Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2gene.[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. 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.[5]
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. PMID1329668.
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. PMID1330133.
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. PMID1627661.
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. PMID3036131.
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. PMID3678589.
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. PMID3800996.
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. PMID3901925.
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. PMID7892174. S2CID10910971.
Anttila S, Hirvonen A, Vainio H, et al. (1994). "Immunohistochemical localization of glutathione S-transferases in human lung". Cancer Res. 53 (23): 5643–8. PMID8242618.
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. PMID8307579.
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. PMID8431482.
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. PMID10676639.
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. PMID11692074.
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
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
Informasi ini disarikan dari Wikipedia dan disajikan kembali untuk tujuan edukasi. Konten tersedia di bawah lisensi CC BY-SA 3.0. Kami tidak bertanggung jawab atas ketidakakuratan data yang bersumber dari kontribusi publik tersebut.
The information displayed on this website is sourced in part or in whole from Wikipedia and has been adapted for the purpose of restating it. We strive to provide accurate and relevant information, however:
There is no guarantee of absolute accuracy. Wikipedia is an open, collaborative project that can be edited by anyone, so information is subject to change.
It is not intended to constitute professional advice. The content displayed is for informational and educational purposes only. For important decisions (e.g., medical, legal, or financial), please consult a professional.
Content copyright. Wikipedia is licensed under the Creative Commons Attribution-ShareAlike License (CC BY-SA). This means that content may be reused with appropriate attribution and shared under a similar license.
Responsible use. Any risk arising from the use of information from this website is entirely the responsibility of the user.
