- GSTA3
Glutathione S-transferase A3, also known as GSTA3, is a human
gene .cite web | title = Entrez Gene: GSTA3 glutathione S-transferase A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2940| accessdate = ]PBB_Summary
section_title =
summary_text = 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-tranferase 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.cite web | title = Entrez Gene: GSTA3 glutathione S-transferase A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2940| accessdate = ]References
Further reading
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citations =
*cite journal | author=Suzuki T, Johnston PN, Board PG |title=Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. |journal=Genomics |volume=18 |issue= 3 |pages= 680–6 |year= 1994 |pmid= 8307579 |doi=
*cite journal | author=Board PG |title=Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. |journal=Biochem. J. |volume=330 ( Pt 2) |issue= |pages= 827–31 |year= 1998 |pmid= 9480897 |doi=
*cite journal | author=Johansson AS, Mannervik B |title=Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 33061–5 |year= 2001 |pmid= 11418619 |doi= 10.1074/jbc.M104539200
*cite journal | author=Johansson AS, Mannervik B |title=Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16648–54 |year= 2002 |pmid= 11872752 |doi= 10.1074/jbc.M201062200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Tetlow N, Coggan M, Casarotto MG, Board PG |title=Functional polymorphism of human glutathione transferase A3: effects on xenobiotic metabolism and steroid biosynthesis. |journal=Pharmacogenetics |volume=14 |issue= 10 |pages= 657–63 |year= 2005 |pmid= 15454730 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Gu Y, Guo J, Pal A, "et al." |title=Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity. |journal=Biochemistry |volume=43 |issue= 50 |pages= 15673–9 |year= 2005 |pmid= 15595823 |doi= 10.1021/bi048757g
*cite journal | author=Suzuki T, Delgado-Escueta AV, Alonso ME, "et al." |title=Mutation analyses of genes on 6p12-p11 in patients with juvenile myoclonic epilepsy. |journal=Neurosci. Lett. |volume=405 |issue= 1-2 |pages= 126–31 |year= 2006 |pmid= 16876319 |doi= 10.1016/j.neulet.2006.06.038PBB_Controls
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