Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1gene.[5]
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 (hepatocytes) and kidney (proximal tubules). 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.[6]
Release of GST-A1 as an indication of cellular necrosis
Increases in serum and urinary GST-A1 have been found in association with hepatocyte and renal proximal tubular necrosis respectively, and have potential for monitoring injury to these tissues.[7][8]
^Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA (January 1998). "Plasma glutathione S-transferase alpha 1-1: a more sensitive marker for hepatocellular damage than serum alanine aminotransferase in hypertensive disorders of pregnancy". American Journal of Obstetrics and Gynecology. 178 (1 Pt 1): 161–5. doi:10.1016/S0002-9378(98)70645-3. PMID9465822.
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Suzuki T, Smith S, Board PG (1994). "Structure and function of the 5' flanking sequences of the human alpha class glutathione S-transferase genes". Biochem. Biophys. Res. Commun. 200 (3): 1665–71. doi:10.1006/bbrc.1994.1643. PMID8185623.
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1ags: 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
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
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