Glutathione S Transferase Alpha 1 (GSTa1)

GSTA1; GST2; GSTA1-1; GTH1; GST class-alpha member 1; GST HA subunit 1; GST-epsilon; Glutathione S-transferase A1, N-terminally processed

SPN	W201
HGNC	4626
MGI	1095417
PubMed	10433206
RGD	2753
UniProt	P08263
Wiki	GSTA1

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.

GSTa1 encodes a glutathione S-tranferase 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.

 

Reference

"Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA."
Biochem. Biophys. Res. Commun. 141:229-237(1986) [PubMed] [Europe PMC] [Abstract]

"The basic glutathione S-transferases from human livers are products of separate genes."
Biochem. Biophys. Res. Commun. 145:474-481(1987) [PubMed] [Europe PMC] [Abstract]

"Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA."
Biochem. Soc. Trans. 15:734-736(1987) [PubMed] [Europe PMC] [Abstract]

"Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12."
Proc. Natl. Acad. Sci. U.S.A. 84:2377-2381(1987) [PubMed] [Europe PMC] [Abstract]

"Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene."
Arch. Biochem. Biophys. 292:589-593(1992) [PubMed] [Europe PMC] [Abstract]

"Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line."
Protein Expr. Purif. 3:80-84(1992) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities."
J. Biol. Chem. 263:12797-12800(1988) [PubMed] [Europe PMC] [Abstract]

"Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver."
Biochim. Biophys. Acta 1161:333-336(1993) [PubMed] [Europe PMC] [Abstract]

"Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other alpha class glutathione S-transferases."
Biochem. J. 264:437-445(1989) [PubMed] [Europe PMC] [Abstract]

"The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase."
Biochem. J. 275:171-174(1991) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes."
J. Mol. Biol. 232:192-212(1993) [PubMed] [Europe PMC] [Abstract]

"Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate."
Structure 3:717-727(1995) [PubMed] [Europe PMC] [Abstract]

"1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site."
Proteins 48:618-627(2002) [PubMed] [Europe PMC] [Abstract]

"Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1."
Proc. Natl. Acad. Sci. U.S.A. 101:13163-13167(2004) [PubMed] [Europe PMC] [Abstract]

"Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study."
J. Mol. Biol. 349:825-838(2005) [PubMed] [Europe PMC] [Abstract]

"New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix."
Acta Crystallogr. D 62:197-207(2006) [PubMed] [Europe PMC] [Abstract]

"Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals."
Biochemistry 48:7698-7704(2009) [PubMed] [Europe PMC] [Abstract]

"The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function."
Acta Crystallogr. F 66:776-780(2010) [PubMed] [Europe PMC] [Abstract]