Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene.[5][6][7]

GSTA3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGSTA3, GSTA3-3, GTA3, glutathione S-transferase alpha 3
External IDsOMIM: 605449; MGI: 95856; HomoloGene: 37355; GeneCards: GSTA3; OMA:GSTA3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000847
NM_001363542

NM_001077353
NM_001288617
NM_010356

RefSeq (protein)

NP_000838
NP_001350471

NP_001070821
NP_001275546
NP_034486

Location (UCSC)Chr 6: 52.9 – 52.91 MbChr 1: 21.31 – 21.34 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. 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 genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000174156Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025934Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Suzuki T, Johnston PN, Board PG (Mar 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.
  6. ^ Board PG (Apr 1998). "Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4". Biochem J. 330 (2): 827–31. doi:10.1042/bj3300827. PMC 1219212. PMID 9480897.
  7. ^ a b "Entrez Gene: GSTA3 glutathione S-transferase A3".

Further reading

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