|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6306 |
| Enzyme 1 Name |
Cytochrome P450 3A4 |
| Enzyme 1 Synonyms |
- Quinine 3-monooxygenase
- CYPIIIA4
- Nifedipine oxidase
- Taurochenodeoxycholate 6-alpha- hydroxylase
- NF-25
- P450-PCN1
|
| Enzyme 1 Gene Name |
CYP3A4 |
| Enzyme 1 Protein Sequence |
>Cytochrome P450 3A4
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
|
| Enzyme 1 Number of Residues |
503 |
| Enzyme 1 Molecular Weight |
57344 |
| Enzyme 1 Theoretical pI |
8.25 |
| Enzyme 1 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 1 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 1 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 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
- quinine + NADPH + H+ + O2 = 3-hydroxyquinine + NADP+ + H2O
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
181374  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P08684  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
CP3A4_HUMAN  |
| Enzyme 1 PDB ID |
1TQN  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 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 1 GenBank Gene ID |
M18907  |
| Enzyme 1 GeneCard ID |
CYP3A4  |
| Enzyme 1 GenAtlas ID |
CYP3A4  |
| Enzyme 1 HGNC ID |
HGNC:2637  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7q21.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6324 |
| Enzyme 2 Name |
Cytochrome P450 2C9 |
| Enzyme 2 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 2 Gene Name |
CYP2C9 |
| Enzyme 2 Protein Sequence |
>Cytochrome P450 2C9
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
|
| Enzyme 2 Number of Residues |
490 |
| Enzyme 2 Molecular Weight |
55629 |
| Enzyme 2 Theoretical pI |
7.99 |
| Enzyme 2 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 2 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 2 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 2 Pathways |
- Limonene and pinene degradation (map00903
)
- Monoterpenoid biosynthesis (map00902
)
|
| Enzyme 2 Reactions |
- (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
181366  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P11712  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CP2C9_HUMAN  |
| Enzyme 2 PDB ID |
1R9O  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
M21940  |
| Enzyme 2 GeneCard ID |
CYP2C9  |
| Enzyme 2 GenAtlas ID |
CYP2C9  |
| Enzyme 2 HGNC ID |
HGNC:2623  |
| Enzyme 2 Chromosome Location |
10 |
| Enzyme 2 Locus |
10q24 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6326 |
| Enzyme 3 Name |
Cytochrome P450 2C19 |
| Enzyme 3 Synonyms |
- (R-limonene 6-monooxygenase
- (S-limonene 6-monooxygenase
- (S- limonene 7-monooxygenase
- CYPIIC19
- P450-11A
- Mephenytoin 4- hydroxylase
- CYPIIC17
- P450-254C
|
| Enzyme 3 Gene Name |
CYP2C19 |
| Enzyme 3 Protein Sequence |
>Cytochrome P450 2C19
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
|
| Enzyme 3 Number of Residues |
490 |
| Enzyme 3 Molecular Weight |
55932 |
| Enzyme 3 Theoretical pI |
7.42 |
| Enzyme 3 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 3 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 3 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 3 Pathways |
- Limonene and pinene degradation (map00903
)
- Monoterpenoid biosynthesis (map00902
)
|
| Enzyme 3 Reactions |
- (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + 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 |
181344  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P33261  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CP2CJ_HUMAN  |
| Enzyme 3 PDB ID |
1R9O  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 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 3 GenBank Gene ID |
M61854  |
| Enzyme 3 GeneCard ID |
CYP2C19  |
| Enzyme 3 GenAtlas ID |
CYP2C19  |
| Enzyme 3 HGNC ID |
HGNC:2621  |
| Enzyme 3 Chromosome Location |
10 |
| Enzyme 3 Locus |
10q24.1-q24.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6840 |
| Enzyme 4 Name |
Cytochrome P450 2E1 |
| Enzyme 4 Synonyms |
- CYPIIE1
- P450-J
|
| Enzyme 4 Gene Name |
CYP2E1 |
| Enzyme 4 Protein Sequence |
>Cytochrome P450 2E1
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
|
| Enzyme 4 Number of Residues |
493 |
| Enzyme 4 Molecular Weight |
56850 |
| Enzyme 4 Theoretical pI |
8.22 |
| Enzyme 4 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 4 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 4 Specific Function |
Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + 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 |
181360  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P05181  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CP2E1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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 4 GenBank Gene ID |
J02625  |
| Enzyme 4 GeneCard ID |
CYP2E1  |
| Enzyme 4 GenAtlas ID |
CYP2E1  |
| Enzyme 4 HGNC ID |
HGNC:2631  |
| Enzyme 4 Chromosome Location |
10 |
| Enzyme 4 Locus |
10q24.3-qter |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6843 |
| Enzyme 5 Name |
Cytochrome P450 1B1 |
| Enzyme 5 Synonyms |
- CYPIB1
|
| Enzyme 5 Gene Name |
CYP1B1 |
| Enzyme 5 Protein Sequence |
>Cytochrome P450 1B1
MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI
GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF
ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL
LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL
VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA
EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL
DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV
FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL
FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE
TCQ
|
| Enzyme 5 Number of Residues |
543 |
| Enzyme 5 Molecular Weight |
60847 |
| Enzyme 5 Theoretical pI |
9.23 |
| Enzyme 5 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 5 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 5 Specific Function |
Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
501031  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q16678  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
CP1B1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 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 5 GenBank Gene ID |
U03688  |
| Enzyme 5 GeneCard ID |
CYP1B1  |
| Enzyme 5 GenAtlas ID |
CYP1B1  |
| Enzyme 5 HGNC ID |
HGNC:2597  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2p21 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6847 |
| Enzyme 6 Name |
Cytochrome P450 2F1 |
| Enzyme 6 Synonyms |
- CYPIIF1
|
| Enzyme 6 Gene Name |
CYP2F1 |
| Enzyme 6 Protein Sequence |
>Cytochrome P450 2F1
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSK
EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDR
WKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLADVRKTEGEPFDPTFVLSRSVSNIIC
SVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDILDPRFPSLLDWVPGPHQRIFQ
NFKCLRDLIAHSVHDHQASSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGT
KTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA
DIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF
KKSPAFMPFSAGRRLCLGELLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNL
PRPFQLCLRPR
|
| Enzyme 6 Number of Residues |
491 |
| Enzyme 6 Molecular Weight |
55500 |
| Enzyme 6 Theoretical pI |
7.40 |
| Enzyme 6 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 6 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 6 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 6 Pathways |
|
| Enzyme 6 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
181358  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P24903  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
CP2F1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
J02906  |
| Enzyme 6 GeneCard ID |
CYP2F1  |
| Enzyme 6 GenAtlas ID |
CYP2F1  |
| Enzyme 6 HGNC ID |
HGNC:2632  |
| Enzyme 6 Chromosome Location |
19 |
| Enzyme 6 Locus |
19q13.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6849 |
| Enzyme 7 Name |
Cytochrome P450 2B6 |
| Enzyme 7 Synonyms |
- CYPIIB6
- P450 IIB1
|
| Enzyme 7 Gene Name |
CYP2B6 |
| Enzyme 7 Protein Sequence |
>Cytochrome P450 2B6
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
|
| Enzyme 7 Number of Residues |
491 |
| Enzyme 7 Molecular Weight |
56279 |
| Enzyme 7 Theoretical pI |
8.44 |
| Enzyme 7 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 7 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
181296  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P20813  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
CP2B6_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
M29874  |
| Enzyme 7 GeneCard ID |
CYP2B6  |
| Enzyme 7 GenAtlas ID |
CYP2B6  |
| Enzyme 7 HGNC ID |
HGNC:2615  |
| Enzyme 7 Chromosome Location |
19 |
| Enzyme 7 Locus |
19q13.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6852 |
| Enzyme 8 Name |
Cytochrome P450 2A13 |
| Enzyme 8 Synonyms |
- CYPIIA13
|
| Enzyme 8 Gene Name |
CYP2A13 |
| Enzyme 8 Protein Sequence |
>Cytochrome P450 2A13
MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN
GERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKE
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFF
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQ
RFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
|
| Enzyme 8 Number of Residues |
494 |
| Enzyme 8 Molecular Weight |
56688 |
| Enzyme 8 Theoretical pI |
9.78 |
| 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 |
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 8 Pathways |
|
| Enzyme 8 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + 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 |
1777437  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q16696  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
CP2AD_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
U22028  |
| Enzyme 8 GeneCard ID |
CYP2A13  |
| Enzyme 8 GenAtlas ID |
CYP2A13  |
| Enzyme 8 HGNC ID |
HGNC:2608  |
| Enzyme 8 Chromosome Location |
19 |
| Enzyme 8 Locus |
19q13.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6854 |
| Enzyme 9 Name |
Cytochrome P450 4B1 |
| Enzyme 9 Synonyms |
- CYPIVB1
- P450-HP
|
| Enzyme 9 Gene Name |
CYP4B1 |
| Enzyme 9 Protein Sequence |
>Cytochrome P450 4B1
MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE
IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ
WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI
FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT
PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL
SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL
GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP
DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP
SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
|
| Enzyme 9 Number of Residues |
511 |
| Enzyme 9 Molecular Weight |
58992 |
| Enzyme 9 Theoretical pI |
8.39 |
| Enzyme 9 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 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 |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + 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 |
180969  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P13584  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
CP4B1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 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 9 GenBank Gene ID |
J02871  |
| Enzyme 9 GeneCard ID |
CYP4B1  |
| Enzyme 9 GenAtlas ID |
CYP4B1  |
| Enzyme 9 HGNC ID |
HGNC:2644  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p34-p12 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6855 |
| Enzyme 10 Name |
Cytochrome P450 4Z1 |
| Enzyme 10 Synonyms |
- CYPIVZ1
|
| Enzyme 10 Gene Name |
CYP4Z1 |
| Enzyme 10 Protein Sequence |
>Cytochrome P450 4Z1
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEF
YPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESW
VGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELF
QHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFS
SQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFS
EADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLS
QMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWED
PQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHS
RPPQPVRQVVLKSKNGIHVFAKKVC
|
| Enzyme 10 Number of Residues |
505 |
| Enzyme 10 Molecular Weight |
59087 |
| Enzyme 10 Theoretical pI |
9.63 |
| Enzyme 10 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 10 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 10 Specific Function |
RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
29690384  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q86W10  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
CP4Z1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 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 10 GenBank Gene ID |
AY262056  |
| Enzyme 10 GeneCard ID |
CYP4Z1  |
| Enzyme 10 GenAtlas ID |
CYP4Z1  |
| Enzyme 10 HGNC ID |
HGNC:20583  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p33 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6856 |
| Enzyme 11 Name |
Cytochrome P450 1A2 |
| Enzyme 11 Synonyms |
- CYPIA2
- P450-P3
- P(3450
- P450 4
|
| Enzyme 11 Gene Name |
CYP1A2 |
| Enzyme 11 Protein Sequence |
>Cytochrome P450 1A2
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
|
| Enzyme 11 Number of Residues |
515 |
| Enzyme 11 Molecular Weight |
58295 |
| Enzyme 11 Theoretical pI |
9.43 |
| 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 |
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 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 |
30339  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P05177  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
CP1A2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 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 11 GenBank Gene ID |
Z00036  |
| Enzyme 11 GeneCard ID |
CYP1A2  |
| Enzyme 11 GenAtlas ID |
CYP1A2  |
| Enzyme 11 HGNC ID |
HGNC:2596  |
| Enzyme 11 Chromosome Location |
15 |
| Enzyme 11 Locus |
15q24 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6857 |
| Enzyme 12 Name |
Cytochrome P450 19A1 |
| Enzyme 12 Synonyms |
- Aromatase
- CYPXIX
- Estrogen synthetase
- P-450AROM
|
| Enzyme 12 Gene Name |
CYP19A1 |
| Enzyme 12 Protein Sequence |
>Cytochrome P450 19A1
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI
SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL
GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN
ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL
YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI
LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI
YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK
NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH
PDETKNMLEMIFTPRNSDRCLEH
|
| Enzyme 12 Number of Residues |
503 |
| Enzyme 12 Molecular Weight |
57884 |
| Enzyme 12 Theoretical pI |
7.56 |
| 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 |
Catalyzes the formation of aromatic C18 estrogens from C19 androgens |
| 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 |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
179002  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P11511  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
CP19A_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 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 12 GenBank Gene ID |
M22246  |
| Enzyme 12 GeneCard ID |
CYP19A1  |
| Enzyme 12 GenAtlas ID |
CYP19A1  |
| Enzyme 12 HGNC ID |
HGNC:2594  |
| Enzyme 12 Chromosome Location |
15 |
| Enzyme 12 Locus |
15q21.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6858 |
| Enzyme 13 Name |
Cytochrome P450 2C8 |
| Enzyme 13 Synonyms |
- CYPIIC8
- P450 form 1
- P450 MP- 12/MP-20
- P450 IIC2
- S-mephenytoin 4-hydroxylase
|
| Enzyme 13 Gene Name |
CYP2C8 |
| Enzyme 13 Protein Sequence |
>Cytochrome P450 2C8
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
|
| Enzyme 13 Number of Residues |
490 |
| Enzyme 13 Molecular Weight |
55825 |
| Enzyme 13 Theoretical pI |
8.62 |
| Enzyme 13 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 13 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 13 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 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 |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
181326  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P10632  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CP2C8_HUMAN  |
| Enzyme 13 PDB ID |
1PQ2  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 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 13 GenBank Gene ID |
M17397  |
| Enzyme 13 GeneCard ID |
CYP2C8  |
| Enzyme 13 GenAtlas ID |
CYP2C8  |
| Enzyme 13 HGNC ID |
HGNC:2622  |
| Enzyme 13 Chromosome Location |
10 |
| Enzyme 13 Locus |
10q23.33 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6859 |
| Enzyme 14 Name |
Cytochrome P450 2S1 |
| Enzyme 14 Synonyms |
- CYPIIS1
|
| Enzyme 14 Gene Name |
CYP2S1 |
| Enzyme 14 Protein Sequence |
>Cytochrome P450 2S1
MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRL
SKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN
GERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSN
VVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH
VSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLL
FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA
QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA
DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSG
LFNIPPAFQLQVRPTDLHSTTQTR
|
| Enzyme 14 Number of Residues |
504 |
| Enzyme 14 Molecular Weight |
55818 |
| Enzyme 14 Theoretical pI |
8.84 |
| 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 |
Has a potential importance for extrahepatic xenobiotic metabolism |
| 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 |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
13161184  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q96SQ9  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
CP2S1_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 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 14 GenBank Gene ID |
AF335278  |
| Enzyme 14 GeneCard ID |
CYP2S1  |
| Enzyme 14 GenAtlas ID |
CYP2S1  |
| Enzyme 14 HGNC ID |
HGNC:15654  |
| Enzyme 14 Chromosome Location |
19 |
| Enzyme 14 Locus |
19q13.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6861 |
| Enzyme 15 Name |
Cytochrome P450 2J2 |
| Enzyme 15 Synonyms |
- CYPIIJ2
- Arachidonic acid epoxygenase
|
| Enzyme 15 Gene Name |
CYP2J2 |
| Enzyme 15 Protein Sequence |
>Cytochrome P450 2J2
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVD
FEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHI
FKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDP
HFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFL
PGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEEN
LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMP
YTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDT
FNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLS
LKFRMGITISPVSHRLCAVPQV
|
| Enzyme 15 Number of Residues |
502 |
| Enzyme 15 Molecular Weight |
57611 |
| Enzyme 15 Theoretical pI |
8.87 |
| 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 |
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 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 |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
18254513  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P51589  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
CP2J2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 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 15 GenBank Gene ID |
U37143  |
| Enzyme 15 GeneCard ID |
CYP2J2  |
| Enzyme 15 GenAtlas ID |
CYP2J2  |
| Enzyme 15 HGNC ID |
HGNC:2634  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1p31.3-p31.2 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 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 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6862 |
| Enzyme 16 Name |
Cytochrome P450 2A7 |
| Enzyme 16 Synonyms |
- CYPIIA7
- P450-IIA4
|
| Enzyme 16 Gene Name |
CYP2A7 |
| Enzyme 16 Protein Sequence |
>Cytochrome P450 2A7
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMK
FSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSN
GERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSSHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKL
LQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFI
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSSKHVGF
ATIPRNYTMSFLPR
|
| Enzyme 16 Number of Residues |
494 |
| Enzyme 16 Molecular Weight |
56409 |
| Enzyme 16 Theoretical pI |
7.96 |
| Enzyme 16 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 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 |
181270  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P20853  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
CP2A7_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 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 16 GenBank Gene ID |
M33317  |
| Enzyme 16 GeneCard ID |
CYP2A7  |
| Enzyme 16 GenAtlas ID |
CYP2A7  |
| Enzyme 16 HGNC ID |
HGNC:2611  |
| Enzyme 16 Chromosome Location |
19 |
| Enzyme 16 Locus |
19q13.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
13116 |
| Enzyme 17 Name |
Cytochrome P450, family 1, subfamily A, polypeptide 1 |
| Enzyme 17 Synonyms |
- Cytochrome P450, family 1, subfamily A, polypeptide 1, isoform CRA_a
|
| Enzyme 17 Gene Name |
CYP1A1 |
| Enzyme 17 Protein Sequence |
>Cytochrome P450, family 1, subfamily A, polypeptide 1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
|
| Enzyme 17 Number of Residues |
512 |
| Enzyme 17 Molecular Weight |
58166 |
| Enzyme 17 Theoretical pI |
8.47 |
| Enzyme 17 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 17 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 17 Specific Function |
Not Available |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
117606758  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
A0N0X8  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
A0N0X8_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
EF094025  |
| Enzyme 17 GeneCard ID |
A0N0X8  |
| Enzyme 17 GenAtlas ID |
Not Available |
| Enzyme 17 HGNC ID |
Not Available |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
Not Available |
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
15174 |
| Enzyme 18 Name |
Cytochrome P450, family 3, subfamily A, polypeptide 7 |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
CYP3A7 |
| Enzyme 18 Protein Sequence |
>Cytochrome P450, family 3, subfamily A, polypeptide 7
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
|
| Enzyme 18 Number of Residues |
503 |
| Enzyme 18 Molecular Weight |
57471 |
| Enzyme 18 Theoretical pI |
9.52 |
| 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 |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
A4D288  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
A4D288_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
CH236956  |
| Enzyme 18 GeneCard ID |
A4D288  |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
Not Available |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
15175 |
| Enzyme 19 Name |
Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6) |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
CYP2D6 |
| Enzyme 19 Protein Sequence |
>Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLCIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVTPSPYELCAVPR
|
| Enzyme 19 Number of Residues |
497 |
| Enzyme 19 Molecular Weight |
55731 |
| Enzyme 19 Theoretical pI |
7.09 |
| Enzyme 19 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 19 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
45768272  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q6NWU0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
Q6NWU0_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 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 19 GenBank Gene ID |
BC067432  |
| Enzyme 19 GeneCard ID |
Q6NWU0  |
| Enzyme 19 GenAtlas ID |
CYP2D6  |
| Enzyme 19 HGNC ID |
HGNC:2625  |
| Enzyme 19 Chromosome Location |
22 |
| Enzyme 19 Locus |
22q13.1 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
15176 |
| Enzyme 20 Name |
Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a) |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
CYP3A5 |
| Enzyme 20 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 20 Number of Residues |
502 |
| Enzyme 20 Molecular Weight |
57109 |
| Enzyme 20 Theoretical pI |
9.09 |
| Enzyme 20 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 20 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
A4D289  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
A4D289_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
CH236956  |
| Enzyme 20 GeneCard ID |
A4D289  |
| Enzyme 20 GenAtlas ID |
Not Available |
| Enzyme 20 HGNC ID |
Not Available |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
15177 |
| Enzyme 21 Name |
Cytochrome P450, family 4, subfamily X, polypeptide 1 (Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b) (Cytochrome P450) |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
CYP4X1 |
| Enzyme 21 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 21 Number of Residues |
509 |
| Enzyme 21 Molecular Weight |
58876 |
| Enzyme 21 Theoretical pI |
8.62 |
| Enzyme 21 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 21 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
55664877  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q5VVE5  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
Q5VVE5_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 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 21 GenBank Gene ID |
AL450996  |
| Enzyme 21 GeneCard ID |
Q5VVE5  |
| Enzyme 21 GenAtlas ID |
CYP4X1  |
| Enzyme 21 HGNC ID |
HGNC:20244  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
Not Available |
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
15178 |
| Enzyme 22 Name |
Putative uncharacterized protein CYP3A43 (Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e) |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
CYP3A43 |
| Enzyme 22 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 22 Number of Residues |
504 |
| Enzyme 22 Molecular Weight |
57758 |
| Enzyme 22 Theoretical pI |
8.25 |
| 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 |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
41471313  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q75MK2  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
Q75MK2_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 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 22 GenBank Gene ID |
AC011904  |
| Enzyme 22 GeneCard ID |
Q75MK2  |
| Enzyme 22 GenAtlas ID |
CYP3A43  |
| Enzyme 22 HGNC ID |
HGNC:17450  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
16465 |
| Enzyme 23 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 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
CYP2A6 |
| Enzyme 23 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 23 Number of Residues |
494 |
| Enzyme 23 Molecular Weight |
56518 |
| Enzyme 23 Theoretical pI |
9.69 |
| 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 |
Not Available |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
B2R7F6  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
B2R7F6_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
Not Available |
| Enzyme 23 GenBank Gene ID |
AK312964  |
| Enzyme 23 GeneCard ID |
B2R7F6  |
| Enzyme 23 GenAtlas ID |
Not Available |
| Enzyme 23 HGNC ID |
Not Available |
| Enzyme 23 Chromosome Location |
19 |
| Enzyme 23 Locus |
19q13.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
16466 |
| Enzyme 24 Name |
cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b) |
| Enzyme 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
Not Available |
| Enzyme 24 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 24 Number of Residues |
490 |
| Enzyme 24 Molecular Weight |
55711 |
| Enzyme 24 Theoretical pI |
7.22 |
| Enzyme 24 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 24 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 24 Specific Function |
Not Available |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
B2R8K2  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
B2R8K2_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
Not Available |
| Enzyme 24 GenBank Gene ID |
AK313403  |
| Enzyme 24 GeneCard ID |
B2R8K2  |
| Enzyme 24 GenAtlas ID |
Not Available |
| Enzyme 24 HGNC ID |
Not Available |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
Not Available |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |