GSTA2

GSTA2
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1AGS, 2VCT, 2WJU, 4ACS
Identifiers
Aliases	GSTA2 , GST2, GSTA2-2, GTA2, GTH2, glutathione S-transferase alpha 2
External IDs	OMIM: 138360 HomoloGene: 47952 GeneCards: GSTA2
Gene location (Human)
Chr.	Chromosome 6 (human)
End	52,763,475 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; duodenum; ; gallbladder; ; islet of Langerhans; ; liver; ; kidney; ; right lobe of liver; ; trachea; ; Right adrenal gland; ; metanephros;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity ; glutathione transferase activity ; protein binding ;
Cellular component	cytoplasm ; cytosol ; extracellular exosome ;
Biological process	metabolism ; epithelial cell differentiation ; glutathione derivative biosynthetic process ; glutathione metabolic process ; interleukin-12-mediated signaling pathway ; xenobiotic metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	2939
	n/a
	ENSG00000244067
	n/a
	P09210
	n/a
	NM_000846
	n/a
	NP_000837
	n/a
	Wikidata
View/Edit Human

Last updated March 04, 2023

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.^[3]

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.^[3]

Related Research Articles

Glutathione <i>S</i>-transferase Family of enzymes

Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase is an enzyme that in humans is encoded by the AGA gene.

<span class="mw-page-title-main">Glutathione S-transferase A1</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial is an enzyme that in humans is encoded by the DBT gene.

Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.

Glutamate-cysteine ligase regulatory subunit is an enzyme that in humans is encoded by the GCLM gene.

Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene.

Glutathione S-transferase M3 (brain), also known as GSTM2, is an enzyme which in humans is encoded by the GSTM99

Meprin A subunit alpha also known as endopeptidase-2 or PABA peptide hydrolase is the alpha subunit of the meprin A enzyme that in humans is encoded by the MEP1A gene. The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.

Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.

Glutathione S-transferase theta-2 is an enzyme that in humans is encoded by the GSTT2 gene.

UDP glucuronosyltransferase 2 family, polypeptide B4, also known as UGT2B4, is an enzyme that in humans is encoded by the UGT2B4 gene.

Glutathione S-transferase Zeta 1 is an enzyme that in humans is encoded by the GSTZ1 gene on chromosome 14.

Meprin A subunit beta is a protein that in humans is encoded by the MEP1B gene.

Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene.

The RPS2 gene is the gene which, in humans, encodes the 40S ribosomal protein S2.

Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene.

Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene.

D-aspartate oxidase is an enzyme that is encoded by the DDO gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000244067 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: GSTA2 glutathione S-transferase A2".

Röhrdanz E, Nguyen T, Pickett CB (1992). "Isolation and characterization of the human glutathione S-transferase A2 subunit gene". Arch. Biochem. Biophys. 298 (2): 747–52. doi:10.1016/0003-9861(92)90475-C. PMID 1329668.
Stenberg G, Björnestedt R, Mannervik B (1992). "Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line". Protein Expr. Purif. 3 (1): 80–4. doi:10.1016/1046-5928(92)90060-A. PMID 1330133.
Klöne A, Hussnätter R, Sies H (1992). "Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2". Biochem. J. 285 (3): 925–8. doi:10.1042/bj2850925. PMC 1132883 . PMID 1497629.
Bogaards JJ, van Ommen B, van Bladeren PJ (1992). "Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea". Biochem. J. 286 (2): 383–8. doi:10.1042/bj2860383. PMC 1132909 . PMID 1530570.
Strange RC, Fryer AA, Matharoo B, et al. (1992). "The human glutathione S-transferases: comparison of isoenzyme expression in normal and astrocytoma brain". Biochim. Biophys. Acta. 1139 (3): 222–8. doi:10.1016/0925-4439(92)90138-D. PMID 1627661.
Hayes JD, Kerr LA, Cronshaw AD (1990). "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. 264 (2): 437–45. doi:10.1042/bj2640437. PMC 1133600 . PMID 2604726.
Board PG, Webb GC (1987). "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. 84 (8): 2377–81. Bibcode:1987PNAS...84.2377B. doi: 10.1073/pnas.84.8.2377 . PMC 304654 . PMID 3031680.
Rhoads DM, Zarlengo RP, Tu CP (1987). "The basic glutathione S-transferases from human livers are products of separate genes". Biochem. Biophys. Res. Commun. 145 (1): 474–81. doi:10.1016/0006-291X(87)91345-3. PMID 3036131.
Chow NW, Whang-Peng J, Kao-Shan CS, et al. (1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities". J. Biol. Chem. 263 (26): 12797–800. doi: 10.1016/S0021-9258(18)37626-9 . PMID 3138230.
Tu CP, Qian B (1988). "Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA". Biochem. Soc. Trans. 15 (4): 734–6. doi:10.1042/bst0150734. PMID 3678589.
Tu CP, Qian B (1987). "Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA". Biochem. Biophys. Res. Commun. 141 (1): 229–37. doi:10.1016/S0006-291X(86)80358-8. PMID 3800996.
Satoh K, Kitahara A, Sato K (1985). "Identification of heterogeneous and microheterogeneous subunits of glutathione S-transferase in rat liver cytosol". Arch. Biochem. Biophys. 242 (1): 104–11. doi:10.1016/0003-9861(85)90484-9. PMID 3901925.
Zeng K, Rose JP, Chen HC, et al. (1995). "A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal". Proteins. 20 (3): 259–63. doi:10.1002/prot.340200306. PMID 7892174. S2CID 10910971.
Anttila S, Hirvonen A, Vainio H, et al. (1994). "Immunohistochemical localization of glutathione S-transferases in human lung". Cancer Res. 53 (23): 5643–8. PMID 8242618.
Suzuki T, Johnston PN, Board PG (1994). "Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes". Genomics. 18 (3): 680–6. doi:10.1016/S0888-7543(05)80373-8. PMID 8307579.
Ahmad H, Singhal SS, Saxena M, Awasthi YC (1993). "Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver". Biochim. Biophys. Acta. 1161 (2–3): 333–6. doi:10.1016/0167-4838(93)90234-i. PMID 8431482.
Rowe JD, Nieves E, Listowsky I (1997). "Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera". Biochem. J. 325 (2): 481–6. doi:10.1042/bj3250481. PMC 1218585 . PMID 9230131.
Coles BF, Anderson KE, Doerge DR, et al. (2000). "Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype". Cancer Res. 60 (3): 573–9. PMID 10676639.
Tetlow N, Liu D, Board P (2001). "Polymorphism of human Alpha class glutathione transferases". Pharmacogenetics. 11 (7): 609–17. doi:10.1097/00008571-200110000-00007. PMID 11668220.
Coles BF, Morel F, Rauch C, et al. (2002). "Effect of polymorphism in the human glutathione S-transferase A1 promoter on hepatic GSTA1 and GSTA2 expression". Pharmacogenetics. 11 (8): 663–9. doi:10.1097/00008571-200111000-00004. PMID 11692074.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000244067 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-3] 1 2 "Entrez Gene: GSTA2 glutathione S-transferase A2".

[1]

[2]

[3]

GSTA2

Related Research Articles

References

Further reading