|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5308 |
| Enzyme 1 Name |
Prostaglandin E synthase |
| Enzyme 1 Synonyms |
- Microsomal glutathione S- transferase 1-like 1
- MGST1-L1
- p53-induced apoptosis protein 12
|
| Enzyme 1 Gene Name |
PTGES |
| Enzyme 1 Protein Sequence |
>Prostaglandin E synthase
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCR
SDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGK
LRAPIRSVTYTLAQLPCASMALQILWEAARHL
|
| Enzyme 1 Number of Residues |
152 |
| Enzyme 1 Molecular Weight |
17103 |
| Enzyme 1 Theoretical pI |
9.77 |
| Enzyme 1 GO Classification |
Not Available |
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15- dihydroxy-9-oxoprosta-5,13-dienoate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
2415308  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O14684  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PTGES_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>462 bp
ATGCCTGCCCACAGCCTGGTGATGAGCAGCCCGGCCCTCCCGGCCTTCCTGCTCTGCAGC
ACGCTGCTGGTCATCAAGATGTACGTGGTGGCCATCATCACGGGCCAAGTGAGGCTGCGG
AAGAAGGCCTTTGCCAACCCCGAGGATGCCCTGAGACACGGAGGAGGCCCCCAGTATTGC
AGGAGCGACCCCGACGTGGAACGCTGCCTCAGGGCCCACCGGAACGACATGGAGACCATC
TACCCCTTCCTTTTCCTGGGCTTCGTCTACTCCTTTCTGGGTCCTAACCCTTTTGTCGCC
TGGATGCACTTCCTGGTCTTCCTCGTGGGCCGTGTGGCACACACCGTGGCCTACCTGGGG
AAGCTGCGGGCACCCATCCGCTCCGTGACCTACACCCTGGCCCAGCTCCCCTGCGCCTCC
ATGGCTCTGCAGATCCTCTGGGAAGCGGCCCGCCACCTGTGA
|
| Enzyme 1 GenBank Gene ID |
AF010316  |
| Enzyme 1 GeneCard ID |
PTGES  |
| Enzyme 1 GenAtlas ID |
PTGES  |
| Enzyme 1 HGNC ID |
HGNC:9599  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q34.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed
]
- Jakobsson PJ, Thoren S, Morgenstern R, Samuelsson B: Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7220-5. [PubMed
]
- Forsberg L, Leeb L, Thoren S, Morgenstern R, Jakobsson P: Human glutathione dependent prostaglandin E synthase: gene structure and regulation. FEBS Lett. 2000 Apr 7;471(1):78-82. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5428 |
| Enzyme 2 Name |
Glutathione reductase, mitochondrial precursor |
| Enzyme 2 Synonyms |
- GR
- GRase
|
| Enzyme 2 Gene Name |
GSR |
| Enzyme 2 Protein Sequence |
>Glutathione reductase, mitochondrial precursor
MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
|
| Enzyme 2 Number of Residues |
522 |
| Enzyme 2 Molecular Weight |
56258 |
| Enzyme 2 Theoretical pI |
8.66 |
| Enzyme 2 GO Classification |
| Function |
- FAD binding
- adenyl nucleotide binding
- binding
- catalytic activity
- disulfide oxidoreductase activity
- electron transporter activity
- glutathione-disulfide reductase activity
- nucleotide binding
- oxidoreductase activity
- purine nucleotide binding
- transporter activity
|
| Process |
- cellular metabolism
- coenzyme metabolism
- cofactor metabolism
- electron transport
- generation of precursor metabolites and energy
- glutathione metabolism
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
RNA processing and modification |
| Enzyme 2 Specific Function |
Maintains high levels of reduced glutathione in the cytosol |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
31825  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P00390  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
GSHR_HUMAN  |
| Enzyme 2 PDB ID |
1BWC  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1440 bp
ATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGCGCCGTGGCC
TCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCGCGCAGGGCG
GCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGCACTTGCGTG
AATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCTGAATTCATG
CATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGGCGTGTTATT
AAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAACAATCTCACC
AAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCCAAGCCCACA
ATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACAGGTGGTATG
CCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACCAGCGATGGA
TTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGTTACATTGCT
GTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATGATACGGCAT
GATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAGGAGCTGGAG
AACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAGACTTTGTCG
GGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATGACCATGATT
CCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAGGACCTGAGT
TTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGACGAATTCCAG
AATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCTCTTCTTACT
CCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATATAAGGAAGAT
TCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCTATTGGGACA
GTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTGAAGACCTAT
TCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAATGTGTGATG
AAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAGGGACTTGGG
TGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACGAAGGCAGAC
TTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACACTTCGTTGA
|
| Enzyme 2 GenBank Gene ID |
X15722  |
| Enzyme 2 GeneCard ID |
GSR  |
| Enzyme 2 GenAtlas ID |
GSR  |
| Enzyme 2 HGNC ID |
HGNC:4623  |
| Enzyme 2 Chromosome Location |
8 |
| Enzyme 2 Locus |
8p21.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed
]
- Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed
]
- Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed
]
- Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed
]
- Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed
]
- Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed
]
- Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed
]
- Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed
]
- Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5629 |
| Enzyme 3 Name |
Lactoylglutathione lyase |
| Enzyme 3 Synonyms |
- Methylglyoxalase
- Aldoketomutase
- Glyoxalase I
- Glx I
- Ketone-aldehyde mutase
- S-D- lactoylglutathione methylglyoxal lyase
|
| Enzyme 3 Gene Name |
GLO1 |
| Enzyme 3 Protein Sequence |
>Lactoylglutathione lyase
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQK
CDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNS
DPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKM
ATLM
|
| Enzyme 3 Number of Residues |
184 |
| Enzyme 3 Molecular Weight |
20778 |
| Enzyme 3 Theoretical pI |
4.92 |
| Enzyme 3 GO Classification |
| Function |
- carbon-sulfur lyase activity
- catalytic activity
- lactoylglutathione lyase activity
- lyase activity
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Amino acid transport and metabolism |
| Enzyme 3 Specific Function |
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- (R)-S-lactoylglutathione = glutathione + methylglyoxal
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
219664  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q04760  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
LGUL_HUMAN  |
| Enzyme 3 PDB ID |
1QIP  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>555 bp
ATGGCAGAACCGCAGCCCCCGTCCGGCGGCCTCACGGACGAGGCCGCCCTCAGTTGCTGC
TCCGACGCGGACCCCAGTACCAAGGATTTTCTATTGCAGCAGACCATGCTACGAGTGAAG
GATCCTAAGAAGTCACTGGATTTTTATACTAGAGTTCTTGGAATGACGCTAATCCAAAAA
TGTGATTTTCCCATTATGAAGTTTTCACTCTACTTCTTGGCTTATGAGGATAAAAATGAC
ATCCCTAAAGAAAAAGATGAAAAAATAGCCTGGGCGCTCTCCAGAAAAGCTACACTTGAG
CTGACACACAATTGGGGCACTGAAGATGATGCGACCCAGAGTTACCACAATGGCAATTCA
GACCCTCGAGGATTCGGTCATATTGGAATTGCTGTTCCTGATGTATACAGTGCTTGTAAA
AGGTTTGAAGAACTGGGAGTCAAATTTGTGAAGAAACCTGATGATGGTAAAATGAAAGGC
CTGGCATTTATTCAAGATCCTGATGGCTACTGGATTGAAATTTTGAATCCTAACAAAATG
GCAACCTTAATGTAG
|
| Enzyme 3 GenBank Gene ID |
D13315  |
| Enzyme 3 GeneCard ID |
GLO1  |
| Enzyme 3 GenAtlas ID |
GLO1  |
| Enzyme 3 HGNC ID |
HGNC:4323  |
| Enzyme 3 Chromosome Location |
6 |
| Enzyme 3 Locus |
6p21.3-p21.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Kim NS, Umezawa Y, Ohmura S, Kato S: Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J Biol Chem. 1993 May 25;268(15):11217-21. [PubMed
]
- Ranganathan S, Walsh ES, Godwin AK, Tew KD: Cloning and characterization of human colon glyoxalase-I. J Biol Chem. 1993 Mar 15;268(8):5661-7. [PubMed
]
- Ridderstrom M, Mannervik B: Optimized heterologous expression of the human zinc enzyme glyoxalase I. Biochem J. 1996 Mar 1;314 ( Pt 2):463-7. [PubMed
]
- Ranganathan S, Ciaccio PJ, Walsh ES, Tew KD: Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation. Gene. 1999 Nov 15;240(1):149-55. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA: Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. EMBO J. 1997 Jun 16;16(12):3386-95. [PubMed
]
- Ridderstrom M, Cameron AD, Jones TA, Mannervik B: Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I. J Biol Chem. 1998 Aug 21;273(34):21623-8. [PubMed
]
- Cameron AD, Ridderstrom M, Olin B, Kavarana MJ, Creighton DJ, Mannervik B: Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry. 1999 Oct 12;38(41):13480-90. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6005 |
| Enzyme 4 Name |
Gamma-glutamyltranspeptidase 1 precursor |
| Enzyme 4 Synonyms |
- Gamma- glutamyltransferase 1
- GGT 1
- CD224 antigen[Contains: Gamma- glutamyltranspeptidase 1 heavy chain
- Gamma-glutamyltranspeptidase 1 light chain]
|
| Enzyme 4 Gene Name |
GGT1 |
| Enzyme 4 Protein Sequence |
>Gamma-glutamyltranspeptidase 1 precursor
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
|
| Enzyme 4 Number of Residues |
569 |
| Enzyme 4 Molecular Weight |
61411 |
| Enzyme 4 Theoretical pI |
7.14 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive |
| Enzyme 4 Pathways |
- Arachidonic acid metabolism (map00590
)
- Cyanoamino acid metabolism (map00460
)
- Glutathione Metabolism (map00480
)
- Selenoamino Acid Metabolism (map00450
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 4 Reactions |
- (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
183138  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P19440  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
GGT1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1710 bp
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
|
| Enzyme 4 GenBank Gene ID |
J04131  |
| Enzyme 4 GeneCard ID |
GGT1  |
| Enzyme 4 GenAtlas ID |
GGT1  |
| Enzyme 4 HGNC ID |
HGNC:4250  |
| Enzyme 4 Chromosome Location |
22 |
| Enzyme 4 Locus |
22q11.23 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed
]
- Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed
]
- Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed
]
- Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed
]
- Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed
]
- Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed
]
- Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed
]
- Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed
]
- Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed
]
- Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed
]
- Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6071 |
| Enzyme 5 Name |
Glutathione synthetase |
| Enzyme 5 Synonyms |
- Glutathione synthase
- GSH synthetase
- GSH-S
|
| Enzyme 5 Gene Name |
GSS |
| Enzyme 5 Protein Sequence |
>Glutathione synthetase
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
|
| Enzyme 5 Number of Residues |
474 |
| Enzyme 5 Molecular Weight |
52385 |
| Enzyme 5 Theoretical pI |
5.73 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- glutathione synthase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- cellular metabolism
- coenzyme metabolism
- cofactor metabolism
- glutathione biosynthesis
- glutathione metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
886284  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P48637  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GSHB_HUMAN  |
| Enzyme 5 PDB ID |
2HGS  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1425 bp
ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA
|
| Enzyme 5 GenBank Gene ID |
L42531  |
| Enzyme 5 GeneCard ID |
GSS  |
| Enzyme 5 GenAtlas ID |
GSS  |
| Enzyme 5 HGNC ID |
HGNC:4624  |
| Enzyme 5 Chromosome Location |
20 |
| Enzyme 5 Locus |
20q11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed
]
- Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6087 |
| Enzyme 6 Name |
Leukotriene C4 synthase |
| Enzyme 6 Synonyms |
- Leukotriene-C(4synthase
- LTC4 synthase
|
| Enzyme 6 Gene Name |
LTC4S |
| Enzyme 6 Protein Sequence |
>Leukotriene C4 synthase
MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYF
PLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVA
LAALGLLAHFLPAALRAALLGRLRTLLPWA
|
| Enzyme 6 Number of Residues |
150 |
| Enzyme 6 Molecular Weight |
16567 |
| Enzyme 6 Theoretical pI |
10.40 |
| Enzyme 6 GO Classification |
| Function |
- enzyme activator activity
- enzyme regulator activity
|
| Process |
- carboxylic acid metabolism
- cellular metabolism
- fatty acid metabolism
- icosanoid metabolism
- leukotriene metabolism
- metabolism
- organic acid metabolism
- physiological process
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4 |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- leukotriene C4 = leukotriene A4 + glutathione
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
520485  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q16873  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
LTC4S_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>453 bp
ATGAAGGACGAGGTAGCTCTACTGGCTGCTGTCACCCTCCTGGGAGTCCTGCTGCAAGCC
TACTTCTCCCTGCAGGTGATCTCGGCGCGCAGGGCCTTCCGCGTGTCGCCGCCGCTCACC
ACCGGCCCACCCGAGTTCGAGCGCGTCTACCGAGCCCAGGTGAACTGCAGCGAGTACTTC
CCGCTGTTCCTCGCCACGCTCTGGGTCGCCGGCATCTTCTTTCATGAAGGGGCGGCGGCC
CTGTGCGGCCTGGTCTACCTGTTCGCGCGCCTCCGCTACTTCCAGGGCTACGCGCGCTCC
GCGCAGCTCAGGCTGGCACCGCTGTACGCGAGCGCGCGCGCCCTCTGGCTGCTGGTGGCG
CTGGCTGCGCTCGGCCTGCTCGCCCACTTCCTCCCGGCCGCGCTGCGCGCCGCGCTCCTC
GGACGGCTCCGGACGCTGCTGCCGTGGGCCTGA
|
| Enzyme 6 GenBank Gene ID |
U09353  |
| Enzyme 6 GeneCard ID |
LTC4S  |
| Enzyme 6 GenAtlas ID |
LTC4S  |
| Enzyme 6 HGNC ID |
HGNC:6719  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q35 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Lam BK, Penrose JF, Freeman GJ, Austen KF: Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7663-7. [PubMed
]
- Welsch DJ, Creely DP, Hauser SD, Mathis KJ, Krivi GG, Isakson PC: Molecular cloning and expression of human leukotriene-C4 synthase. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9745-9. [PubMed
]
- Penrose JF, Spector J, Baldasaro M, Xu K, Boyce J, Arm JP, Austen KF, Lam BK: Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. J Biol Chem. 1996 May 10;271(19):11356-61. [PubMed
]
- Bigby TD, Hodulik CR, Arden KC, Fu L: Molecular cloning of the human leukotriene C4 synthase gene and assignment to chromosome 5q35. Mol Med. 1996 Sep;2(5):637-46. [PubMed
]
- Nicholson DW, Ali A, Vaillancourt JP, Calaycay JR, Mumford RA, Zamboni RJ, Ford-Hutchinson AW: Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):2015-9. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6088 |
| Enzyme 7 Name |
Glutathione S-transferase Mu 2 |
| Enzyme 7 Synonyms |
- GSTM2-2
- GST class-mu 2
|
| Enzyme 7 Gene Name |
GSTM2 |
| Enzyme 7 Protein Sequence |
>Glutathione S-transferase Mu 2
MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDF
EKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK
|
| Enzyme 7 Number of Residues |
218 |
| Enzyme 7 Molecular Weight |
25745 |
| Enzyme 7 Theoretical pI |
6.29 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
183301  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P28161  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GSTM2_HUMAN  |
| Enzyme 7 PDB ID |
1XW5  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>657 bp
ATGCCCATGACACTGGGGTACTGGAACATCCGCGGGCTGGCCCATTCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGACTCACAAGATCACCCAGAGCAATGCCATCCTGCGGTACATT
GCCCGCAAGCACAACCTGTGCGGGGAATCAGAAAAGGAGCAGATTCGCGAAGACATTTTG
GAGAACCAGTTTATGGACAGCCGTATGCAGCTGGCCAAACTCTGCTATGACCCAGATTTT
GAGAAACTGAAACCAGAATACCTGCAGGCACTCCCTGAAATGCTGAAGCTCTACTCACAG
TTTCTGGGGAAGCAGCCATGGTTTCTTGGGGACAAGATCACCTTTGTGGATTTCATCGCT
TATGATGTCCTTGAGAGAAACCAAGTATTTGAGCCCAGCTGCCTGGATGCCTTCCCAAAC
CTGAAGGACTTCATCTCCCGATTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCACAAAGATGGCTGTCTGGGGCAACAAGTAG
|
| Enzyme 7 GenBank Gene ID |
M63509  |
| Enzyme 7 GeneCard ID |
GSTM2  |
| Enzyme 7 GenAtlas ID |
GSTM2  |
| Enzyme 7 HGNC ID |
HGNC:4634  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p13.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Vorachek WR, Pearson WR, Rule GS: Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4443-7. [PubMed
]
- Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed
]
- Raghunathan S, Chandross RJ, Kretsinger RH, Allison TJ, Penington CJ, Rule GS: Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J Mol Biol. 1994 May 20;238(5):815-32. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6089 |
| Enzyme 8 Name |
Glutathione peroxidase 7 precursor |
| Enzyme 8 Synonyms |
- CL683
|
| Enzyme 8 Gene Name |
GPX7 |
| Enzyme 8 Protein Sequence |
>Glutathione peroxidase 7 precursor
MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFT
DQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAV
TGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLI
LLKREDL
|
| Enzyme 8 Number of Residues |
187 |
| Enzyme 8 Molecular Weight |
20996 |
| Enzyme 8 Theoretical pI |
8.46 |
| Enzyme 8 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 8 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 8 Specific Function |
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 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 |
25990366  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q96SL4  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GPX7_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>564 bp
ATGGTGGCGGCGACGGTGGCAGCGGCGTGGCTGCTCCTGTGGGCTGCGGCCTGCGCGCAG
CAGGAGCAGGACTTCTACGACTTCAAGGCGGTCAACATCCGGGGCAAACTGGTGTCGCTG
GAGAAGTACCGCGGATCGGTGTCCCTGGTGGTGAATGTGGCCAGCGAGTGCGGCTTCACA
GACCAGCACTACCGAGCCCTGCAGCAGCTGCAGCGAGACCTGGGCCCCCACCACTTTAAC
GTGCTCGCCTTCCCCTGCAACCAGTTTGGCCAACAGGAGCCTGACAGCAACAAGGAGATT
GAGAGCTTTGCCCGCCGCACCTACAGTGTCTCATTCCCCATGTTTAGCAAGATTGCAGTC
ACCGGTACTGGTGCCCATCCTGCCTTCAAGTACCTGGCCCAGACTTCTGGGAAGGAGCCC
ACCTGGAACTTCTGGAAGTACCTAGTAGCCCCAGATGGAAAGGTGGTAGGGGCTTGGGAC
CCAACTGTGTCAGTGGAGGAGGTCAGACCCCAGATCACAGCGCTCGTGAGGAAGCTCATC
CTACTGAAGCGAGAAGACTTATAA
|
| Enzyme 8 GenBank Gene ID |
AF320068  |
| Enzyme 8 GeneCard ID |
GPX7  |
| Enzyme 8 GenAtlas ID |
GPX7  |
| Enzyme 8 HGNC ID |
HGNC:4559  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p32 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6090 |
| Enzyme 9 Name |
Epididymal secretory glutathione peroxidase precursor |
| Enzyme 9 Synonyms |
- Epididymis-specific glutathione peroxidase-like protein
- EGLP
|
| Enzyme 9 Gene Name |
GPX5 |
| Enzyme 9 Protein Sequence |
>Epididymal secretory glutathione peroxidase precursor
MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYV
GKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLK
YVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIR
WNFEKFLVGPDGIPVMRWSHRATVSSVKTDILAYLKQFKTK
|
| Enzyme 9 Number of Residues |
221 |
| Enzyme 9 Molecular Weight |
25203 |
| Enzyme 9 Theoretical pI |
8.89 |
| Enzyme 9 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 9 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 9 Specific Function |
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathionine peroxidase-like protective system against peroxide damage in sperm membrane lipids |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 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 |
3288455  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O75715  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
GPX5_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>666 bp
ATGACTACACAGTTAAGGGTCGTCCATCTGCTTCCCCTTCTCCTAGCCTGCTTTGTGCAA
ACAAGTCCCAAGCAGGAGAAGATGAAGATGGATTGCCACAAAGACGAGAAAGGCACCATC
TATGACTATGAGGCCATCGCACTTAATAAGAATGAATATGTTTCCTTCAAGCAGTATGTG
GGCAAGCACATCCTCTTCGTCAACGTGGCCACCTACTGTGGTCTGACAGCGCAATATCCT
GAACTAAATGCACTCCAGGAGGAGCTGAAGCCCTATGGTCTAGTTGTGTTGGGCTTTCCC
TGCAACCAATTTGGAAAGCAAGAACCAGGAGATAACAAAGAGATTCTTCCTGGGCTCAAG
TATGTCCGTCCAGGGGGAGGATTTGTACCTAGTTTCCAGCTTTTTGAGAAAGGGGATGTG
AATGGTGAAAAAGAACAGAAAGTCTTCAGTTTCTTGAAGCACTCCTGTCCTCATCCCTCT
GAGATTTTGGGCACATTCAAATCTATATCCTGGGACCCTGTAAAGGTCCATGACATCCGT
TGGAACTTTGAAAAGTTCCTGGTGGGGCCTGATGGAATCCCTGTCATGCGCTGGTCCCAC
CGGGCTACGGTCAGCTCAGTCAAGACAGACATCCTGGCGTACTTGAAGCAATTCAAAACC
AAATAG
|
| Enzyme 9 GenBank Gene ID |
AJ005277  |
| Enzyme 9 GeneCard ID |
GPX5  |
| Enzyme 9 GenAtlas ID |
GPX5  |
| Enzyme 9 HGNC ID |
HGNC:4557  |
| Enzyme 9 Chromosome Location |
6 |
| Enzyme 9 Locus |
6p22.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Hall L, Williams K, Perry AC, Frayne J, Jury JA: The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. Biochem J. 1998 Jul 1;333 ( Pt 1):5-9. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6091 |
| Enzyme 10 Name |
Glutathione S-transferase Mu 1 |
| Enzyme 10 Synonyms |
- GSTM1-1
- GST class-mu 1
- GSTM1a-1a
- GSTM1b-1b
- HB subunit 4
- GTH4
|
| Enzyme 10 Gene Name |
GSTM1 |
| Enzyme 10 Protein Sequence |
>Glutathione S-transferase Mu 1
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
|
| Enzyme 10 Number of Residues |
218 |
| Enzyme 10 Molecular Weight |
25712 |
| Enzyme 10 Theoretical pI |
6.67 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
31924  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P09488  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
GSTM1_HUMAN  |
| Enzyme 10 PDB ID |
1XWK  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>657 bp
ATGCCCATGATACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTATGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCTTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGACCATGGACAACCATATGCAGCTGGGCATGATCTGCTACAATCCAGAATTT
GAGAAACTGAAGCCAAAGTACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAAACAAGATCACTTTTGTAGATTTTCTCGTC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCTCAAAGATGGCTGTCTGGGGCAACAAGTAG
|
| Enzyme 10 GenBank Gene ID |
X08020  |
| Enzyme 10 GeneCard ID |
GSTM1  |
| Enzyme 10 GenAtlas ID |
GSTM1  |
| Enzyme 10 HGNC ID |
HGNC:4632  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p13.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- DeJong JL, Chang CM, Whang-Peng J, Knutsen T, Tu CP: The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA. Nucleic Acids Res. 1988 Sep 12;16(17):8541-54. [PubMed
]
- Seidegard J, Vorachek WR, Pero RW, Pearson WR: Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7293-7. [PubMed
]
- Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed
]
- Comstock KE, Sanderson BJ, Claflin G, Henner WD: GST1 gene deletion determined by polymerase chain reaction. Nucleic Acids Res. 1990 Jun 25;18(12):3670. [PubMed
]
- Pearson WR, Vorachek WR, Xu SJ, Berger R, Hart I, Vannais D, Patterson D: Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am J Hum Genet. 1993 Jul;53(1):220-33. [PubMed
]
- Tsuchida S, Maki T, Sato K: Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. Multiplicity of the human class Mu forms. J Biol Chem. 1990 May 5;265(13):7150-7. [PubMed
]
- Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed
]
- Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed
]
- Singhal SS, Ahmad H, Sharma R, Gupta S, Haque AK, Awasthi YC: Purification and characterization of human muscle glutathione S-transferases: evidence that glutathione S-transferase zeta corresponds to a locus distinct from GST1, GST2, and GST3. Arch Biochem Biophys. 1991 Feb 15;285(1):64-73. [PubMed
]
- Singhal SS, Saxena M, Awasthi S, Ahmad H, Sharma R, Awasthi YC: Gender related differences in the expression and characteristics of glutathione S-transferases of human colon. Biochim Biophys Acta. 1992 Nov 15;1171(1):19-26. [PubMed
]
- Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed
]
- Patskovsky YV, Patskovska LN, Listowsky I: Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. Biochemistry. 1999 Jan 26;38(4):1193-202. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6092 |
| Enzyme 11 Name |
Hydroxyacylglutathione hydrolase |
| Enzyme 11 Synonyms |
- Glyoxalase II
- GLX II
|
| Enzyme 11 Gene Name |
HAGH |
| Enzyme 11 Protein Sequence |
>Hydroxyacylglutathione hydrolase
MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHA
GGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS
KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNL
KFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD
PVTTMRAVRREKDQFKMPRD
|
| Enzyme 11 Number of Residues |
260 |
| Enzyme 11 Molecular Weight |
28860 |
| Enzyme 11 Theoretical pI |
7.36 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
1237213  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q16775  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
GLO2_HUMAN  |
| Enzyme 11 PDB ID |
1QH3  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>783 bp
ATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAACTACATGTACCTGGTCATTGATGAT
GAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAGCCCCAGAAGGTCGTGGACGCGGCG
AGAAAGCACGGGGTGAAACTGACCACAGTGCTCACCACCCACCACCACTGGGACCATGCT
GGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGACTGAAGGTGTACGGGGGTGACGAC
CGTATCGGGGCCCTGACTCACAAGATCACTCACCTGTCCACACTGCAGGTGGGGTCTCTG
AACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCAGGACACATTTGTTACTTCGTGAGC
AAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACAGGTGACACCTTGTTTGTGGCTGGC
TGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATGTGTAAAGCTCTGCTGGAGGTCTTG
GGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGCCACGAGTACACCATCAACAACCTC
AAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCCATCCGGGAGAAGCTGGCCTGGGCC
AAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCATCCACCCTGGCAGAGGAGTTTACC
TACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTGCAGCAGCACGCAGGTGAGACGGAC
CCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAGGACCAGTTCAAGATGCCCCGGGAC
TGA
|
| Enzyme 11 GenBank Gene ID |
X90999  |
| Enzyme 11 GeneCard ID |
HAGH  |
| Enzyme 11 GenAtlas ID |
HAGH  |
| Enzyme 11 HGNC ID |
HGNC:4805  |
| Enzyme 11 Chromosome Location |
16 |
| Enzyme 11 Locus |
16p13.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Ridderstrom M, Saccucci F, Hellman U, Bergman T, Principato G, Mannervik B: Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J Biol Chem. 1996 Jan 5;271(1):319-23. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
- Cameron AD, Ridderstrom M, Olin B, Mannervik B: Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6093 |
| Enzyme 12 Name |
Glutathione S-transferase kappa 1 |
| Enzyme 12 Synonyms |
- GST 13-13
- Glutathione S-transferase subunit 13
- GST class-kappa
- GSTK1-1
- hGSTK1
|
| Enzyme 12 Gene Name |
GSTK1 |
| Enzyme 12 Protein Sequence |
>Glutathione S-transferase kappa 1
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
|
| Enzyme 12 Number of Residues |
226 |
| Enzyme 12 Molecular Weight |
25497 |
| Enzyme 12 Theoretical pI |
8.69 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- disulfide oxidoreductase activity
- oxidoreductase activity
- protein disulfide oxidoreductase activity
|
| Process |
| — |
| Component |
- cell
- periplasmic space
- periplasmic space (sensu Gram-negative Bacteria)
|
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB) |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
41351794  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9Y2Q3  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
GSTK1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
|
| Enzyme 12 GenBank Gene ID |
AY520571  |
| Enzyme 12 GeneCard ID |
GSTK1  |
| Enzyme 12 GenAtlas ID |
GSTK1  |
| Enzyme 12 HGNC ID |
HGNC:16906  |
| Enzyme 12 Chromosome Location |
7 |
| Enzyme 12 Locus |
- |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6095 |
| Enzyme 13 Name |
Glutathione S-transferase Mu 3 |
| Enzyme 13 Synonyms |
- GSTM3-3
- GST class-mu 3
- hGSTM3-3
|
| Enzyme 13 Gene Name |
GSTM3 |
| Enzyme 13 Protein Sequence |
>Glutathione S-transferase Mu 3
MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLD
FPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCY
SSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLD
EFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
|
| Enzyme 13 Number of Residues |
225 |
| Enzyme 13 Molecular Weight |
26560 |
| Enzyme 13 Theoretical pI |
5.19 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
306820  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P21266  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
GSTM3_HUMAN  |
| Enzyme 13 PDB ID |
3GTU  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>678 bp
ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA
|
| Enzyme 13 GenBank Gene ID |
J05459  |
| Enzyme 13 GeneCard ID |
GSTM3  |
| Enzyme 13 GenAtlas ID |
GSTM3  |
| Enzyme 13 HGNC ID |
HGNC:4635  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p13.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I: A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes. J Biol Chem. 1990 Jun 5;265(16):9188-93. [PubMed
]
- Patskovsky YV, Huang MQ, Takayama T, Listowsky I, Pearson WR: Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster. Arch Biochem Biophys. 1999 Jan 1;361(1):85-93. [PubMed
]
- Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed
]
- Hussey AJ, Hayes JD: Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue. Biochim Biophys Acta. 1993 Nov 10;1203(1):131-41. [PubMed
]
- Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6096 |
| Enzyme 14 Name |
Glutathione S-transferase A1 |
| Enzyme 14 Synonyms |
- GTH1
- HA subunit 1
- GST- epsilon
- GSTA1-1
- GST class-alpha member 1
|
| Enzyme 14 Gene Name |
GSTA1 |
| Enzyme 14 Protein Sequence |
>Glutathione S-transferase A1
MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAK
LALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF
|
| Enzyme 14 Number of Residues |
222 |
| Enzyme 14 Molecular Weight |
25631 |
| Enzyme 14 Theoretical pI |
9.34 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
306809  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P08263  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
GSTA1_HUMAN  |
| Enzyme 14 PDB ID |
1K3Y  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTTCAATGCACGGGGCAGAATGGAGTCCACCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAGAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTCCTTCTGCCCGTATGTCCACCTGAGGAAAAAGATGCCAAG
CTTGCCTTGATCAAGGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCATCTG
GTGGAACTTCTCTACTACGTCGAGGAGCTTGACTCCAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 14 GenBank Gene ID |
M15872  |
| Enzyme 14 GeneCard ID |
GSTA1  |
| Enzyme 14 GenAtlas ID |
GSTA1  |
| Enzyme 14 HGNC ID |
HGNC:4626  |
| Enzyme 14 Chromosome Location |
6 |
| Enzyme 14 Locus |
6p12.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Tu CP, Qian B: Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. Biochem Biophys Res Commun. 1986 Nov 26;141(1):229-37. [PubMed
]
- Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed
]
- Tu CP, Qian B: Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. Biochem Soc Trans. 1987 Aug;15(4):734-6. [PubMed
]
- Board PG, Webb GC: Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2377-81. [PubMed
]
- Rozen F, Nguyen T, Pickett CB: Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene. Arch Biochem Biophys. 1992 Feb 1;292(2):589-93. [PubMed
]
- Chow NW, Whang-Peng J, Kao-Shan CS, Tam MF, Lai HC, Tu CP: Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. J Biol Chem. 1988 Sep 15;263(26):12797-800. [PubMed
]
- Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed
]
- Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed
]
- Board PG, Mannervik B: The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase. Biochem J. 1991 Apr 1;275 ( Pt 1):171-4. [PubMed
]
- Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al.: Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J Mol Biol. 1993 Jul 5;232(1):192-212. [PubMed
]
- Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA: Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure. 1995 Jul 15;3(7):717-27. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6097 |
| Enzyme 15 Name |
Maleylacetoacetate isomerase |
| Enzyme 15 Synonyms |
- MAAI
- Glutathione S- transferase zeta 1
- GSTZ1-1
|
| Enzyme 15 Gene Name |
GSTZ1 |
| Enzyme 15 Protein Sequence |
>Maleylacetoacetate isomerase
MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVP
TLKIDGITIHQSLAIIEYLEETRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLK
QVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDL
TPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
|
| Enzyme 15 Number of Residues |
216 |
| Enzyme 15 Molecular Weight |
24182 |
| Enzyme 15 Theoretical pI |
8.71 |
| Enzyme 15 GO Classification |
| Function |
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- aromatic amino acid family metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 15 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 15 Specific Function |
Bifunctional enzyme showing minimal glutathione- conjugating activity with ethacrynic acid and 7-chloro-4- nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T- butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- 4-maleylacetoacetate = 4-fumarylacetoacetate
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
2832731  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
O43708  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
MAAI_HUMAN  |
| Enzyme 15 PDB ID |
1FW1  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>651 bp
ATGCAGGCGGGGAAGCCCATCCTCTATTCCTATTTCCGAAGCTCCTGCTCATGGAGAGTT
CGAATTGCTCTGGCCTTGAAAGGCATCGACTACAAGACGGTGCCCATCAATCTCATAAAG
GATGGGGGCCAACAGTTTTCTAAGGACTTCCAGGCACTGAATCCTATGAAGCAGGTGCCA
ACCCTGAAGATTGATGGAATCACCATTCACCAGTCACTGGCCATCATTGAGTATCTAGAG
GAGACGCGTCCCACTCCGCGACTTCTGCCTCAGGACCCAAAGAAGAGGGCCAGCGTGCGT
ATGATTTCTGACCTCATCGCTGGTGGCATCCAGCCCCTGCAGAACCTGTCTGTCCTGAAG
CAAGTGGGAGAGGAGATGCAGCTGACCTGGGCCCAGAACGCCATCACTTGTGGCTTTAAC
GCCCTGGAGCAGATCCTACAGAGCACAGCGGGCATATACTGTGTAGGAGACGAGGTGACC
ATGGCTGATCTGTGCTTGGTGCCTCAGGTGGCAAATGCTGAAAGATTCAAGGTGGATCTC
ACCCCCTACCCTACCATCAGCTCCATCAACAAGAGGCTGCTGGTCTTGGAGGCCTTCCAG
GTGTCTCACCCCTGCCGGCAGCCAGATACACCCACTGAGCTGAGGGCCTAG
|
| Enzyme 15 GenBank Gene ID |
AJ001838  |
| Enzyme 15 GeneCard ID |
GSTZ1  |
| Enzyme 15 GenAtlas ID |
GSTZ1  |
| Enzyme 15 HGNC ID |
HGNC:4643  |
| Enzyme 15 Chromosome Location |
14 |
| Enzyme 15 Locus |
14q24.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Fernandez-Canon JM, Penalva MA: Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. J Biol Chem. 1998 Jan 2;273(1):329-37. [PubMed
]
- Board PG, Baker RT, Chelvanayagam G, Jermiin LS: Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J. 1997 Dec 15;328 ( Pt 3):929-35. [PubMed
]
- Blackburn AC, Woollatt E, Sutherland GR, Board PG: Characterization and chromosome location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase. Cytogenet Cell Genet. 1998;83(1-2):109-14. [PubMed
]
- Fernandez-Canon JM, Hejna J, Reifsteck C, Olson S, Grompe M: Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase. Genomics. 1999 Jun 15;58(3):263-9. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Tong Z, Board PG, Anders MW: Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. Biochem J. 1998 Apr 15;331 ( Pt 2):371-4. [PubMed
]
- Blackburn AC, Tzeng HF, Anders MW, Board PG: Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis. Pharmacogenetics. 2000 Feb;10(1):49-57. [PubMed
]
- Polekhina G, Board PG, Blackburn AC, Parker MW: Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry. 2001 Feb 13;40(6):1567-76. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6098 |
| Enzyme 16 Name |
Glutathione S-transferase theta-2 |
| Enzyme 16 Synonyms |
- GST class-theta-2
|
| Enzyme 16 Gene Name |
GSTT2 |
| Enzyme 16 Protein Sequence |
>Glutathione S-transferase theta-2
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDG
DFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLG
PLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALG
YELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRI
ARIP
|
| Enzyme 16 Number of Residues |
244 |
| Enzyme 16 Molecular Weight |
27507 |
| Enzyme 16 Theoretical pI |
6.36 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 16 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
Not Available |
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
601918  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P30712  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
GSTT2_HUMAN  |
| Enzyme 16 PDB ID |
3LJR  |
| Enzyme 16 PDB File |
Show |
| Enzyme 16 3D Structure |
|
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>735 bp
ATGGGCCTAGAGCTGTTTCTTGACCTGGTGTCCCAGCCCAGCCGCGCCGTCTACATCTTC
GCCAAGAAGAATGGCATCCCCTTAGAGCTGCGCACCGTGGATTTGGTCAAAGGGCAGCAC
AAGAGCAAGGAGTTCTTGCAGATCAACAGCCTGGGGAAACTGCCGACGCTCAAGGATGGT
GATTTCATCTTGACCGAAAGCTCGGCCATCCTGATTTACCTGAGCTGTAAGTACCAGACG
CCGGACCACTGGTATCCATCTGACCTGCAGGCTCGTGCCCGTGTTCATGAGTACCTGGGC
TGGCATGCCGACTGCATCCGTGGCACCTTTGGTATACCCCTGTGGGTCCAGGTGTTGGGG
CCACTCATTGGGGTCCAGGTGCCCGAGGAGAAGGTGGAACGCAACAGGACTGCCATGGAC
CAGGCCCTGCAATGGCTGGAGGACAAGTTCCTGGGGGACAGGCCCTTCCTCGCTGGCCAG
CAGGTGACACTGGCTGATCTCATGGCCCTGGAGGAGCTGATGCAGCCGGTGGCTCTCGGC
TACGAACTGTTTGAGGGACGGCCACGACTGGCAGCATGGCGTGGACGAGTGGAGGCTTTC
CTGGGTGCTGAGCTATGCCAGGAGGCCCACAGCATCATCTTGAGCATCCTGGAACAGGCG
GCCAAGAAAACCCTCCCAACACCCTCACCAGAGGCCTATCAGGCTATGCTGCTTCGAATC
GCCAGGATCCCCTGA
|
| Enzyme 16 GenBank Gene ID |
L38503  |
| Enzyme 16 GeneCard ID |
GSTT2  |
| Enzyme 16 GenAtlas ID |
GSTT2  |
| Enzyme 16 HGNC ID |
HGNC:4642  |
| Enzyme 16 Chromosome Location |
22 |
| Enzyme 16 Locus |
22q11.2|22q11.23 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Tan KL, Webb GC, Baker RT, Board PG: Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22. Genomics. 1995 Jan 20;25(2):381-7. [PubMed
]
- Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Hussey AJ, Hayes JD: Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem J. 1992 Sep 15;286 ( Pt 3):929-35. [PubMed
]
- Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed
]
- Rossjohn J, McKinstry WJ, Oakley AJ, Verger D, Flanagan J, Chelvanayagam G, Tan KL, Board PG, Parker MW: Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure. 1998 Mar 15;6(3):309-22. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6100 |
| Enzyme 17 Name |
Glutathione S-transferase Mu 4 |
| Enzyme 17 Synonyms |
- GSTM4-4
- GST class-mu 4
- GTS-Mu2
|
| Enzyme 17 Gene Name |
GSTM4 |
| Enzyme 17 Protein Sequence |
>Glutathione S-transferase Mu 4
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
|
| Enzyme 17 Number of Residues |
218 |
| Enzyme 17 Molecular Weight |
25562 |
| Enzyme 17 Theoretical pI |
5.69 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1- chloro-2,4-dinitrobenzene |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
Not Available |
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
306819  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q03013  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
GSTM4_HUMAN  |
| Enzyme 17 PDB ID |
4GTU  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTAGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
|
| Enzyme 17 GenBank Gene ID |
M96234  |
| Enzyme 17 GeneCard ID |
GSTM4  |
| Enzyme 17 GenAtlas ID |
GSTM4  |
| Enzyme 17 HGNC ID |
HGNC:4636  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1p13.3 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Comstock KE, Johnson KJ, Rifenbery D, Henner WD: Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4. J Biol Chem. 1993 Aug 15;268(23):16958-65. [PubMed
]
- Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed
]
- Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed
]
- Taylor JB, Oliver J, Sherrington R, Pemble SE: Structure of human glutathione S-transferase class Mu genes. Biochem J. 1991 Mar 1;274 ( Pt 2):587-93. [PubMed
]
- Comstock KE, Widersten M, Hao XY, Henner WD, Mannervik B: A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Arch Biochem Biophys. 1994 Jun;311(2):487-95. [PubMed
]
- Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6101 |
| Enzyme 18 Name |
Glutathione S-transferase Mu 5 |
| Enzyme 18 Synonyms |
- GSTM5-5
- GST class-mu 5
|
| Enzyme 18 Gene Name |
GSTM5 |
| Enzyme 18 Protein Sequence |
>Glutathione S-transferase Mu 5
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLN
LKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
|
| Enzyme 18 Number of Residues |
218 |
| Enzyme 18 Molecular Weight |
25675 |
| Enzyme 18 Theoretical pI |
7.49 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
468260  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P46439  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
GSTM5_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>657 bp
ATGCCCATGACTCTGGGGTACTGGGACATCCGTGGGCTGGCCCACGCCATCCGCTTGCTC
CTGGAATACACAGACTCAAGCTATGTGGAAAAGAAGTACACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAATGCCATCCTGCGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGTTATGGATAACCACATGGAGCTGGTCAGACTGTGCTATGACCCAGATTTT
GAGAAACTGAAGCCAAAATACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAGACAAGATCACCTTTGTGGATTTCCTTGCC
TATGATGTCCTTGACATGAAGCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCTAAAC
TTGAAGGACTTCATCTCCCGCTTTGAGGGTTTGAAGAAGATCTCTGCCTACATGAAGTCC
AGCCAATTCCTCCGAGGTCTTTTGTTTGGAAAGTCAGCTACATGGAACAGCAAATAG
|
| Enzyme 18 GenBank Gene ID |
L02321  |
| Enzyme 18 GeneCard ID |
GSTM5  |
| Enzyme 18 GenAtlas ID |
GSTM5  |
| Enzyme 18 HGNC ID |
HGNC:4637  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
1p13.3 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Takahashi Y, Campbell EA, Hirata Y, Takayama T, Listowsky I: A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5. J Biol Chem. 1993 Apr 25;268(12):8893-8. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6102 |
| Enzyme 19 Name |
Microsomal glutathione S-transferase 2 |
| Enzyme 19 Synonyms |
- Microsomal GST- 2
- Microsomal GST-II
|
| Enzyme 19 Gene Name |
MGST2 |
| Enzyme 19 Protein Sequence |
>Microsomal glutathione S-transferase 2
MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFY
PIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTL
LGALGIANSFLDEYLDLNIAKKLRRQF
|
| Enzyme 19 Number of Residues |
147 |
| Enzyme 19 Molecular Weight |
16621 |
| Enzyme 19 Theoretical pI |
9.88 |
| Enzyme 19 GO Classification |
| Function |
- enzyme activator activity
- enzyme regulator activity
|
| Process |
- carboxylic acid metabolism
- cellular metabolism
- fatty acid metabolism
- icosanoid metabolism
- leukotriene metabolism
- metabolism
- organic acid metabolism
- physiological process
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Can catalyze the production of LTC4 from LTA4 and reduced glutathione. Can catalyze the conjugation of 1-chloro-2,4- dinitrobenzene with reduced glutathione |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
Not Available |
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
1747521  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q99735  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
MGST2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>444 bp
ATGGCCGGGAACTCGATCCTGCTGGCTGCTGTCTCTATTCTCTCGGCCTGTCAGCAAAGT
TATTTTGCTTTGCAAGTTGGAAAGGCAAGATTAAAATACAAAGTTACGCCCCCAGCAGTC
ACTGGGTCACCAGAGTTTGAGAGAGTATTTCGGGCACAACAAAACTGTGTGGAGTTTTAT
CCTATATTCATAATTACATTGTGGATGGCTGGGTGGTATTTCAACCAAGTTTTTGCTACT
TGTCTGGGTCTGGTGTACATATATGGCCGTCACCTATACTTCTGGGGATATTCAGAAGCT
GCTAAAAAACGGATCACCGGTTTCCGACTGAGTCTGGGGATTTTGGCCTTGTTGACCCTC
CTAGGTGCCCTGGGAATTGCAAACAGCTTTCTGGATGAATATCTGGACCTCAATATTGCC
AAGAAACTGAGGCGGCAATTCTAA
|
| Enzyme 19 GenBank Gene ID |
U77604  |
| Enzyme 19 GeneCard ID |
MGST2  |
| Enzyme 19 GenAtlas ID |
MGST2  |
| Enzyme 19 HGNC ID |
HGNC:7063  |
| Enzyme 19 Chromosome Location |
4 |
| Enzyme 19 Locus |
4q28.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Jakobsson PJ, Mancini JA, Ford-Hutchinson AW: Identification and characterization of a novel human microsomal glutathione S-transferase with leukotriene C4 synthase activity and significant sequence identity to 5-lipoxygenase-activating protein and leukotriene C4 synthase. J Biol Chem. 1996 Sep 6;271(36):22203-10. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6103 |
| Enzyme 20 Name |
Glutathione transferase omega-1 |
| Enzyme 20 Synonyms |
- GSTO 1-1
|
| Enzyme 20 Gene Name |
GSTO1 |
| Enzyme 20 Protein Sequence |
>Glutathione transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
|
| Enzyme 20 Number of Residues |
241 |
| Enzyme 20 Molecular Weight |
27566 |
| Enzyme 20 Theoretical pI |
6.54 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 20 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 20 Specific Function |
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
2393722  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P78417  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
GSTO1_HUMAN  |
| Enzyme 20 PDB ID |
1EEM  |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>726 bp
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA
|
| Enzyme 20 GenBank Gene ID |
U90313  |
| Enzyme 20 GeneCard ID |
GSTO1  |
| Enzyme 20 GenAtlas ID |
GSTO1  |
| Enzyme 20 HGNC ID |
HGNC:13312  |
| Enzyme 20 Chromosome Location |
10 |
| Enzyme 20 Locus |
10q25.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J: Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem. 2000 Aug 11;275(32):24798-806. [PubMed
]
- Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed
]
- Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed
]
- Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6104 |
| Enzyme 21 Name |
Glutathione S-transferase A5 |
| Enzyme 21 Synonyms |
- Glutathione S-transferase A5-5
- GST class-alpha member 5
|
| Enzyme 21 Gene Name |
GSTA5 |
| Enzyme 21 Protein Sequence |
>Glutathione S-transferase A5
MAEKPKLHYSNARGSMESIRWLLAAAGVELEEKFLESAEDLDKLRNDGSLLFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDMKERALIDMYTEGIVDLTEMILLLLICQPEERDAK
TALVKEKIKNRYFPAFEKVLKSHRQDYLVGNKLSWADIHLVELFYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSQRKPPMDEKSLEEARKIFRF
|
| Enzyme 21 Number of Residues |
222 |
| Enzyme 21 Molecular Weight |
25722 |
| Enzyme 21 Theoretical pI |
8.37 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
RX + glutathione = HX + R-S-glutathione |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
23197582  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q7RTV2  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
GSTA5_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATGCACGGGGCAGTATGGAGTCCATTCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTGGAAGAGAAATTTCTAGAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGGAGTTTGCTGTTCCAGCAAGTACCAATGGTTGAGATT
GACGGGATGAAGCTGGTGCAGACCAGAGCCATTCTTAACTACATTGCCAGCAAATACAAC
CTTTATGGGAAAGACATGAAGGAGAGAGCCCTGATTGATATGTACACAGAAGGTATAGTA
GATTTGACTGAAATGATCCTTCTTCTGCTCATATGTCAACCAGAGGAAAGAGATGCCAAG
ACTGCCTTGGTCAAAGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACAGACAAGACTACCTTGTTGGCAACAAGCTGAGCTGGGCTGACATTCACCTG
GTGGAACTTTTCTACTACGTGGAAGAGCTTGACTCGAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTGCAGCCT
GGCAGCCAGAGAAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 21 GenBank Gene ID |
BK000212  |
| Enzyme 21 GeneCard ID |
GSTA5  |
| Enzyme 21 GenAtlas ID |
GSTA5  |
| Enzyme 21 HGNC ID |
HGNC:19662  |
| Enzyme 21 Chromosome Location |
6 |
| Enzyme 21 Locus |
6p12.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Morel F, Rauch C, Coles B, Le Ferrec E, Guillouzo A: The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter. Pharmacogenetics. 2002 Jun;12(4):277-86. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6105 |
| Enzyme 22 Name |
Glutathione S-transferase A2 |
| Enzyme 22 Synonyms |
- GTH2
- HA subunit 2
- GST- gamma
- GSTA2-2
- GST class-alpha member 2
|
| Enzyme 22 Gene Name |
GSTA2 |
| Enzyme 22 Protein Sequence |
>Glutathione S-transferase A2
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
|
| Enzyme 22 Number of Residues |
222 |
| Enzyme 22 Molecular Weight |
25664 |
| Enzyme 22 Theoretical pI |
9.07 |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
306811  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P09210  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
GSTA2_HUMAN  |
| Enzyme 22 PDB ID |
1AGS  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 22 GenBank Gene ID |
M16594  |
| Enzyme 22 GeneCard ID |
GSTA2  |
| Enzyme 22 GenAtlas ID |
GSTA2  |
| Enzyme 22 HGNC ID |
HGNC:4627  |
| Enzyme 22 Chromosome Location |
6 |
| Enzyme 22 Locus |
6p12.1 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed
]
- Rohrdanz E, Nguyen T, Pickett CB: Isolation and characterization of the human glutathione S-transferase A2 subunit gene. Arch Biochem Biophys. 1992 Nov 1;298(2):747-52. [PubMed
]
- Klone A, Hussnatter R, Sies H: Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. Biochem J. 1992 Aug 1;285 ( Pt 3):925-8. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed
]
- Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed
]
- Tetlow N, Liu D, Board P: Polymorphism of human Alpha class glutathione transferases. Pharmacogenetics. 2001 Oct;11(7):609-17. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6106 |
| Enzyme 23 Name |
Glutathione peroxidase 6 precursor |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
GPX6 |
| Enzyme 23 Protein Sequence |
>Glutathione peroxidase 6 precursor
MFQQFQASCLVLFFLVGFAQQTLKPQNRKVDCNKGVTGTIYEYGALTLNGEEYIQFKQFA
GKHVLFVNVAAYCGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGLK
YVCPGSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSSSQLFWEPMKVHDIR
WNFEKFLVGPDGVPVMHWFHQAPVSTVKSDILEYLKQFNTH
|
| Enzyme 23 Number of Residues |
221 |
| Enzyme 23 Molecular Weight |
24924 |
| Enzyme 23 Theoretical pI |
6.66 |
| Enzyme 23 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 23 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 23 Specific Function |
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
Not Available |
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
32492913  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P59796  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
GPX6_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>666 bp
ATGTTCCAGCAGTTCCAGGCCTCCTGTCTTGTCCTGTTTTTCCTGGTTGGCTTTGCTCAG
CAGACCCTAAAGCCTCAAAATAGGAAGGTGGATTGCAACAAAGGGGTAACAGGCACCATC
TATGAGTATGGAGCCCTCACCCTCAACGGCGAGGAGTACATCCAATTCAAGCAGTTTGCA
GGCAAGCACGTCCTGTTTGTCAATGTGGCCGCCTATTGAGGCTTGGCAGCTCAGTATCCT
GAACTGAATGCACTACAGGAGGAGCTGAAGAATTTTGGTGTCATTGTGTTGGCCTTTCCC
TGCAACCAGTTTGGAAAACAAGAACCAGGAACAAACTCAGAAATACTTCTTGGTCTCAAG
TATGTGTGTCCAGGTAGTGGCTTTGTCCCCAGTTTCCAGCTCTTTGAGAAAGGGGATGTG
AATGGAGAAAAAGAACAGAAGGTCTTTACTTTCCTGAAGAACTCCTGCCCTCCGACCTCT
GATCTTTTGGGCTCATCAAGCCAACTCTTCTGGGAGCCCATGAAGGTCCATGATATCCGC
TGGAACTTTGAGAAATTTCTGGTGGGGCCCGATGGAGTCCCTGTCATGCATTGGTTCCAC
CAGGCTCCAGTCAGCACAGTCAAGTCAGACATCCTGGAGTACCTAAAGCAGTTCAATACC
CACTAG
|
| Enzyme 23 GenBank Gene ID |
AY324826  |
| Enzyme 23 GeneCard ID |
GPX6  |
| Enzyme 23 GenAtlas ID |
GPX6  |
| Enzyme 23 HGNC ID |
HGNC:4558  |
| Enzyme 23 Chromosome Location |
6 |
| Enzyme 23 Locus |
6p22.1 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6107 |
| Enzyme 24 Name |
Glutathione S-transferase A3 |
| Enzyme 24 Synonyms |
- Glutathione S-transferase A3-3
- GST class-alpha member 3
|
| Enzyme 24 Gene Name |
GSTA3 |
| Enzyme 24 Protein Sequence |
>Glutathione S-transferase A3
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
|
| Enzyme 24 Number of Residues |
222 |
| Enzyme 24 Molecular Weight |
25302 |
| Enzyme 24 Theoretical pI |
9.69 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
951352  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q16772  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
GSTA3_HUMAN  |
| Enzyme 24 PDB ID |
1TDI  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>688 bp
AAACCAGAAGACTGTTACCATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGG
CAGAATGGAGCCCATCCGGTGGCTCTTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATT
TATAGGATCTGCAGAAGATTTGGGAAAGTTAAGAAATGATGGAAGTTTGATGTTCCAGCA
AGTGCCAATGGTTGAGATTGATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTA
CATTGCCAGCAAATACAACCTCTATGGGAAAGACATAAAGGAGAGAGCCCTAATTGATAT
GTATACAGAAGGTATGGCAGATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCCAGC
TGAGGAAAAAGATGCCAAGATTGCCTTGATCAAAGAGAAAATAAAAAGTCGCTATTTCCC
TGCCTTCGAAAAAGTGTTACAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAG
CCGGGCTGACATTAGCCTGGTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCT
TATCTCCAACTTCCCTCTGCTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGT
GAAGAAGTTTCTACAGCCTGGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGA
AGAAGCCAGAAAGATTTTCAGGTTTTAA
|
| Enzyme 24 GenBank Gene ID |
L13275  |
| Enzyme 24 GeneCard ID |
GSTA3  |
| Enzyme 24 GenAtlas ID |
GSTA3  |
| Enzyme 24 HGNC ID |
HGNC:4628  |
| Enzyme 24 Chromosome Location |
6 |
| Enzyme 24 Locus |
6p12.1 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Suzuki T, Johnston PN, Board PG: Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. Genomics. 1993 Dec;18(3):680-6. [PubMed
]
- Johansson AS, Mannervik B: Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J Biol Chem. 2001 Aug 31;276(35):33061-5. Epub 2001 Jun 20. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Board PG: Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochem J. 1998 Mar 1;330 ( Pt 2):827-31. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
6108 |
| Enzyme 25 Name |
Glutathione S-transferase A4 |
| Enzyme 25 Synonyms |
- Glutathione S-transferase A4-4
- GST class-alpha member 4
|
| Enzyme 25 Gene Name |
GSTA4 |
| Enzyme 25 Protein Sequence |
>Glutathione S-transferase A4
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
|
| Enzyme 25 Number of Residues |
222 |
| Enzyme 25 Molecular Weight |
25705 |
| Enzyme 25 Theoretical pI |
8.72 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE) |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
2597924  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
O15217  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
GSTA4_HUMAN  |
| Enzyme 25 PDB ID |
1GUM  |
| Enzyme 25 PDB File |
Show |
| Enzyme 25 3D Structure |
|
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>669 bp
ATGGCAGCAAGGCCCAAGCTCCACTATCCCAACGGAAGAGGCCGGATGGAGTCCGTGAGA
TGGGTTTTAGCTGCCGCCGGAGTCGAGTTTGATGAAGAATTTCTGGAAACAAAAGAACAG
TTGTACAAGTTGCAGGATGGTAACCACCTGCTGTTCCAACAAGTGCCCATGGTTGAAATT
GACGGGATGAAGTTGGTACAGACCCGAAGCATTCTCCACTACATAGCAGACAAGCACAAT
CTCTTTGGCAAGAACCTCAAGGAGAGAACCCTGATTGACATGTACGTGGAGGGGACACTG
GATCTGCTGGAACTGCTTATCATGCATCCTTTCTTAAAACCAGATGATCAGCAAAAGGAA
GTGGTTAACATGGCCCAGAAGGCTATAATTAGATACTTTCCTGTGTTTGAAAAGATTTTA
AGGGGTCACGGACAAAGCTTTCTTGTTGGTAATCAGCTGAGCCTTGCAGATGTGATTTTA
CTCCAAACCATTTTAGCTCTAGAAGAGAAAATTCCTAATATCCTGTCTGCATTTCCTTTC
CTCCAGGAATACACAGTGAAACTAAGTAATATCCCTACAATTAAGAGATTCCTTGAACCT
GGCAGCAAGAAGAAGCCTCCCCCTGATGAAATTTATGTGAGAACCGTCTACAACATCTTT
AGGCCATAA
|
| Enzyme 25 GenBank Gene ID |
Y13047  |
| Enzyme 25 GeneCard ID |
GSTA4  |
| Enzyme 25 GenAtlas ID |
GSTA4  |
| Enzyme 25 HGNC ID |
HGNC:4629  |
| Enzyme 25 Chromosome Location |
6 |
| Enzyme 25 Locus |
6p12.1 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Hubatsch I, Ridderstrom M, Mannervik B: Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem J. 1998 Feb 15;330 ( Pt 1):175-9. [PubMed
]
- Board PG: Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochem J. 1998 Mar 1;330 ( Pt 2):827-31. [PubMed
]
- Liu S, Stoesz SP, Pickett CB: Identification of a novel human glutathione S-transferase using bioinformatics. Arch Biochem Biophys. 1998 Apr 15;352(2):306-13. [PubMed
]
- Desmots F, Rauch C, Henry C, Guillouzo A, Morel F: Genomic organization, 5'-flanking region and chromosomal localization of the human glutathione transferase A4 gene. Biochem J. 1998 Dec 1;336 ( Pt 2):437-42. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Bruns CM, Hubatsch I, Ridderstrom M, Mannervik B, Tainer JA: Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J Mol Biol. 1999 May 7;288(3):427-39. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
6109 |
| Enzyme 26 Name |
Glutathione peroxidase 1 |
| Enzyme 26 Synonyms |
- GSHPx-1
- GPx-1
- Cellular glutathione peroxidase
|
| Enzyme 26 Gene Name |
GPX1 |
| Enzyme 26 Protein Sequence |
>Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLCGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
|
| Enzyme 26 Number of Residues |
201 |
| Enzyme 26 Molecular Weight |
21899 |
| Enzyme 26 Theoretical pI |
6.50 |
| Enzyme 26 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 26 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 26 Specific Function |
Protects the hemoglobin in erythrocytes from oxidative breakdown |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
Not Available |
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
577777  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P07203  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
GPX1_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>606 bp
ATGTGTGCTGCTCGGCTAGCGGCGGCGGCGGCCCAGTCGGTGTATGCCTTCTCGGCGCGC
CCGTTGGCCGGCGGGGAGCCTGTGAGCCTGGGCTCCCTGCGGGGCAAGGTACTACTTATC
GAGAATGTGGCGTCCCTCTGAGGCACCACGGTCCGGGACTACACCCAGATGAACGAGCTG
CAGCGGCGCCTCGGACCCCGGGGCCTGGTGGTGCTCGGCTTCCCGTGCAACCAGTTTGGG
CATCAGGAGAACGCCAAGAACGAAGAGATTCTGAATTCCCTCAAGTACGTCCGGCCTGGT
GGTGGGTTCGAGCCCAACTTCATGCTCTTCGAGAAGTGCGAGGTGAACGGTGCGGGGGCG
CACCCTCTCTTCGCCTTCCTGCGGGAGGCCCTGCCAGCTCCCAGCGACGACGCCACCGCG
CTTATGACCGACCCCAAGCTCATCACCTGGTCTCCGGTGTGTCGCAACGATGTTGCCTGG
AACTTTGAGAAGTTCCTGGTGGGCCCTGACGGTGTGCCCCTACGCAGGTACAGCCGCCGC
TTCCAGACCATTGACATCGAGCCTGACATCGAAGCCCTGCTGTCTCAAGGGCCCAGCTGT
GCCTAG
|
| Enzyme 26 GenBank Gene ID |
Y00433  |
| Enzyme 26 GeneCard ID |
GPX1  |
| Enzyme 26 GenAtlas ID |
GPX1  |
| Enzyme 26 HGNC ID |
HGNC:4553  |
| Enzyme 26 Chromosome Location |
3 |
| Enzyme 26 Locus |
3p21.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Sukenaga Y, Ishida K, Takeda T, Takagi K: cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178. [PubMed
]
- Ishida K, Morino T, Takagi K, Sukenaga Y: Nucleotide sequence of a human gene for glutathione peroxidase. Nucleic Acids Res. 1987 Dec 10;15(23):10051. [PubMed
]
- Mullenbach GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA: Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 1987 Jul 10;15(13):5484. [PubMed
]
- Chada S, Le Beau MM, Casey L, Newburger PE: Isolation and chromosomal localization of the human glutathione peroxidase gene. Genomics. 1990 Feb;6(2):268-71. [PubMed
]
- Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed
]
- Forsberg L, de Faire U, Morgenstern R: Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1. Hum Mutat. 1999;13(4):294-300. [PubMed
]
- Kote-Jarai Z, Durocher F, Edwards SM, Hamoudi R, Jackson RA, Ardern-Jones A, Murkin A, Dearnaley DP, Kirby R, Houlston R, Easton DF, Eeles R: Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer. Prostate Cancer Prostatic Dis. 2002;5(3):189-92. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
6110 |
| Enzyme 27 Name |
Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor |
| Enzyme 27 Synonyms |
- PHGPx
- GPX-4
|
| Enzyme 27 Gene Name |
GPX4 |
| Enzyme 27 Protein Sequence |
>Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
|
| Enzyme 27 Number of Residues |
197 |
| Enzyme 27 Molecular Weight |
22128 |
| Enzyme 27 Theoretical pI |
8.41 |
| Enzyme 27 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 27 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 27 Specific Function |
Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage |
| Enzyme 27 Pathways |
|
| Enzyme 27 Reactions |
- 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
Not Available |
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
825667  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P36969  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
GPX4_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>594 bp
ATGAGCCTCGGCCGCCTTTGCCGCCTACTGAAGCCGGCGCTGCTCTGTGGGGCTCTGGCC
GCGCCTGGCCTGGCCGGGACCATGTGCGCGTCCCGGGACGACTGGCGCTGTGCGCGCTCC
ATGCACGAGTTTTCCGCCAAGGACATCGACGGGCACATGGTTAACCTGGACAAGTACCGG
GGCTTCGTGTGCATCGTCACCAACGTGGCCTCCCAGTGAGGCAAGACCGAAGTAAACTAC
ACTCAGCTCGTCGACCTGCACGCCCGATACGCTGAGTGTGGTTTGCGGATCCTGGCCTTC
CCGTGTAACCAGTTCGGGAAGCAGGAGCCAGGGAGTAACGAAGAGATCAAAGAGTTCGCC
GCGGGCTACAACGTCAAATTCGATATGTTCAGCAAGATCTGCGTGAACGGGGACGACGCC
CACCCGCTGTGGAAGTGGATGAAGATCCAACCCAAGGGCAAGGGCATCCTGGGAAATGCC
ATCAAGTGGAACTTCACCAAGTTCCTCATCGACAAGAACGGCTGCGTGGTGAAGCGCTAC
GGACCCATGGAGGAGCCCCTGGTGATAGAGAAGGACCTGCCCCACTATTTCTAG
|
| Enzyme 27 GenBank Gene ID |
X71973  |
| Enzyme 27 GeneCard ID |
GPX4  |
| Enzyme 27 GenAtlas ID |
GPX4  |
| Enzyme 27 HGNC ID |
HGNC:4556  |
| Enzyme 27 Chromosome Location |
19 |
| Enzyme 27 Locus |
19p13.3 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Esworthy RS, Doan K, Doroshow JH, Chu FF: Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 1994 Jul 8;144(2):317-8. [PubMed
]
- Kelner MJ, Montoya MA: Structural organization of the human selenium-dependent phospholipid hydroperoxide glutathione peroxidase gene (GPX4): chromosomal localization to 19p13.3. Biochem Biophys Res Commun. 1998 Aug 10;249(1):53-5. [PubMed
]
- Maiorino M, Bosello V, Ursini F, Foresta C, Garolla A, Scapin M, Sztajer H, Flohe L: Genetic variations of gpx-4 and male infertility in humans. Biol Reprod. 2003 Apr;68(4):1134-41. Epub 2002 Nov 27. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
6111 |
| Enzyme 28 Name |
Glutathione peroxidase 3 precursor |
| Enzyme 28 Synonyms |
- GSHPx-3
- GPx-3
- Plasma glutathione peroxidase
- GSHPx-P
- Extracellular glutathione peroxidase
- GPx-P
|
| Enzyme 28 Gene Name |
GPX3 |
| Enzyme 28 Protein Sequence |
>Glutathione peroxidase 3 precursor
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYCGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
|
| Enzyme 28 Number of Residues |
226 |
| Enzyme 28 Molecular Weight |
25506 |
| Enzyme 28 Theoretical pI |
8.19 |
| Enzyme 28 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 28 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 28 Specific Function |
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
Not Available |
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
2160390  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P22352  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
GPX3_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>681 bp
ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA
|
| Enzyme 28 GenBank Gene ID |
D00632  |
| Enzyme 28 GeneCard ID |
GPX3  |
| Enzyme 28 GenAtlas ID |
GPX3  |
| Enzyme 28 HGNC ID |
HGNC:4555  |
| Enzyme 28 Chromosome Location |
5 |
| Enzyme 28 Locus |
5q23 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J: Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem (Tokyo). 1990 Aug;108(2):145-8. [PubMed
]
- Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed
]
- Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T: The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32. Gene. 1994 Aug 5;145(2):293-7. [PubMed
]
- Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol. 2000 Sep;23(3):350-4. [PubMed
]
- Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow JH: Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys. 1991 May 1;286(2):330-6. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
6112 |
| Enzyme 29 Name |
Glutathione transferase omega-2 |
| Enzyme 29 Synonyms |
- GSTO-2
|
| Enzyme 29 Gene Name |
GSTO2 |
| Enzyme 29 Protein Sequence |
>Glutathione transferase omega-2
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKP
EWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELF
CKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWP
WFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDF
GLC
|
| Enzyme 29 Number of Residues |
243 |
| Enzyme 29 Molecular Weight |
28254 |
| Enzyme 29 Theoretical pI |
7.62 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 29 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 29 Specific Function |
RX + glutathione = HX + R-S-glutathione |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
37777744  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q9H4Y5  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
GSTO2_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>732 bp
ATGTCTGGGGATGCGACCAGGACCCTGGGGAAAGGAAGCCAGCCCCCAGGGCCAGTCCCG
GAGGGGCTGATCCGCATCTACAGCATGAGGTTCTGCCCCTATTCTCACAGGACCCGCCTC
GTCCTCAAGGCCAAAGACATCAGACATGAAGTGGTCAACATTAACCTGAGAAACAAGCCT
GAATGGTACTATACAAAGCACCCTTTTGGCCACATTCCTGTCCTGGAGACCAGCCAATGT
CAACTGATCTATGAATCTGTTATTGCTTGTGAGTACCTGGATGATGCTTATCCAGGAAGG
AAGCTGTTTCCATATGACCCTTATGAACGAGCTCGCCAAAAGATGTTATTGGAGCTATTT
TGTAAGGTCCCACATTTGACCAAGGAGTGCCTGGTAGCGTTGAGATGTGGGAGAGAATGC
ACTAATCTGAAGGCAGCCCTGCGTCAGGAATTCAGCAACCTGGAAGAGATTCTTGAGTAT
CAGAACACCACCTTCTTTGGTGGAACCTGTATATCCATGATTGATTACCTCCTCTGGCCC
TGGTTTGAGCGGCTGGATGTGTATGGGATACTGGACTGTGTGAGCCACACGCCAGCCCTG
CGGCTCTGGATATCAGCCATGAAGTGGGACCCCACAGTCTGTGCTCTTCTCATGGATAAG
AGCATTTTCCAGGGCTTCTTGAATCTCTATTTTCAGAACAACCCTAATGCCTTTGACTTT
GGGCTGTGCTGA
|
| Enzyme 29 GenBank Gene ID |
AY350731  |
| Enzyme 29 GeneCard ID |
GSTO2  |
| Enzyme 29 GenAtlas ID |
GSTO2  |
| Enzyme 29 HGNC ID |
HGNC:23064  |
| Enzyme 29 Chromosome Location |
10 |
| Enzyme 29 Locus |
10q25.1 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
6113 |
| Enzyme 30 Name |
Glutathione S-transferase theta-1 |
| Enzyme 30 Synonyms |
- GST class-theta-1
- Glutathione transferase T1-1
|
| Enzyme 30 Gene Name |
GSTT1 |
| Enzyme 30 Protein Sequence |
>Glutathione S-transferase theta-1
MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDG
DFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMF
PVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGA
GCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
|
| Enzyme 30 Number of Residues |
240 |
| Enzyme 30 Molecular Weight |
27335 |
| Enzyme 30 Theoretical pI |
7.60 |
| Enzyme 30 GO Classification |
Not Available |
| Enzyme 30 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 30 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2- epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4- nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
Not Available |
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
510905  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P30711  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
GSTT1_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>723 bp
ATGGGTCTGGAGCTCTACCTGGACCTGCTGTCCCAGCCCTGCCGCGCTGTTTACATCTTT
GCCAAGAAGAACGACATTCCCTTCGAGCTGCGCATCGTGGATCTGATTAAAGGTCAGCAC
TTAAGCGATGCCTTTGCCCAGGTGAACCCCCTCAAGAAGGTGCCGGCCTTGAAGGACGGG
GACTTCACCTTGACGGAGAGTGTGGCCATCCTGCTCTACCTGACGCGCAAATATAAGGTC
CCTGACTACTGGTACCCTCAGGACCTGCAGGCCCGTGCCCGTGTGGATGAGTACCTGGCA
TGGCAGCACACGACTCTGCGGAGAAGCTGCCTCCGGGCCTTGTGGCATAAGGTGATGTTC
CCTGTGTTCCTGGGTGGGCCAGTATCTCCCCAGACACTGGCAGCCACCCTGGCAGAGTTG
GATGTGACCCTGCAGTTGCTCGAGGACAAGTTCCTCCAGAACAAGGCCTTCCTTACTGGT
CCTCACATCTCCTTAGCTGACCTCGTAGCCATCACGGAGCTGATGCATCCCGTGGGTGCT
GGCTGCCAAGTCTTCGAAGGCCGACCCAAGCTGGCCACATGGCGGCAGCGCGTGGAGGCA
GCAGTGGGGGAGGACCTCTTCCAGGAGGCCCATGAGGTCATTCTGAAGGCCAAGGACTTC
CCACCTGCAGACCCCACCATAAAGCAGAAGCTGATGCCCTGGGTGCTGGCCATGATCCGG
TGA
|
| Enzyme 30 GenBank Gene ID |
X79389  |
| Enzyme 30 GeneCard ID |
GSTT1  |
| Enzyme 30 GenAtlas ID |
GSTT1  |
| Enzyme 30 HGNC ID |
HGNC:4641  |
| Enzyme 30 Chromosome Location |
22 |
| Enzyme 30 Locus |
22q11.23 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Pemble S, Schroeder KR, Spencer SR, Meyer DJ, Hallier E, Bolt HM, Ketterer B, Taylor JB: Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem J. 1994 May 15;300 ( Pt 1):271-6. [PubMed
]
- Jemth P, Mannervik B: Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Arch Biochem Biophys. 1997 Dec 15;348(2):247-54. [PubMed
]
- Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Meyer DJ, Coles B, Pemble SE, Gilmore KS, Fraser GM, Ketterer B: Theta, a new class of glutathione transferases purified from rat and man. Biochem J. 1991 Mar 1;274 ( Pt 2):409-14. [PubMed
]
- Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
6114 |
| Enzyme 31 Name |
Glutathione peroxidase 2 |
| Enzyme 31 Synonyms |
- GSHPx-2
- GPx-2
- Glutathione peroxidase-gastrointestinal
- GSHPx-GI
- Glutathione peroxidase- related protein 2
- Gastrointestinal glutathione peroxidase
- GPRP
|
| Enzyme 31 Gene Name |
GPX2 |
| Enzyme 31 Protein Sequence |
>Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLCGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
|
| Enzyme 31 Number of Residues |
190 |
| Enzyme 31 Molecular Weight |
21907 |
| Enzyme 31 Theoretical pI |
7.84 |
| Enzyme 31 GO Classification |
| Function |
- antioxidant activity
- glutathione peroxidase activity
- peroxidase activity
|
| Process |
- cellular metabolism
- metabolism
- oxygen and reactive oxygen species metabolism
- physiological process
- response to oxidative stress
|
| Component |
| — |
|
| Enzyme 31 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 31 Specific Function |
Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
4902773  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P18283  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
GPX2_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>573 bp
ATGGCTTTCATTGCCAAGTCCTTCTATGACCTCAGTGCCATCAGCCTGGATGGGGAGAAG
GTAGATTTCAATACGTTCCGGGGCAGGGCCGTGCTGATTGAGAATGTGCGTTCGCTCTGA
GGCACAACCACCCGGGACTTCACCCAGCTCAACGAGCTGCAATGCCGCTTTCCCAGGCGC
CTGGTGGTCCTTGGCTTCCCTTGCAACCAATTTGGACATCAGGAGAACAGTCAGAATGAG
GAGATCCTGAACAGTCTCAAGTATGTCCGTCCTGGGGGTGGATACCAGCCCACCTTCACC
CTTGTCCAAAAATGTGAGGTGAATGGGCAGAACGAGCATCCTGTCTTCGCCTACCTGAAG
GACAAGCTCCCCTACCCTTATGATGACCCATTTTCCCTCATGACCGATCCCAAGCTCATC
ATTTGGAGCCCTGTGCGCCGCTCAGATGTGGCCTGGAACTTTGAGAAGTTCCTCATAGGG
CCGGAGGGAGAGCCCTTCCGACGCTACAGCCGCACCTTCCCAACCATCAACATTGAGCCT
GACATCAAGCGCCTCCTTAAAGTTGCCATATAG
|
| Enzyme 31 GenBank Gene ID |
X53463  |
| Enzyme 31 GeneCard ID |
GPX2  |
| Enzyme 31 GenAtlas ID |
GPX2  |
| Enzyme 31 HGNC ID |
HGNC:4554  |
| Enzyme 31 Chromosome Location |
14 |
| Enzyme 31 Locus |
14q24.1 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Akasaka M, Mizoguchi J, Takahashi K: A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619. [PubMed
]
- Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem. 1993 Feb 5;268(4):2571-6. [PubMed
]
- Kelner MJ, Bagnell RD, Montoya MA, Lanham KA: Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene. 2000 May 2;248(1-2):109-16. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
6115 |
| Enzyme 32 Name |
Glutathione S-transferase P |
| Enzyme 32 Synonyms |
- GST class-pi
- GSTP1-1
|
| Enzyme 32 Gene Name |
GSTP1 |
| Enzyme 32 Protein Sequence |
>Glutathione S-transferase P
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGD
LTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAY
VGRLSARPKLKAFLASPEYVNLPINGNGKQ
|
| Enzyme 32 Number of Residues |
210 |
| Enzyme 32 Molecular Weight |
23356 |
| Enzyme 32 Theoretical pI |
5.30 |
| Enzyme 32 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
Not Available |
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
31946  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P09211  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
GSTP1_HUMAN  |
| Enzyme 32 PDB ID |
13GS  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>633 bp
ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG
CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG
GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC
CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT
GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC
CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG
AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC
AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG
CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT
GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG
AACCTCCCCATCAATGGCAACGGGAAACAGTGA
|
| Enzyme 32 GenBank Gene ID |
X06547  |
| Enzyme 32 GeneCard ID |
GSTP1  |
| Enzyme 32 GenAtlas ID |
GSTP1  |
| Enzyme 32 HGNC ID |
HGNC:4638  |
| Enzyme 32 Chromosome Location |
11 |
| Enzyme 32 Locus |
11q13 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Kano T, Sakai M, Muramatsu M: Structure and expression of a human class pi glutathione S-transferase messenger RNA. Cancer Res. 1987 Nov 1;47(21):5626-30. [PubMed
]
- Cowell IG, Dixon KH, Pemble SE, Ketterer B, Taylor JB: The structure of the human glutathione S-transferase pi gene. Biochem J. 1988 Oct 1;255(1):79-83. [PubMed
]
- Morrow CS, Cowan KH, Goldsmith ME: Structure of the human genomic glutathione S-transferase-pi gene. Gene. 1989 Jan 30;75(1):3-11. [PubMed
]
- Moscow JA, Fairchild CR, Madden MJ, Ransom DT, Wieand HS, O'Brien EE, Poplack DG, Cossman J, Myers CE, Cowan KH: Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res. 1989 Mar 15;49(6):1422-8. [PubMed
]
- Ali-Osman F, Akande O, Antoun G, Mao JX, Buolamwini J: Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J Biol Chem. 1997 Apr 11;272(15):10004-12. [PubMed
]
- Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed
]
- Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed
]
- Singh SV, Ahmad H, Kurosky A, Awasthi YC: Purification and characterization of unique glutathione S-transferases from human muscle. Arch Biochem Biophys. 1988 Jul;264(1):13-22. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed
]
- Ahmad H, Wilson DE, Fritz RR, Singh SV, Medh RD, Nagle GT, Awasthi YC, Kurosky A: Primary and secondary structural analyses of glutathione S-transferase pi from human placenta. Arch Biochem Biophys. 1990 May 1;278(2):398-408. [PubMed
]
- Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW: Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol. 1992 Sep 5;227(1):214-26. [PubMed
]
- Oakley AJ, Rossjohn J, Lo Bello M, Caccuri AM, Federici G, Parker MW: The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry. 1997 Jan 21;36(3):576-85. [PubMed
]
- Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P: Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry. 1997 Aug 12;36(32):9690-702. [PubMed
]
- Oakley AJ, Lo Bello M, Battistoni A, Ricci G, Rossjohn J, Villar HO, Parker MW: The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol. 1997 Nov 21;274(1):84-100. [PubMed
]
- Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W: Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor. Structure. 1997 Oct 15;5(10):1287-95. [PubMed
]
- Ji X, Blaszczyk J, Xiao B, O'Donnell R, Hu X, Herzog C, Singh SV, Zimniak P: Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry. 1999 Aug 10;38(32):10231-8. [PubMed
]
- Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lo Bello M, Caccuri AM, Federici G, Ricci G: Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure. Biochemistry. 1998 Mar 3;37(9):3020-7. [PubMed
]
- Kong KH, Inoue H, Takahashi K: Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1. Protein Eng. 1993 Jan;6(1):93-9. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
6871 |
| Enzyme 33 Name |
Glutathione-requiring prostaglandin D synthase |
| Enzyme 33 Synonyms |
- Glutathione-dependent PGD synthetase
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- H-PGDS
|
| Enzyme 33 Gene Name |
PTGDS2 |
| Enzyme 33 Protein Sequence |
>Glutathione-requiring prostaglandin D synthase
MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLT
LHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELL
TYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKK
VQAIPAVANWIKRRPQTKL
|
| Enzyme 33 Number of Residues |
199 |
| Enzyme 33 Molecular Weight |
23344 |
| Enzyme 33 Theoretical pI |
5.64 |
| Enzyme 33 GO Classification |
Not Available |
| Enzyme 33 General Function |
Not Available |
| Enzyme 33 Specific Function |
Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
3046817  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
O60760  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PTGD2_HUMAN  |
| Enzyme 33 PDB ID |
1IYI  |
| Enzyme 33 PDB File |
Show |
| Enzyme 33 3D Structure |
|
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>600 bp
ATGCCAAACTACAAACTCACTTATTTTAATATGAGGGGGAGAGCAGAAATTATTCGTTAC
ATATTTGCTTATTTGGACATACAGTATGAAGACCACAGAATAGAACAAGCTGACTGGCCT
GAAATCAAATCAACTCTCCCATTTGGAAAAATCCCCATTTTGGAAGTTGATGGACTTACT
CTTCACCAGAGCCTAGCAATAGCAAGATATTTGACCAAAAACACAGATTTGGCTGGAAAC
ACAGAAATGGAACAATGTCATGTTGATGCTATTGTGGACACTCTGGATGATTTCATGTCA
TGTTTTCCTTGGGCAGAGAAAAAGCAAGATGTGAAAGAGCAGATGTTCAATGAGCTGCTC
ACGTATAATGCGCCTCATCTTATGCAAGACTTGGACACATATTTAGGGGGGAGAGAATGG
CTTATTGGTAACTCTGTAACTTGGGCAGACTTCTACTGGGAGATTTGCAGTACCACACTT
TTGGTCTTTAAGCCTGACCTGTTAGACAACCATCCAAGGCTGGTGACTTTACGGAAGAAA
GTCCAAGCCATTCCTGCCGTCGCTAACTGGATAAAACGAAGGCCCCAAACCAAACTCTAG
|
| Enzyme 33 GenBank Gene ID |
D82073  |
| Enzyme 33 GeneCard ID |
Not Available |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Kanaoka Y, Fujimori K, Kikuno R, Sakaguchi Y, Urade Y, Hayaishi O: Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase. Eur J Biochem. 2000 Jun;267(11):3315-22. [PubMed
]
- Suzuki T, Watanabe K, Kanaoka Y, Sato T, Hayaishi O: Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester. Biochem Biophys Res Commun. 1997 Dec 18;241(2):288-93. [PubMed
]
- Mahmud I, Ueda N, Yamaguchi H, Yamashita R, Yamamoto S, Kanaoka Y, Urade Y, Hayaishi O: Prostaglandin D synthase in human megakaryoblastic cells. J Biol Chem. 1997 Nov 7;272(45):28263-6. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
7832 |
| Enzyme 34 Name |
RalA-binding protein 1 |
| Enzyme 34 Synonyms |
- RalBP1
- Ral-interacting protein 1
- 76 kDa Ral-interacting protein
- Dinitrophenyl S-glutathione ATPase
- DNP-SG ATPase
|
| Enzyme 34 Gene Name |
RALBP1 |
| Enzyme 34 Protein Sequence |
>RalA-binding protein 1
MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDV
VSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKK
KEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQ
IDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKV
DELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKV
QEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVF
FTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGI
KDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVIN
ILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSS
ESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAK
AEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI
|
| Enzyme 34 Number of Residues |
655 |
| Enzyme 34 Molecular Weight |
76064 |
| Enzyme 34 Theoretical pI |
5.68 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Replication, recombination and repair |
| Enzyme 34 Specific Function |
Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
974143  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q15311  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
RBP1_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1968 bp
ATGACTGAGTGCTTCCTGCCCCCCACCAGCAGCCCCAGTGAACACCGCAGGGTGGAGCAT
GGCAGCGGGCTTACCCGGACCCCCAGCTCTGAAGAGATCAGCCCTACTAAGTTTCCTGGA
TTGTACCGCACTGGCGAGCCCTCACCTCCCCATGACATCCTCCATGAGCCTCCTGATGTA
GTGTCTGATGATGAGAAAGATCATGGGAAGAAAAAAGGGAAATTTAAGAAAAAGGAAAAG
AGGACTGAAGGCTATGCAGCCTTTCAGGAAGATAGCTCTGGAGATGAGGCAGAAAGTCCT
TCTAAAATGAAGAGGTCCAAGGGAATCCATGTTTTCAAGAAGCCCAGCTTTTCTAAAAAG
AAGGAAAAGGATTTTAAAATAAAAGAGAAACCCAAAGAAGAAAAGCATAAAGAAGAAAAG
CACAAAGAAGAAAAACATAAAGAGAAGAAGTCAAAAGACTTGACAGCAGCTGATGTTGTT
AAACAGTGGAAGGAAAAGAAGAAAAAGAAAAAGCCAATTCAGGAGCCAGAGGTGCCTCAG
ATTGATGTTCCAAATCTCAAACCCATTTTTGGAATTCCTTTGGCTGATGCAGTAGAGAGG
ACCATGATGTATGATGGCATTCGGCTGCCAGCCGTTTTCCGTGAATGTATAGATTACGTA
GAGAAGTATGGCATGAAGTGTGAAGGCATCTACAGAGTATCAGGAATTAAATCAAAGGTG
GATGAGCTAAAAGCAGCCTATGACCGGGAGGAGTCTACAAACTTGGAAGACTATGAGCCT
AACACTGTAGCCAGTTTGCTGAAGCAGTATTTGCGAGACCTTCCAGAGAATTTGCTTACC
AAAGAGCTTATGCCCAGATTTGAAGAGGCTTGTGGGAGGACCACGGAGACTGAGAAAGTG
CAGGAATTCCAGCGTTTACTCAAAGAACTGCCAGAATGTAACTATCTTCTGATTTCTTGG
CTCATTGTGCACATGGACCATGTCATTGCAAAGGAACTGGAAACAAAAATGAATATACAG
AACATTTCTATAGTGCTCAGCCCAACTGTGCAGATCAGCAATCGAGTCCTGTATGTGTTT
TTCACACATGTGCAAGAACTCTTTGGAAATGTGGTACTAAAGCAAGTGATGAAACCTCTG
CGATGGTCTAACATGGCCACGATGCCCACGCTGCCAGAGACCCAGGCGGGCATCAAGGAG
GAGATCAGGAGACAGGAGTTTCTTTTGAATTGTTTACATCGAGATCTGCAGGGTGGGATA
AAGGATTTGTCTAAAGAAGAAAGATTATGGGAAGTACAAAGAATTTTGACAGCCCTCAAA
AGAAAACTGAGAGAAGCTAAAAGACAGGAGTGTGAAACCAAGATTGCACAAGAGATAGCC
AGTCTTTCAAAAGAGGATGTTTCCAAAGAAGAGATGAATGAAAATGAAGAAGTTATAAAT
ATTCTCCTTGCTCAGGAGAATGAGATCCTGACTGAACAGGAGGAGCTCCTGGCCATGGAG
CAGTTTCTGCGCCGGCAGATTGCCTCAGAAAAAGAAGAGATTGAACGCCTCAGAGCTGAG
ATTGCTGAAATTCAGAGTCGCCAGCAGCACGGCCGAAGTGAGACTGAGGAGTACTCCTCC
GAGAGCGAGAGCGAGAGTGAGGATGAGGAGGAGCTGCAGATCATTCTGGAAGACTTACAG
AGACAGAACGAAGAGCTGGAAATAAAGAACAATCATTTGAATCAAGCAATTCATGAGGAG
CGCGAGGCCATCATCGAGCTGCGCGTGCAGCTGCGGCTGCTCCAGATGCAGCGAGCCAAG
GCCGAGCAGCAGGCGCAGGAGGACGAGGAGCCTGAGTGGCGCGGGGGTGCCGTCCAGCCG
CCCAGAGACGGCGTCCTTGAGCCAAAAGCAGCTAAAGAGCAGCCAAAGGCAGGCAAGGAG
CCGGCAAAGCCATCGCCCAGCAGGGATAGGAAGGAGACGTCCATCTGA
|
| Enzyme 34 GenBank Gene ID |
L42542  |
| Enzyme 34 GeneCard ID |
RALBP1  |
| Enzyme 34 GenAtlas ID |
RALBP1  |
| Enzyme 34 HGNC ID |
HGNC:9841  |
| Enzyme 34 Chromosome Location |
18 |
| Enzyme 34 Locus |
18p11.3 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH: Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. [PubMed
]
- Awasthi S, Cheng J, Singhal SS, Saini MK, Pandya U, Pikula S, Bandorowicz-Pikula J, Singh SV, Zimniak P, Awasthi YC: Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin. Biochemistry. 2000 Aug 8;39(31):9327-34. [PubMed
]
- Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A: Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J Biol Chem. 1998 Jan 9;273(2):814-21. [PubMed
]
- Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P, Awasthi S, Awasthi YC: RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Arch Biochem Biophys. 2001 Jul 15;391(2):171-9. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
11578 |
| Enzyme 35 Name |
Hydroxyacylglutathione hydrolase-like protein |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
HAGHL |
| Enzyme 35 Protein Sequence |
>Hydroxyacylglutathione hydrolase-like protein
MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHA
RGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLW
EDDCPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLE
FAQKVEPCNDHVRAKLSWAKARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRG
MRMTCPLCRRLWARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG
|
| Enzyme 35 Number of Residues |
290 |
| Enzyme 35 Molecular Weight |
31558 |
| Enzyme 35 Theoretical pI |
Not Available |
| Enzyme 35 GO Classification |
Not Available |
| Enzyme 35 General Function |
Not Available |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
- H2O + (R)-S-Lactoylglutathione --> Reduced glutathione + H+ + D-Lactate
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
45708670  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q6PII5  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
Q6PII5_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
Not Available |
| Enzyme 35 GenBank Gene ID |
BC033796  |
| Enzyme 35 GeneCard ID |
Not Available |
| Enzyme 35 GenAtlas ID |
HAGHL  |
| Enzyme 35 HGNC ID |
HGNC:14177  |
| Enzyme 35 Chromosome Location |
Not Available |
| Enzyme 35 Locus |
Not Available |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 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 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
12987 |
| Enzyme 36 Name |
Gamma-glutamyltransferase 6 homolog |
| Enzyme 36 Synonyms |
Not Available |
| Enzyme 36 Gene Name |
GGT6 |
| Enzyme 36 Protein Sequence |
>Gamma-glutamyltransferase 6 homolog
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWVRV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
|
| Enzyme 36 Number of Residues |
493 |
| Enzyme 36 Molecular Weight |
50538 |
| Enzyme 36 Theoretical pI |
6.04 |
| Enzyme 36 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 36 General Function |
Amino acid transport and metabolism |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
38970000  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q6P531  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
Q6P531_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
Not Available |
| Enzyme 36 GenBank Gene ID |
BC063111  |
| Enzyme 36 GeneCard ID |
Q6P531  |
| Enzyme 36 GenAtlas ID |
GGT6  |
| Enzyme 36 HGNC ID |
HGNC:26891  |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 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 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
13120 |
| Enzyme 37 Name |
Uncharacterized protein GSTZ1 |
| Enzyme 37 Synonyms |
- Glutathione transferase zeta 1
- Maleylacetoacetate isomerase, isoform CRA_a
|
| Enzyme 37 Gene Name |
GSTZ1 |
| Enzyme 37 Protein Sequence |
>Uncharacterized protein GSTZ1
MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
|
| Enzyme 37 Number of Residues |
161 |
| Enzyme 37 Molecular Weight |
17896 |
| Enzyme 37 Theoretical pI |
5.76 |
| Enzyme 37 GO Classification |
| Function |
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- aromatic amino acid family metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 37 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 37 Specific Function |
Not Available |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
A6NNB8  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
A6NNB8_HUMAN  |
| Enzyme 37 PDB ID |
1FW1  |
| Enzyme 37 PDB File |
Show |
| Enzyme 37 3D Structure |
|
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
Not Available |
| Enzyme 37 GenBank Gene ID |
AC007954  |
| Enzyme 37 GeneCard ID |
A6NNB8  |
| Enzyme 37 GenAtlas ID |
GSTZ1  |
| Enzyme 37 HGNC ID |
HGNC:4643  |
| Enzyme 37 Chromosome Location |
Not Available |
| Enzyme 37 Locus |
Not Available |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
15189 |
| Enzyme 38 Name |
GGTL3 protein (Fragment) |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
GGTL3 |
| Enzyme 38 Protein Sequence |
>GGTL3 protein (Fragment)
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLA
|
| Enzyme 38 Number of Residues |
592 |
| Enzyme 38 Molecular Weight |
62567 |
| Enzyme 38 Theoretical pI |
4.64 |
| Enzyme 38 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 38 General Function |
Amino acid transport and metabolism |
| Enzyme 38 Specific Function |
Not Available |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
118600847  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
A0PJJ9  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
A0PJJ9_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1777 bp
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAAGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCC
|
| Enzyme 38 GenBank Gene ID |
BC033745  |
| Enzyme 38 GeneCard ID |
A0PJJ9  |
| Enzyme 38 GenAtlas ID |
Not Available |
| Enzyme 38 HGNC ID |
Not Available |
| Enzyme 38 Chromosome Location |
20 |
| Enzyme 38 Locus |
20q11.22 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 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 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
15190 |
| Enzyme 39 Name |
Gamma-glutamyltransferase-like activity 1 |
| Enzyme 39 Synonyms |
Not Available |
| Enzyme 39 Gene Name |
GGTLA1 |
| Enzyme 39 Protein Sequence |
>Gamma-glutamyltransferase-like activity 1
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAI
LQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPS
LLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVL
SRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRL
GQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLR
GFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQL
IRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRT
GIILNNELLDLCERCPRGSGTTPSPAVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINK
AQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQE
VQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
|
| Enzyme 39 Number of Residues |
587 |
| Enzyme 39 Molecular Weight |
62333 |
| Enzyme 39 Theoretical pI |
7.59 |
| Enzyme 39 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 39 General Function |
Amino acid transport and metabolism |
| Enzyme 39 Specific Function |
Not Available |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
49256405  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q6GMP0  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
Q6GMP0_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1764 bp
ATGGCCCGGGGCTACGGGGCCACGGTCAGCCTAGTCCTGCTGGGTCTGGGGCTGGCGCTG
GCTGTCATTGTGCTGGCTGTGGTCCTCTCTCGACACCAGGCCCCATGTGGCCCCCAGGCC
TTTGCCCACGCTGCTGTTGCCGCCGACTCCAAGGTCTGCTCGGATATTGGACGAGCCATC
CTCCAGCAGCAGGGCTCACCCGTGGATGCCACCATCGCGGCTCTGGTCTGCACCAGCGTC
GTCAACCCTCAGAGCATGGGCCTGGGCGGAGGGGTCATCTTCACCATCTACAATGTGACA
ACAGGGAAGGTGGAGGTCATCAATGCCCGGGAGACGGTGCCGGCCAGCCACGCCCCGAGC
CTGCTGGACCAGTGTGCACAGGCTCTGCCACTGGGCACAGGGGCCCAGTGGATCGGGGTG
CCCGGGGAGCTCCGTGGCTATGCCGAGGCCCACCGCCGCCATGGCCGCCTGCCCTGGGCG
CAGCTGTTCCAGCCCACCATCGCGCTGCTCCGAGGGGGGCATGTGGTGGCCCCTGTCCTC
AGCCGTTTCCTGCACAACAGCATCCTGCGGCCTTCCTTGCAGGCGTCAACCCTGCGCCAG
CTCTTCTTCAACGGGACAGAACCCCTGAGGCCTCAGGACCCACTCCCATGGCCTGCACTG
GCCACCACCCTGGAGACCGTGGCCACAGAGGGCGTGGAGGTCTTCTACACGGGGAGGCTG
GGCCAGATGCTGGTGGAGGACATTGCCAAGGAAGGGAGCCAGCTGACGCTGCAGGACCTG
GCCAAGTTCCAGCCCGAGGTGGTGGATGCCCTGGAGGTGCCCCTGGGGGACTATACCCTG
TACTCACCACCGCCGCCTGCAGGGGGTGCCATTCTCAGCTTTATCCTCAACGTGCTAAGA
GGGTTCAACTTCTCAACAGAGTCTATGGCCAGGCCTGAAGGGAGGGTGAACGTGTACCAC
CACCTTGTAGAGACGCTCAAGTTTGCCAAGGGGCAGAGGTGGAGGCTGGGGGACCCTCGA
AGCCACCCGAAGCTCCAGAATGCCTCCCGGGACCTGCTGGGGGAGACCCTGGCCCAGCTC
ATCCGCCAACAGATCGATGGCCGGGGGGACCACCAGCTCAGCCACTACAGCTTGGCCGAG
GCCTGGGGCCACGGGACAGGCACGTCCCATGTGTCTGTGCTGGGGGAGGATGGCAGCGCC
GTGGCTGCCACCAGCACCATCAACACACCCTTTGGAGCGATGGTGTATTCACCACGGACA
GGCATCATCCTCAACAACGAGCTCCTGGACTTATGCGAGCGATGCCCCCGGGGTTCCGGC
ACCACCCCCTCACCTGCAGTGAGTGGAGACAGGGTGGGTGGAGCTCCCGGAAGGTGCTGG
CCCCCAGTTCCAGGCGAGCGTTCCCCATCCTCCATGGTGCCCTCCATCTTGATCAACAAA
GCCCAGGGGTCGAAGCTAGTGATTGGCGGGGCTGGCGGGGAGCTCATCATCTCTGCTGTG
GCCCAGGCCATCATGAGCAAGCTGTGGCTTGGCTTTGACCTGAGAGCGGCCATTGCAGCC
CCCATCCTGCATGTCAACAGCAAGGGCTGTGTGGAGTACGAGCCCAACTTCAGCCAGGAG
GTGCAGAGGGGACTCCAAGACCGTGGCCAGAACCAGACCCAGAGGCCCTTCTTCCTGAAC
GTGGTCCAGGCTGTGTCCCAGGAGGGGGCCTGTGTGTACGCCGTCTCGGACCTGAGGAAG
AGTGGGGAGGCCGCAGGCTACTAA
|
| Enzyme 39 GenBank Gene ID |
BC073999  |
| Enzyme 39 GeneCard ID |
Q6GMP0  |
| Enzyme 39 GenAtlas ID |
GGT5  |
| Enzyme 39 HGNC ID |
HGNC:4260  |
| Enzyme 39 Chromosome Location |
22 |
| Enzyme 39 Locus |
22q11.23 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 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 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
15211 |
| Enzyme 40 Name |
Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b) |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
GSTA3 |
| Enzyme 40 Protein Sequence |
>Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
|
| Enzyme 40 Number of Residues |
222 |
| Enzyme 40 Molecular Weight |
25302 |
| Enzyme 40 Theoretical pI |
9.69 |
| Enzyme 40 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Not Available |
| Enzyme 40 Specific Function |
Not Available |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
Not Available |
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
114731581  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q068V6  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
Q068V6_HUMAN  |
| Enzyme 40 PDB ID |
1TDI  |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>669 bp
ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA
|
| Enzyme 40 GenBank Gene ID |
DQ993361  |
| Enzyme 40 GeneCard ID |
Q068V6  |
| Enzyme 40 GenAtlas ID |
GSTA3  |
| Enzyme 40 HGNC ID |
HGNC:4628  |
| Enzyme 40 Chromosome Location |
Not Available |
| Enzyme 40 Locus |
Not Available |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
Not Available |
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
15212 |
| Enzyme 41 Name |
cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d) |
| Enzyme 41 Synonyms |
Not Available |
| Enzyme 41 Gene Name |
GSTM4 |
| Enzyme 41 Protein Sequence |
>cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
|
| Enzyme 41 Number of Residues |
218 |
| Enzyme 41 Molecular Weight |
25562 |
| Enzyme 41 Theoretical pI |
5.69 |
| Enzyme 41 GO Classification |
Not Available |
| Enzyme 41 General Function |
Not Available |
| Enzyme 41 Specific Function |
Not Available |
| Enzyme 41 Pathways |
Not Available |
| Enzyme 41 Reactions |
Not Available |
| Enzyme 41 Pfam Domain Function |
Not Available |
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
158257192  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
A8K765  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
A8K765_HUMAN  |
| Enzyme 41 PDB ID |
4GTU  |
| Enzyme 41 PDB File |
Show |
| Enzyme 41 3D Structure |
|
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
|
| Enzyme 41 GenBank Gene ID |
AK291880  |
| Enzyme 41 GeneCard ID |
A8K765  |
| Enzyme 41 GenAtlas ID |
Not Available |
| Enzyme 41 HGNC ID |
Not Available |
| Enzyme 41 Chromosome Location |
Not Available |
| Enzyme 41 Locus |
Not Available |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
Not Available |
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
15213 |
| Enzyme 42 Name |
LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056) |
| Enzyme 42 Synonyms |
Not Available |
| Enzyme 42 Gene Name |
LOC51064 |
| Enzyme 42 Protein Sequence |
>LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
|
| Enzyme 42 Number of Residues |
226 |
| Enzyme 42 Molecular Weight |
25497 |
| Enzyme 42 Theoretical pI |
8.69 |
| Enzyme 42 GO Classification |
| Function |
- catalytic activity
- disulfide oxidoreductase activity
- oxidoreductase activity
- protein disulfide oxidoreductase activity
|
| Process |
| — |
| Component |
- cell
- periplasmic space
- periplasmic space (sensu Gram-negative Bacteria)
|
|
| Enzyme 42 General Function |
Not Available |
| Enzyme 42 Specific Function |
Not Available |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
158260183  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q6FII1  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
Q6FII1_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
|
| Enzyme 42 GenBank Gene ID |
AK289580  |
| Enzyme 42 GeneCard ID |
Q6FII1  |
| Enzyme 42 GenAtlas ID |
LOC51064  |
| Enzyme 42 HGNC ID |
HGNC:16906  |
| Enzyme 42 Chromosome Location |
Not Available |
| Enzyme 42 Locus |
Not Available |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 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 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
15214 |
| Enzyme 43 Name |
cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a) |
| Enzyme 43 Synonyms |
Not Available |
| Enzyme 43 Gene Name |
MGST1 |
| Enzyme 43 Protein Sequence |
>cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAK
KYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIA
YLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL
|
| Enzyme 43 Number of Residues |
155 |
| Enzyme 43 Molecular Weight |
17599 |
| Enzyme 43 Theoretical pI |
9.71 |
| Enzyme 43 GO Classification |
Not Available |
| Enzyme 43 General Function |
Not Available |
| Enzyme 43 Specific Function |
Not Available |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
Not Available |
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
158255732  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
A8K533  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
A8K533_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>468 bp
ATGGTTGACCTCACCCAGGTAATGGATGATGAAGTATTCATGGCTTTTGCATCCTATGCA
ACAATTATTCTTTCAAAAATGATGCTTATGAGTACTGCAACTGCATTCTATAGATTGACA
AGAAAGGTTTTTGCCAATCCAGAAGACTGTGTAGCATTTGGCAAAGGTGAAAATGCCAAG
AAGTATCTTCGAACAGATGACAGAGTAGAACGTGTACGCAGAGCCCACCTGAATGACCTT
GAAAATATTATTCCATTTCTTGGAATTGGCCTCCTGTATTCCTTGAGTGGTCCCGACCCC
TCTACAGCCATCCTGCACTTCAGACTATTTGTCGGAGCACGGATCTACCACACCATTGCA
TATTTGACACCCCTTCCCCAGCCAAATAGAGCTTTGAGTTTTTTTGTTGGATATGGAGTT
ACTCTTTCCATGGCTTACAGGTTGCTGAAAAGTAAATTGTACCTGTAA
|
| Enzyme 43 GenBank Gene ID |
AK291148  |
| Enzyme 43 GeneCard ID |
A8K533  |
| Enzyme 43 GenAtlas ID |
Not Available |
| Enzyme 43 HGNC ID |
Not Available |
| Enzyme 43 Chromosome Location |
12 |
| Enzyme 43 Locus |
12p12.3-p12.1 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
Not Available |
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
16491 |
| Enzyme 44 Name |
cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum) |
| Enzyme 44 Synonyms |
Not Available |
| Enzyme 44 Gene Name |
TXNDC12 |
| Enzyme 44 Protein Sequence |
>cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum)
METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVI
IHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP
SGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL
|
| Enzyme 44 Number of Residues |
172 |
| Enzyme 44 Molecular Weight |
19206 |
| Enzyme 44 Theoretical pI |
5.10 |
| Enzyme 44 GO Classification |
Not Available |
| Enzyme 44 General Function |
Not Available |
| Enzyme 44 Specific Function |
Not Available |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
Not Available |
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
Not Available |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
B3KQS0  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
B3KQS0_HUMAN  |
| Enzyme 44 PDB ID |
1SEN  |
| Enzyme 44 PDB File |
Show |
| Enzyme 44 3D Structure |
|
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
Not Available |
| Enzyme 44 GenBank Gene ID |
AK075409  |
| Enzyme 44 GeneCard ID |
B3KQS0  |
| Enzyme 44 GenAtlas ID |
Not Available |
| Enzyme 44 HGNC ID |
Not Available |
| Enzyme 44 Chromosome Location |
Not Available |
| Enzyme 44 Locus |
Not Available |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
Not Available |
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
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| Enzyme 45 ID |
16492 |
| Enzyme 45 Name |
cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b) |
| Enzyme 45 Synonyms |
Not Available |
| Enzyme 45 Gene Name |
GSTA4 |
| Enzyme 45 Protein Sequence |
>cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
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| Enzyme 45 Number of Residues |
222 |
| Enzyme 45 Molecular Weight |
25705 |
| Enzyme 45 Theoretical pI |
8.72 |
| Enzyme 45 GO Classification |
| Function |
- catalytic activity
- glutathione transferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
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| Process |
- metabolism
- physiological process
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| Component |
| — |
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| Enzyme 45 General Function |
Not Available |
| Enzyme 45 Specific Function |
Not Available |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
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| Enzyme 45 Transmembrane Regions |
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| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
Not Available |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
B2RD15  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
B2RD15_HUMAN  |
| Enzyme 45 PDB ID |
1GUM  |
| Enzyme 45 PDB File |
Show |
| Enzyme 45 3D Structure |
|
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
Not Available |
| Enzyme 45 GenBank Gene ID |
AK315369  |
| Enzyme 45 GeneCard ID |
B2RD15  |
| Enzyme 45 GenAtlas ID |
Not Available |
| Enzyme 45 HGNC ID |
Not Available |
| Enzyme 45 Chromosome Location |
Not Available |
| Enzyme 45 Locus |
Not Available |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
Not Available |
| Enzyme 45 Metabolite References |
Not Available |
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Enzyme 46
[top]
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| Enzyme 46 ID |
16493 |
| Enzyme 46 Name |
cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a) |
| Enzyme 46 Synonyms |
Not Available |
| Enzyme 46 Gene Name |
MGST3 |
| Enzyme 46 Protein Sequence |
>cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRA
HQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSI
ALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH
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| Enzyme 46 Number of Residues |
152 |
| Enzyme 46 Molecular Weight |
16516 |
| Enzyme 46 Theoretical pI |
9.68 |
| Enzyme 46 GO Classification |
Not Available |
| Enzyme 46 General Function |
Not Available |
| Enzyme 46 Specific Function |
Not Available |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
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| Enzyme 46 Signals |
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| Enzyme 46 Transmembrane Regions |
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| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
Not Available |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
B2R592  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
B2R592_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
Not Available |
| Enzyme 46 GenBank Gene ID |
AK312103  |
| Enzyme 46 GeneCard ID |
B2R592  |
| Enzyme 46 GenAtlas ID |
Not Available |
| Enzyme 46 HGNC ID |
Not Available |
| Enzyme 46 Chromosome Location |
Not Available |
| Enzyme 46 Locus |
Not Available |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
Not Available |
| Enzyme 46 Metabolite References |
Not Available |
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Enzyme 47
[top]
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| Enzyme 47 ID |
16494 |
| Enzyme 47 Name |
cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3) |
| Enzyme 47 Synonyms |
Not Available |
| Enzyme 47 Gene Name |
Not Available |
| Enzyme 47 Protein Sequence |
>cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRALL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLIFPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
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| Enzyme 47 Number of Residues |
377 |
| Enzyme 47 Molecular Weight |
41970 |
| Enzyme 47 Theoretical pI |
9.50 |
| Enzyme 47 GO Classification |
| Function |
- electron transporter activity
- transporter activity
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| Process |
- cell homeostasis
- cell redox homeostasis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- homeostasis
- metabolism
- physiological process
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| Component |
| — |
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| Enzyme 47 General Function |
Not Available |
| Enzyme 47 Specific Function |
Not Available |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
- (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265] ALL_REAC R02265
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| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
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| Enzyme 47 Transmembrane Regions |
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| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
Not Available |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
B3KPZ2  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
B3KPZ2_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
Not Available |
| Enzyme 47 GenBank Gene ID |
AK057049  |
| Enzyme 47 GeneCard ID |
B3KPZ2  |
| Enzyme 47 GenAtlas ID |
Not Available |
| Enzyme 47 HGNC ID |
Not Available |
| Enzyme 47 Chromosome Location |
Not Available |
| Enzyme 47 Locus |
Not Available |
| Enzyme 47 SNPs |
Not Available |
| Enzyme 47 General References |
Not Available |
| Enzyme 47 Metabolite References |
Not Available |