Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3gene.[5][6][7]
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]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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. PMID8307579.
Tetlow N, Coggan M, Casarotto MG, Board PG (2005). "Functional polymorphism of human glutathione transferase A3: effects on xenobiotic metabolism and steroid biosynthesis". Pharmacogenetics. 14 (10): 657–63. doi:10.1097/00008571-200410000-00003. PMID15454730.
Gu Y, Guo J, Pal A, et al. (2005). "Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity". Biochemistry. 43 (50): 15673–9. doi:10.1021/bi048757g. PMID15595823.
Suzuki T, Delgado-Escueta AV, Alonso ME, et al. (2006). "Mutation analyses of genes on 6p12-p11 in patients with juvenile myoclonic epilepsy". Neurosci. Lett. 405 (1–2): 126–31. doi:10.1016/j.neulet.2006.06.038. PMID16876319. S2CID20526126.
1gsd: GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM
1gse: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)
1gsf: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID
1guh: STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES
1k3l: Crystal Structure Analysis of S-hexyl-glutathione Complex of Glutathione Transferase at 1.5 Angstroms Resolution
1k3o: Crystal Structure Analysis of apo Glutathione S-Transferase
1k3y: Crystal Structure Analysis of human Glutathione S-transferase with S-hexyl glutatione and glycerol at 1.3 Angstrom
1pkw: Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione
1pkz: Crystal structure of human glutathione transferase (GST) A1-1
1pl1: Crystal structure of human glutathione transferase (GST) A1-1 in complex with a decarboxy-glutathione
1pl2: Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione
1tdi: Crystal Structure of hGSTA3-3 in Complex with Glutathione
1usb: RATIONAL DESIGN OF A NOVEL ENZYME - EFFICIENT THIOESTER HYDROLYSIS ENABLED BY THE INCORPORATION OF A SINGLE HIS RESIDUE INTO HUMAN GLUTATHIONE TRANSFERASE A1-1
1xwg: Human GST A1-1 T68E mutant
1ydk: Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione