|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6088 |
| Enzyme 1 Name |
Glutathione S-transferase Mu 2 |
| Enzyme 1 Synonyms |
- GSTM2-2
- GST class-mu 2
|
| Enzyme 1 Gene Name |
GSTM2 |
| Enzyme 1 Protein Sequence |
>Glutathione S-transferase Mu 2
MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDF
EKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK
|
| Enzyme 1 Number of Residues |
218 |
| Enzyme 1 Molecular Weight |
25745 |
| Enzyme 1 Theoretical pI |
6.29 |
| Enzyme 1 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 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
183301  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P28161  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GSTM2_HUMAN  |
| Enzyme 1 PDB ID |
1XW5  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>657 bp
ATGCCCATGACACTGGGGTACTGGAACATCCGCGGGCTGGCCCATTCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGACTCACAAGATCACCCAGAGCAATGCCATCCTGCGGTACATT
GCCCGCAAGCACAACCTGTGCGGGGAATCAGAAAAGGAGCAGATTCGCGAAGACATTTTG
GAGAACCAGTTTATGGACAGCCGTATGCAGCTGGCCAAACTCTGCTATGACCCAGATTTT
GAGAAACTGAAACCAGAATACCTGCAGGCACTCCCTGAAATGCTGAAGCTCTACTCACAG
TTTCTGGGGAAGCAGCCATGGTTTCTTGGGGACAAGATCACCTTTGTGGATTTCATCGCT
TATGATGTCCTTGAGAGAAACCAAGTATTTGAGCCCAGCTGCCTGGATGCCTTCCCAAAC
CTGAAGGACTTCATCTCCCGATTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCACAAAGATGGCTGTCTGGGGCAACAAGTAG
|
| Enzyme 1 GenBank Gene ID |
M63509  |
| Enzyme 1 GeneCard ID |
GSTM2  |
| Enzyme 1 GenAtlas ID |
GSTM2  |
| Enzyme 1 HGNC ID |
HGNC:4634  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6091 |
| Enzyme 2 Name |
Glutathione S-transferase Mu 1 |
| Enzyme 2 Synonyms |
- GSTM1-1
- GST class-mu 1
- GSTM1a-1a
- GSTM1b-1b
- HB subunit 4
- GTH4
|
| Enzyme 2 Gene Name |
GSTM1 |
| Enzyme 2 Protein Sequence |
>Glutathione S-transferase Mu 1
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
|
| Enzyme 2 Number of Residues |
218 |
| Enzyme 2 Molecular Weight |
25712 |
| Enzyme 2 Theoretical pI |
6.67 |
| Enzyme 2 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 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
31924  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P09488  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
GSTM1_HUMAN  |
| Enzyme 2 PDB ID |
1XWK  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>657 bp
ATGCCCATGATACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTATGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCTTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGACCATGGACAACCATATGCAGCTGGGCATGATCTGCTACAATCCAGAATTT
GAGAAACTGAAGCCAAAGTACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAAACAAGATCACTTTTGTAGATTTTCTCGTC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCTCAAAGATGGCTGTCTGGGGCAACAAGTAG
|
| Enzyme 2 GenBank Gene ID |
X08020  |
| Enzyme 2 GeneCard ID |
GSTM1  |
| Enzyme 2 GenAtlas ID |
GSTM1  |
| Enzyme 2 HGNC ID |
HGNC:4632  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p13.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6095 |
| Enzyme 3 Name |
Glutathione S-transferase Mu 3 |
| Enzyme 3 Synonyms |
- GSTM3-3
- GST class-mu 3
- hGSTM3-3
|
| Enzyme 3 Gene Name |
GSTM3 |
| Enzyme 3 Protein Sequence |
>Glutathione S-transferase Mu 3
MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLD
FPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCY
SSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLD
EFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
|
| Enzyme 3 Number of Residues |
225 |
| Enzyme 3 Molecular Weight |
26560 |
| Enzyme 3 Theoretical pI |
5.19 |
| Enzyme 3 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 3 General Function |
Not Available |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
306820  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P21266  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
GSTM3_HUMAN  |
| Enzyme 3 PDB ID |
3GTU  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>678 bp
ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA
|
| Enzyme 3 GenBank Gene ID |
J05459  |
| Enzyme 3 GeneCard ID |
GSTM3  |
| Enzyme 3 GenAtlas ID |
GSTM3  |
| Enzyme 3 HGNC ID |
HGNC:4635  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6096 |
| Enzyme 4 Name |
Glutathione S-transferase A1 |
| Enzyme 4 Synonyms |
- GTH1
- HA subunit 1
- GST- epsilon
- GSTA1-1
- GST class-alpha member 1
|
| Enzyme 4 Gene Name |
GSTA1 |
| Enzyme 4 Protein Sequence |
>Glutathione S-transferase A1
MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAK
LALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF
|
| Enzyme 4 Number of Residues |
222 |
| Enzyme 4 Molecular Weight |
25631 |
| Enzyme 4 Theoretical pI |
9.34 |
| Enzyme 4 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 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
306809  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P08263  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
GSTA1_HUMAN  |
| Enzyme 4 PDB ID |
1K3Y  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTTCAATGCACGGGGCAGAATGGAGTCCACCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAGAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTCCTTCTGCCCGTATGTCCACCTGAGGAAAAAGATGCCAAG
CTTGCCTTGATCAAGGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCATCTG
GTGGAACTTCTCTACTACGTCGAGGAGCTTGACTCCAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 4 GenBank Gene ID |
M15872  |
| Enzyme 4 GeneCard ID |
GSTA1  |
| Enzyme 4 GenAtlas ID |
GSTA1  |
| Enzyme 4 HGNC ID |
HGNC:4626  |
| Enzyme 4 Chromosome Location |
6 |
| Enzyme 4 Locus |
6p12.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6098 |
| Enzyme 5 Name |
Glutathione S-transferase theta-2 |
| Enzyme 5 Synonyms |
- GST class-theta-2
|
| Enzyme 5 Gene Name |
GSTT2 |
| Enzyme 5 Protein Sequence |
>Glutathione S-transferase theta-2
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDG
DFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLG
PLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALG
YELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRI
ARIP
|
| Enzyme 5 Number of Residues |
244 |
| Enzyme 5 Molecular Weight |
27507 |
| Enzyme 5 Theoretical pI |
6.36 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 5 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
601918  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P30712  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GSTT2_HUMAN  |
| Enzyme 5 PDB ID |
3LJR  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>735 bp
ATGGGCCTAGAGCTGTTTCTTGACCTGGTGTCCCAGCCCAGCCGCGCCGTCTACATCTTC
GCCAAGAAGAATGGCATCCCCTTAGAGCTGCGCACCGTGGATTTGGTCAAAGGGCAGCAC
AAGAGCAAGGAGTTCTTGCAGATCAACAGCCTGGGGAAACTGCCGACGCTCAAGGATGGT
GATTTCATCTTGACCGAAAGCTCGGCCATCCTGATTTACCTGAGCTGTAAGTACCAGACG
CCGGACCACTGGTATCCATCTGACCTGCAGGCTCGTGCCCGTGTTCATGAGTACCTGGGC
TGGCATGCCGACTGCATCCGTGGCACCTTTGGTATACCCCTGTGGGTCCAGGTGTTGGGG
CCACTCATTGGGGTCCAGGTGCCCGAGGAGAAGGTGGAACGCAACAGGACTGCCATGGAC
CAGGCCCTGCAATGGCTGGAGGACAAGTTCCTGGGGGACAGGCCCTTCCTCGCTGGCCAG
CAGGTGACACTGGCTGATCTCATGGCCCTGGAGGAGCTGATGCAGCCGGTGGCTCTCGGC
TACGAACTGTTTGAGGGACGGCCACGACTGGCAGCATGGCGTGGACGAGTGGAGGCTTTC
CTGGGTGCTGAGCTATGCCAGGAGGCCCACAGCATCATCTTGAGCATCCTGGAACAGGCG
GCCAAGAAAACCCTCCCAACACCCTCACCAGAGGCCTATCAGGCTATGCTGCTTCGAATC
GCCAGGATCCCCTGA
|
| Enzyme 5 GenBank Gene ID |
L38503  |
| Enzyme 5 GeneCard ID |
GSTT2  |
| Enzyme 5 GenAtlas ID |
GSTT2  |
| Enzyme 5 HGNC ID |
HGNC:4642  |
| Enzyme 5 Chromosome Location |
22 |
| Enzyme 5 Locus |
22q11.2|22q11.23 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6101 |
| Enzyme 6 Name |
Glutathione S-transferase Mu 5 |
| Enzyme 6 Synonyms |
- GSTM5-5
- GST class-mu 5
|
| Enzyme 6 Gene Name |
GSTM5 |
| Enzyme 6 Protein Sequence |
>Glutathione S-transferase Mu 5
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLN
LKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
|
| Enzyme 6 Number of Residues |
218 |
| Enzyme 6 Molecular Weight |
25675 |
| Enzyme 6 Theoretical pI |
7.49 |
| Enzyme 6 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 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- RX + glutathione = HX + R-S-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 |
468260  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P46439  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GSTM5_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>657 bp
ATGCCCATGACTCTGGGGTACTGGGACATCCGTGGGCTGGCCCACGCCATCCGCTTGCTC
CTGGAATACACAGACTCAAGCTATGTGGAAAAGAAGTACACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAATGCCATCCTGCGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGTTATGGATAACCACATGGAGCTGGTCAGACTGTGCTATGACCCAGATTTT
GAGAAACTGAAGCCAAAATACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAGACAAGATCACCTTTGTGGATTTCCTTGCC
TATGATGTCCTTGACATGAAGCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCTAAAC
TTGAAGGACTTCATCTCCCGCTTTGAGGGTTTGAAGAAGATCTCTGCCTACATGAAGTCC
AGCCAATTCCTCCGAGGTCTTTTGTTTGGAAAGTCAGCTACATGGAACAGCAAATAG
|
| Enzyme 6 GenBank Gene ID |
L02321  |
| Enzyme 6 GeneCard ID |
GSTM5  |
| Enzyme 6 GenAtlas ID |
GSTM5  |
| Enzyme 6 HGNC ID |
HGNC:4637  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
1p13.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6102 |
| Enzyme 7 Name |
Microsomal glutathione S-transferase 2 |
| Enzyme 7 Synonyms |
- Microsomal GST- 2
- Microsomal GST-II
|
| Enzyme 7 Gene Name |
MGST2 |
| Enzyme 7 Protein Sequence |
>Microsomal glutathione S-transferase 2
MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFY
PIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTL
LGALGIANSFLDEYLDLNIAKKLRRQF
|
| Enzyme 7 Number of Residues |
147 |
| Enzyme 7 Molecular Weight |
16621 |
| Enzyme 7 Theoretical pI |
9.88 |
| Enzyme 7 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 7 General Function |
Not Available |
| Enzyme 7 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 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 |
1747521  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q99735  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
MGST2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>444 bp
ATGGCCGGGAACTCGATCCTGCTGGCTGCTGTCTCTATTCTCTCGGCCTGTCAGCAAAGT
TATTTTGCTTTGCAAGTTGGAAAGGCAAGATTAAAATACAAAGTTACGCCCCCAGCAGTC
ACTGGGTCACCAGAGTTTGAGAGAGTATTTCGGGCACAACAAAACTGTGTGGAGTTTTAT
CCTATATTCATAATTACATTGTGGATGGCTGGGTGGTATTTCAACCAAGTTTTTGCTACT
TGTCTGGGTCTGGTGTACATATATGGCCGTCACCTATACTTCTGGGGATATTCAGAAGCT
GCTAAAAAACGGATCACCGGTTTCCGACTGAGTCTGGGGATTTTGGCCTTGTTGACCCTC
CTAGGTGCCCTGGGAATTGCAAACAGCTTTCTGGATGAATATCTGGACCTCAATATTGCC
AAGAAACTGAGGCGGCAATTCTAA
|
| Enzyme 7 GenBank Gene ID |
U77604  |
| Enzyme 7 GeneCard ID |
MGST2  |
| Enzyme 7 GenAtlas ID |
MGST2  |
| Enzyme 7 HGNC ID |
HGNC:7063  |
| Enzyme 7 Chromosome Location |
4 |
| Enzyme 7 Locus |
4q28.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6103 |
| Enzyme 8 Name |
Glutathione transferase omega-1 |
| Enzyme 8 Synonyms |
- GSTO 1-1
|
| Enzyme 8 Gene Name |
GSTO1 |
| Enzyme 8 Protein Sequence |
>Glutathione transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
|
| Enzyme 8 Number of Residues |
241 |
| Enzyme 8 Molecular Weight |
27566 |
| Enzyme 8 Theoretical pI |
6.54 |
| Enzyme 8 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 8 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 8 Specific Function |
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
2393722  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P78417  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GSTO1_HUMAN  |
| Enzyme 8 PDB ID |
1EEM  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>726 bp
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA
|
| Enzyme 8 GenBank Gene ID |
U90313  |
| Enzyme 8 GeneCard ID |
GSTO1  |
| Enzyme 8 GenAtlas ID |
GSTO1  |
| Enzyme 8 HGNC ID |
HGNC:13312  |
| Enzyme 8 Chromosome Location |
10 |
| Enzyme 8 Locus |
10q25.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6104 |
| Enzyme 9 Name |
Glutathione S-transferase A5 |
| Enzyme 9 Synonyms |
- Glutathione S-transferase A5-5
- GST class-alpha member 5
|
| Enzyme 9 Gene Name |
GSTA5 |
| Enzyme 9 Protein Sequence |
>Glutathione S-transferase A5
MAEKPKLHYSNARGSMESIRWLLAAAGVELEEKFLESAEDLDKLRNDGSLLFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDMKERALIDMYTEGIVDLTEMILLLLICQPEERDAK
TALVKEKIKNRYFPAFEKVLKSHRQDYLVGNKLSWADIHLVELFYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSQRKPPMDEKSLEEARKIFRF
|
| Enzyme 9 Number of Residues |
222 |
| Enzyme 9 Molecular Weight |
25722 |
| Enzyme 9 Theoretical pI |
8.37 |
| Enzyme 9 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 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
RX + glutathione = HX + R-S-glutathione |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
23197582  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q7RTV2  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
GSTA5_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATGCACGGGGCAGTATGGAGTCCATTCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTGGAAGAGAAATTTCTAGAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGGAGTTTGCTGTTCCAGCAAGTACCAATGGTTGAGATT
GACGGGATGAAGCTGGTGCAGACCAGAGCCATTCTTAACTACATTGCCAGCAAATACAAC
CTTTATGGGAAAGACATGAAGGAGAGAGCCCTGATTGATATGTACACAGAAGGTATAGTA
GATTTGACTGAAATGATCCTTCTTCTGCTCATATGTCAACCAGAGGAAAGAGATGCCAAG
ACTGCCTTGGTCAAAGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACAGACAAGACTACCTTGTTGGCAACAAGCTGAGCTGGGCTGACATTCACCTG
GTGGAACTTTTCTACTACGTGGAAGAGCTTGACTCGAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTGCAGCCT
GGCAGCCAGAGAAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 9 GenBank Gene ID |
BK000212  |
| Enzyme 9 GeneCard ID |
GSTA5  |
| Enzyme 9 GenAtlas ID |
GSTA5  |
| Enzyme 9 HGNC ID |
HGNC:19662  |
| Enzyme 9 Chromosome Location |
6 |
| Enzyme 9 Locus |
6p12.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6105 |
| Enzyme 10 Name |
Glutathione S-transferase A2 |
| Enzyme 10 Synonyms |
- GTH2
- HA subunit 2
- GST- gamma
- GSTA2-2
- GST class-alpha member 2
|
| Enzyme 10 Gene Name |
GSTA2 |
| Enzyme 10 Protein Sequence |
>Glutathione S-transferase A2
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
|
| Enzyme 10 Number of Residues |
222 |
| Enzyme 10 Molecular Weight |
25664 |
| Enzyme 10 Theoretical pI |
9.07 |
| 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 |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
306811  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P09210  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
GSTA2_HUMAN  |
| Enzyme 10 PDB ID |
1AGS  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA
|
| Enzyme 10 GenBank Gene ID |
M16594  |
| Enzyme 10 GeneCard ID |
GSTA2  |
| Enzyme 10 GenAtlas ID |
GSTA2  |
| Enzyme 10 HGNC ID |
HGNC:4627  |
| Enzyme 10 Chromosome Location |
6 |
| Enzyme 10 Locus |
6p12.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6112 |
| Enzyme 11 Name |
Glutathione transferase omega-2 |
| Enzyme 11 Synonyms |
- GSTO-2
|
| Enzyme 11 Gene Name |
GSTO2 |
| Enzyme 11 Protein Sequence |
>Glutathione transferase omega-2
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKP
EWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELF
CKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWP
WFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDF
GLC
|
| Enzyme 11 Number of Residues |
243 |
| Enzyme 11 Molecular Weight |
28254 |
| Enzyme 11 Theoretical pI |
7.62 |
| Enzyme 11 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 11 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 11 Specific Function |
RX + glutathione = HX + R-S-glutathione |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
37777744  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9H4Y5  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
GSTO2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>732 bp
ATGTCTGGGGATGCGACCAGGACCCTGGGGAAAGGAAGCCAGCCCCCAGGGCCAGTCCCG
GAGGGGCTGATCCGCATCTACAGCATGAGGTTCTGCCCCTATTCTCACAGGACCCGCCTC
GTCCTCAAGGCCAAAGACATCAGACATGAAGTGGTCAACATTAACCTGAGAAACAAGCCT
GAATGGTACTATACAAAGCACCCTTTTGGCCACATTCCTGTCCTGGAGACCAGCCAATGT
CAACTGATCTATGAATCTGTTATTGCTTGTGAGTACCTGGATGATGCTTATCCAGGAAGG
AAGCTGTTTCCATATGACCCTTATGAACGAGCTCGCCAAAAGATGTTATTGGAGCTATTT
TGTAAGGTCCCACATTTGACCAAGGAGTGCCTGGTAGCGTTGAGATGTGGGAGAGAATGC
ACTAATCTGAAGGCAGCCCTGCGTCAGGAATTCAGCAACCTGGAAGAGATTCTTGAGTAT
CAGAACACCACCTTCTTTGGTGGAACCTGTATATCCATGATTGATTACCTCCTCTGGCCC
TGGTTTGAGCGGCTGGATGTGTATGGGATACTGGACTGTGTGAGCCACACGCCAGCCCTG
CGGCTCTGGATATCAGCCATGAAGTGGGACCCCACAGTCTGTGCTCTTCTCATGGATAAG
AGCATTTTCCAGGGCTTCTTGAATCTCTATTTTCAGAACAACCCTAATGCCTTTGACTTT
GGGCTGTGCTGA
|
| Enzyme 11 GenBank Gene ID |
AY350731  |
| Enzyme 11 GeneCard ID |
GSTO2  |
| Enzyme 11 GenAtlas ID |
GSTO2  |
| Enzyme 11 HGNC ID |
HGNC:23064  |
| Enzyme 11 Chromosome Location |
10 |
| Enzyme 11 Locus |
10q25.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6113 |
| Enzyme 12 Name |
Glutathione S-transferase theta-1 |
| Enzyme 12 Synonyms |
- GST class-theta-1
- Glutathione transferase T1-1
|
| Enzyme 12 Gene Name |
GSTT1 |
| Enzyme 12 Protein Sequence |
>Glutathione S-transferase theta-1
MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDG
DFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMF
PVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGA
GCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
|
| Enzyme 12 Number of Residues |
240 |
| Enzyme 12 Molecular Weight |
27335 |
| Enzyme 12 Theoretical pI |
7.60 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 12 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 12 Pathways |
|
| Enzyme 12 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
510905  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P30711  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
GSTT1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>723 bp
ATGGGTCTGGAGCTCTACCTGGACCTGCTGTCCCAGCCCTGCCGCGCTGTTTACATCTTT
GCCAAGAAGAACGACATTCCCTTCGAGCTGCGCATCGTGGATCTGATTAAAGGTCAGCAC
TTAAGCGATGCCTTTGCCCAGGTGAACCCCCTCAAGAAGGTGCCGGCCTTGAAGGACGGG
GACTTCACCTTGACGGAGAGTGTGGCCATCCTGCTCTACCTGACGCGCAAATATAAGGTC
CCTGACTACTGGTACCCTCAGGACCTGCAGGCCCGTGCCCGTGTGGATGAGTACCTGGCA
TGGCAGCACACGACTCTGCGGAGAAGCTGCCTCCGGGCCTTGTGGCATAAGGTGATGTTC
CCTGTGTTCCTGGGTGGGCCAGTATCTCCCCAGACACTGGCAGCCACCCTGGCAGAGTTG
GATGTGACCCTGCAGTTGCTCGAGGACAAGTTCCTCCAGAACAAGGCCTTCCTTACTGGT
CCTCACATCTCCTTAGCTGACCTCGTAGCCATCACGGAGCTGATGCATCCCGTGGGTGCT
GGCTGCCAAGTCTTCGAAGGCCGACCCAAGCTGGCCACATGGCGGCAGCGCGTGGAGGCA
GCAGTGGGGGAGGACCTCTTCCAGGAGGCCCATGAGGTCATTCTGAAGGCCAAGGACTTC
CCACCTGCAGACCCCACCATAAAGCAGAAGCTGATGCCCTGGGTGCTGGCCATGATCCGG
TGA
|
| Enzyme 12 GenBank Gene ID |
X79389  |
| Enzyme 12 GeneCard ID |
GSTT1  |
| Enzyme 12 GenAtlas ID |
GSTT1  |
| Enzyme 12 HGNC ID |
HGNC:4641  |
| Enzyme 12 Chromosome Location |
22 |
| Enzyme 12 Locus |
22q11.23 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6115 |
| Enzyme 13 Name |
Glutathione S-transferase P |
| Enzyme 13 Synonyms |
- GST class-pi
- GSTP1-1
|
| Enzyme 13 Gene Name |
GSTP1 |
| Enzyme 13 Protein Sequence |
>Glutathione S-transferase P
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGD
LTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAY
VGRLSARPKLKAFLASPEYVNLPINGNGKQ
|
| Enzyme 13 Number of Residues |
210 |
| Enzyme 13 Molecular Weight |
23356 |
| Enzyme 13 Theoretical pI |
5.30 |
| 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 |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
31946  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P09211  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
GSTP1_HUMAN  |
| Enzyme 13 PDB ID |
13GS  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>633 bp
ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG
CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG
GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC
CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT
GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC
CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG
AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC
AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG
CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT
GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG
AACCTCCCCATCAATGGCAACGGGAAACAGTGA
|
| Enzyme 13 GenBank Gene ID |
X06547  |
| Enzyme 13 GeneCard ID |
GSTP1  |
| Enzyme 13 GenAtlas ID |
GSTP1  |
| Enzyme 13 HGNC ID |
HGNC:4638  |
| Enzyme 13 Chromosome Location |
11 |
| Enzyme 13 Locus |
11q13 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
13120 |
| Enzyme 14 Name |
Uncharacterized protein GSTZ1 |
| Enzyme 14 Synonyms |
- Glutathione transferase zeta 1
- Maleylacetoacetate isomerase, isoform CRA_a
|
| Enzyme 14 Gene Name |
GSTZ1 |
| Enzyme 14 Protein Sequence |
>Uncharacterized protein GSTZ1
MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
|
| Enzyme 14 Number of Residues |
161 |
| Enzyme 14 Molecular Weight |
17896 |
| Enzyme 14 Theoretical pI |
5.76 |
| Enzyme 14 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 14 General Function |
Posttranslational modification, protein turnover, chaperones |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
A6NNB8  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
A6NNB8_HUMAN  |
| Enzyme 14 PDB ID |
1FW1  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AC007954  |
| Enzyme 14 GeneCard ID |
A6NNB8  |
| Enzyme 14 GenAtlas ID |
GSTZ1  |
| Enzyme 14 HGNC ID |
HGNC:4643  |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
15211 |
| Enzyme 15 Name |
Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b) |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
GSTA3 |
| Enzyme 15 Protein Sequence |
>Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
|
| Enzyme 15 Number of Residues |
222 |
| Enzyme 15 Molecular Weight |
25302 |
| Enzyme 15 Theoretical pI |
9.69 |
| Enzyme 15 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 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
114731581  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q068V6  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
Q068V6_HUMAN  |
| Enzyme 15 PDB ID |
1TDI  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>669 bp
ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA
|
| Enzyme 15 GenBank Gene ID |
DQ993361  |
| Enzyme 15 GeneCard ID |
Q068V6  |
| Enzyme 15 GenAtlas ID |
GSTA3  |
| Enzyme 15 HGNC ID |
HGNC:4628  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
Not Available |
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
15212 |
| Enzyme 16 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 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
GSTM4 |
| Enzyme 16 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 16 Number of Residues |
218 |
| Enzyme 16 Molecular Weight |
25562 |
| Enzyme 16 Theoretical pI |
5.69 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
Not Available |
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
158257192  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
A8K765  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
A8K765_HUMAN  |
| Enzyme 16 PDB ID |
4GTU  |
| Enzyme 16 PDB File |
Show |
| Enzyme 16 3D Structure |
|
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
|
| Enzyme 16 GenBank Gene ID |
AK291880  |
| Enzyme 16 GeneCard ID |
A8K765  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
Not Available |
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
15213 |
| Enzyme 17 Name |
LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056) |
| Enzyme 17 Synonyms |
Not Available |
| Enzyme 17 Gene Name |
LOC51064 |
| Enzyme 17 Protein Sequence |
>LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
|
| Enzyme 17 Number of Residues |
226 |
| Enzyme 17 Molecular Weight |
25497 |
| Enzyme 17 Theoretical pI |
8.69 |
| Enzyme 17 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 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Not Available |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
158260183  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q6FII1  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
Q6FII1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
|
| Enzyme 17 GenBank Gene ID |
AK289580  |
| Enzyme 17 GeneCard ID |
Q6FII1  |
| Enzyme 17 GenAtlas ID |
LOC51064  |
| Enzyme 17 HGNC ID |
HGNC:16906  |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
15214 |
| Enzyme 18 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 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
MGST1 |
| Enzyme 18 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 18 Number of Residues |
155 |
| Enzyme 18 Molecular Weight |
17599 |
| Enzyme 18 Theoretical pI |
9.71 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
Not Available |
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
158255732  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
A8K533  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
A8K533_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>468 bp
ATGGTTGACCTCACCCAGGTAATGGATGATGAAGTATTCATGGCTTTTGCATCCTATGCA
ACAATTATTCTTTCAAAAATGATGCTTATGAGTACTGCAACTGCATTCTATAGATTGACA
AGAAAGGTTTTTGCCAATCCAGAAGACTGTGTAGCATTTGGCAAAGGTGAAAATGCCAAG
AAGTATCTTCGAACAGATGACAGAGTAGAACGTGTACGCAGAGCCCACCTGAATGACCTT
GAAAATATTATTCCATTTCTTGGAATTGGCCTCCTGTATTCCTTGAGTGGTCCCGACCCC
TCTACAGCCATCCTGCACTTCAGACTATTTGTCGGAGCACGGATCTACCACACCATTGCA
TATTTGACACCCCTTCCCCAGCCAAATAGAGCTTTGAGTTTTTTTGTTGGATATGGAGTT
ACTCTTTCCATGGCTTACAGGTTGCTGAAAAGTAAATTGTACCTGTAA
|
| Enzyme 18 GenBank Gene ID |
AK291148  |
| Enzyme 18 GeneCard ID |
A8K533  |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
Not Available |
| Enzyme 18 Chromosome Location |
12 |
| Enzyme 18 Locus |
12p12.3-p12.1 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
Not Available |
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
16492 |
| Enzyme 19 Name |
cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b) |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
GSTA4 |
| Enzyme 19 Protein Sequence |
>cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
|
| Enzyme 19 Number of Residues |
222 |
| Enzyme 19 Molecular Weight |
25705 |
| Enzyme 19 Theoretical pI |
8.72 |
| Enzyme 19 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 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
B2RD15  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
B2RD15_HUMAN  |
| Enzyme 19 PDB ID |
1GUM  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AK315369  |
| Enzyme 19 GeneCard ID |
B2RD15  |
| Enzyme 19 GenAtlas ID |
Not Available |
| Enzyme 19 HGNC ID |
Not Available |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
16493 |
| Enzyme 20 Name |
cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a) |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
MGST3 |
| Enzyme 20 Protein Sequence |
>cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRA
HQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSI
ALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH
|
| Enzyme 20 Number of Residues |
152 |
| Enzyme 20 Molecular Weight |
16516 |
| Enzyme 20 Theoretical pI |
9.68 |
| Enzyme 20 GO Classification |
Not Available |
| Enzyme 20 General Function |
Not Available |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
B2R592  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
B2R592_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AK312103  |
| Enzyme 20 GeneCard ID |
B2R592  |
| Enzyme 20 GenAtlas ID |
Not Available |
| Enzyme 20 HGNC ID |
Not Available |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
Not Available |
| Enzyme 20 Metabolite References |
Not Available |