Glutathione S Transferase Mu 2, Muscle (GSTm2)

GST-M2; GST4; GSTM2-2; GTHMUS

SPN	W154
HGNC	4634
MGI	1915562
PubMed	10927022
RGD	2756
UniProt	P28161
Wiki	GSTM2

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. 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.

GSTM2functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and 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 certain drugs.

Reference

"Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus."
Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and biological annotation of human chromosome 1."
Nature 441:315-321(2006) [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]

"Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript."
Biochem. J. 294:373-380(1993) [PubMed] [Europe PMC] [Abstract]

, Submitted (MAR-2007) to UniProtKB

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity."
J. Mol. Biol. 238:815-832(1994) [PubMed] [Europe PMC] [Abstract]

"Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution."
Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006) [PubMed] [Europe PMC] [Abstract]

"Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
Cancer Res. 69:8025-8034(2009) [PubMed] [Europe PMC] [Abstract]