGTTGCCACCCCAGTTGAT
TGGAAGGATGGGGATAGTGTGATGGTCCTTCCAACCATCCCTGAAGAAGAAGCCAAAAAA
CTTTTCCCGAAAGGAGTCTTCACCAAAGAGCTCCCATCTGGCAAGAAATACCTCCGCTAC
ACACCCCAGCCTTAA
|
| Enzyme 34 GenBank Gene ID |
AK289352  |
| Enzyme 34 GeneCard ID |
A8JZY7  |
| Enzyme 34 GenAtlas ID |
Not Available |
| Enzyme 34 HGNC ID |
Not Available |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
Not Available |
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
16465 |
| Enzyme 35 Name |
cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6) |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
CYP2A6 |
| Enzyme 35 Protein Sequence |
>cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
|
| Enzyme 35 Number of Residues |
494 |
| Enzyme 35 Molecular Weight |
56518 |
| Enzyme 35 Theoretical pI |
9.69 |
| Enzyme 35 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
B2R7F6  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
B2R7F6_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
Not Available |
| Enzyme 35 GenBank Gene ID |
AK312964  |
| Enzyme 35 GeneCard ID |
B2R7F6  |
| Enzyme 35 GenAtlas ID |
Not Available |
| Enzyme 35 HGNC ID |
Not Available |
| Enzyme 35 Chromosome Location |
19 |
| Enzyme 35 Locus |
19q13.2 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
Not Available |
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
16466 |
| Enzyme 36 Name |
cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b) |
| Enzyme 36 Synonyms |
Not Available |
| Enzyme 36 Gene Name |
Not Available |
| Enzyme 36 Protein Sequence |
>cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
MDPAVALVLCLSCLFLLSLWRQSSGRGRLPSGPTPLPIIGNILQLDVKDMSKSLTNFSKV
YGPVFTVYFGLKPIVVLHGYEAVKEALIDHGEEFSGRGSFPVAEKVNKGLGILFSNGKRW
KEIRRFCLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS
VIFHDRFDYKDQRFLNLMEKFNENLRILSSPWIQVCNNFPALIDYLPGSHNKIAENFAYI
KSYVLERIKEHQESLDMNSARDFIDCFLIKMEQEKHNQQSEFTVESLIATVTDMFGAGTE
TTSTTLRYGLLLLLKYPEVTAKVQEEIECVVGRNRSPCMQDRSHMPYTDAVVHEIQRYID
LLPTNLPHAVTCDVKFKNYLIPKGTTIITSLTSVLHNDKEFPNPEMFDPGHFLDKSGNFK
KSDYFMPFSAGKRMCMGEGLARMELFLFLTTILQNFNLKSQVDPKDIDITPIANAFGRVP
PLYQLCFIPV
|
| Enzyme 36 Number of Residues |
490 |
| Enzyme 36 Molecular Weight |
55711 |
| Enzyme 36 Theoretical pI |
7.22 |
| Enzyme 36 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
Not Available |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
B2R8K2  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
B2R8K2_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
Not Available |
| Enzyme 36 GenBank Gene ID |
AK313403  |
| Enzyme 36 GeneCard ID |
B2R8K2  |
| Enzyme 36 GenAtlas ID |
Not Available |
| Enzyme 36 HGNC ID |
Not Available |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
Not Available |
| Enzyme 36 General References |
Not Available |
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
16475 |
| Enzyme 37 Name |
cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1) |
| Enzyme 37 Synonyms |
- SubName: Pipecolic acid oxidase, isoform CRA_b
|
| Enzyme 37 Gene Name |
PIPOX |
| Enzyme 37 Protein Sequence |
>cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
|
| Enzyme 37 Number of Residues |
390 |
| Enzyme 37 Molecular Weight |
44067 |
| Enzyme 37 Theoretical pI |
8.54 |
| Enzyme 37 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
- sarcosine oxidase activity
|
| Process |
- aromatic compound metabolism
- cellular metabolism
- electron transport
- folic acid and derivative metabolism
- generation of precursor metabolites and energy
- metabolism
- physiological process
- tetrahydrofolate metabolism
|
| Component |
| — |
|
| Enzyme 37 General Function |
Amino acid transport and metabolism |
| Enzyme 37 Specific Function |
Not Available |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
- sarcosine + H2O + O2 = glycine + formaldehyde + H2O2 [RN:R00610] ALL_REAC R00610
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
B3KNH0  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
B3KNH0_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
Not Available |
| Enzyme 37 GenBank Gene ID |
AK027498  |
| Enzyme 37 GeneCard ID |
B3KNH0  |
| Enzyme 37 GenAtlas ID |
Not Available |
| Enzyme 37 HGNC ID |
Not Available |
| Enzyme 37 Chromosome Location |
17 |
| Enzyme 37 Locus |
17q11.2 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
Not Available |
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
16490 |
| Enzyme 38 Name |
Sarcosine dehydrogenase |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
SARDH |
| Enzyme 38 Protein Sequence |
>Sarcosine dehydrogenase
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
|
| Enzyme 38 Number of Residues |
918 |
| Enzyme 38 Molecular Weight |
101038 |
| Enzyme 38 Theoretical pI |
7.26 |
| Enzyme 38 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- oxidoreductase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- glycine catabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 38 General Function |
Amino acid transport and metabolism |
| Enzyme 38 Specific Function |
Not Available |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
Not Available |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
B2RMR5  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
B2RMR5_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
Not Available |
| Enzyme 38 GenBank Gene ID |
BC136363  |
| Enzyme 38 GeneCard ID |
B2RMR5  |
| Enzyme 38 GenAtlas ID |
SARDH  |
| Enzyme 38 HGNC ID |
HGNC:10536  |
| Enzyme 38 Chromosome Location |
Not Available |
| Enzyme 38 Locus |
Not Available |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
Not Available |
| Enzyme 38 Metabolite References |
Not Available |