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'''Glutathione S-transferase Mu 2''' is an [[enzyme]] that in humans is encoded by the ''GSTM2'' [[gene]].<ref name="pmid2034681">{{cite journal |vauthors=Vorachek WR, Pearson WR, Rule GS | title = Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus | journal = Proc Natl Acad Sci U S A | volume = 88 | issue = 10 | pages = 4443–7 |date=Jun 1991 | pmid = 2034681 | pmc = 51676 | doi =10.1073/pnas.88.10.4443 }}</ref><ref name="pmid2345169">{{cite journal |vauthors=Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I | title = A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes | journal = J Biol Chem | volume = 265 | issue = 16 | pages = 9188–93 |date=Jul 1990 | pmid = 2345169 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GSTM2 glutathione S-transferase M2 (muscle)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2946| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_GSTM2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hna.
| PDB = {{PDB2|1hna}}, {{PDB2|1hnb}}, {{PDB2|1hnc}}, {{PDB2|1xw5}}, {{PDB2|1ykc}}, {{PDB2|2ab6}}, {{PDB2|2c4j}}, {{PDB2|2gtu}}, {{PDB2|3gtu}}
| Name = Glutathione S-transferase M2 (muscle)
| HGNCid = 4634
| Symbol = GSTM2
| AltSymbols =; GST4; GSTM; GSTM2-2; GTHMUS; MGC117303
| OMIM = 138380
| ECnumber =
| Homologene = 41816
| MGIid = 1915562
| Function = {{GNF_GO|id=GO:0004364 |text = glutathione transferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
  | Component =
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2946
    | Hs_Ensembl =
    | Hs_RefseqProtein = NP_000839
    | Hs_RefseqmRNA = NM_000848
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =   
    | Mm_EntrezGene = 68312
    | Mm_Ensembl = ENSMUSG00000004035
    | Mm_RefseqmRNA = XM_359308
    | Mm_RefseqProtein = XP_359308
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 108054391
    | Mm_GenLoc_end = 108059801
    | Mm_Uniprot = 
  }}
}}
'''Glutathione S-transferase M2 (muscle)''', also known as '''GSTM2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GSTM2 glutathione S-transferase M2 (muscle)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2946| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = 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. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions 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.<ref name="entrez">{{cite web | title = Entrez Gene: GSTM2 glutathione S-transferase M2 (muscle)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2946| accessdate = }}</ref>
| summary_text = 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. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bogaards JJ, van Ommen B, van Bladeren PJ |title=Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea. |journal=Biochem. J. |volume=286 ( Pt 2) |issue=  |pages= 383-8 |year= 1992 |pmid= 1530570 |doi=  }}
*{{cite journal  |vauthors=Bogaards JJ, van Ommen B, van Bladeren PJ |title=Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea. | series=286 |journal=Biochem. J. |volume=( Pt 2) |issue=  |pages= 383–8 |year= 1992 |pmid= 1530570 |doi= | pmc=1132909 }}
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi=  }}
*{{cite journal  |vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4 }}
*{{cite journal  | author=Taylor JB, Oliver J, Sherrington R, Pemble SE |title=Structure of human glutathione S-transferase class Mu genes. |journal=Biochem. J. |volume=274 ( Pt 2) |issue=  |pages= 587-93 |year= 1991 |pmid= 2006920 |doi=  }}
*{{cite journal  |vauthors=Taylor JB, Oliver J, Sherrington R, Pemble SE |title=Structure of human glutathione S-transferase class Mu genes. | series=274 |journal=Biochem. J. |volume=( Pt 2) |issue=  |pages= 587–93 |year= 1991 |pmid= 2006920 |doi=  | pmc=1150179  }}
*{{cite journal  | author=Vorachek WR, Pearson WR, Rule GS |title=Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 10 |pages= 4443-7 |year= 1991 |pmid= 2034681 |doi=  }}
*{{cite journal  |author1=Laisney V |author2=Nguyen Van Cong |author3=Gross MS |author4=Frezal J |title=Human genes for glutathione S-transferases. |journal=Hum. Genet. |volume=68 |issue= 3 |pages= 221–7 |year= 1985 |pmid= 6500576 |doi=10.1007/BF00418392 }}
*{{cite journal | author=Campbell E, Takahashi Y, Abramovitz M, ''et al.'' |title=A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 9188-93 |year= 1990 |pmid= 2345169 |doi= }}
*{{cite journal   |vauthors=Raghunathan S, Chandross RJ, Kretsinger RH, etal |title=Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. |journal=J. Mol. Biol. |volume=238 |issue= 5 |pages= 815–32 |year= 1994 |pmid= 8182750 |doi= 10.1006/jmbi.1994.1336 }}
*{{cite journal | author=Laisney V, Nguyen Van Cong , Gross MS, Frezal J |title=Human genes for glutathione S-transferases. |journal=Hum. Genet. |volume=68 |issue= 3 |pages= 221-7 |year= 1985 |pmid= 6500576 |doi=  }}
*{{cite journal   |vauthors=Anttila S, Hirvonen A, Vainio H, etal |title=Immunohistochemical localization of glutathione S-transferases in human lung. |journal=Cancer Res. |volume=53 |issue= 23 |pages= 5643–8 |year= 1994 |pmid= 8242618 |doi=  }}
*{{cite journal | author=Raghunathan S, Chandross RJ, Kretsinger RH, ''et al.'' |title=Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. |journal=J. Mol. Biol. |volume=238 |issue= 5 |pages= 815-32 |year= 1994 |pmid= 8182750 |doi= 10.1006/jmbi.1994.1336 }}
*{{cite journal   |vauthors=Pearson WR, Vorachek WR, Xu SJ, etal |title=Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. |journal=Am. J. Hum. Genet. |volume=53 |issue= 1 |pages= 220–33 |year= 1993 |pmid= 8317488 |doi= | pmc=1682241  }}
*{{cite journal  | author=Anttila S, Hirvonen A, Vainio H, ''et al.'' |title=Immunohistochemical localization of glutathione S-transferases in human lung. |journal=Cancer Res. |volume=53 |issue= 23 |pages= 5643-8 |year= 1994 |pmid= 8242618 |doi=  }}
*{{cite journal  |vauthors=Ross VL, Board PG |title=Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. | series=294 |journal=Biochem. J. |volume=( Pt 2) |issue= |pages= 373–80 |year= 1993 |pmid= 8373352 |doi=  | pmc=1134464  }}
*{{cite journal | author=Pearson WR, Vorachek WR, Xu SJ, ''et al.'' |title=Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. |journal=Am. J. Hum. Genet. |volume=53 |issue= 1 |pages= 220-33 |year= 1993 |pmid= 8317488 |doi=  }}
*{{cite journal   |vauthors=Baez S, Segura-Aguilar J, Widersten M, etal |title=Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. | series=324 |journal=Biochem. J. |volume=( Pt 1) |issue= |pages= 25–8 |year= 1997 |pmid= 9164836 |doi= | pmc=1218396 }}
*{{cite journal  | author=Ross VL, Board PG |title=Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. |journal=Biochem. J. |volume=294 ( Pt 2) |issue= |pages= 373-80 |year= 1993 |pmid= 8373352 |doi=  }}
*{{cite journal  |vauthors=Xu S, Wang Y, Roe B, Pearson WR |title=Characterization of the human class Mu glutathione S-transferase gene cluster and the GSTM1 deletion. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3517–27 |year= 1998 |pmid= 9452477 |doi=10.1074/jbc.273.6.3517 }}
*{{cite journal | author=Baez S, Segura-Aguilar J, Widersten M, ''et al.'' |title=Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. |journal=Biochem. J. |volume=324 ( Pt 1) |issue= |pages= 25-8 |year= 1997 |pmid= 9164836 |doi=  }}
*{{cite journal   |vauthors=Patskovska LN, Fedorov AA, Patskovsky YV, etal |title=Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2. |journal=Acta Crystallogr. D |volume=54 |issue= Pt 3 |pages= 458–60 |year= 1998 |pmid= 9761928 |doi=10.1107/S0907444997011190 }}
*{{cite journal | author=Xu S, Wang Y, Roe B, Pearson WR |title=Characterization of the human class Mu glutathione S-transferase gene cluster and the GSTM1 deletion. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3517-27 |year= 1998 |pmid= 9452477 |doi=  }}
*{{cite journal   |vauthors=Coles BF, Anderson KE, Doerge DR, etal |title=Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype. |journal=Cancer Res. |volume=60 |issue= 3 |pages= 573–9 |year= 2000 |pmid= 10676639 |doi=  }}
*{{cite journal | author=Patskovska LN, Fedorov AA, Patskovsky YV, ''et al.'' |title=Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=54 |issue= Pt 3 |pages= 458-60 |year= 1998 |pmid= 9761928 |doi=  }}
*{{cite journal   |vauthors=Luo JK, Hornby JA, Wallace LA, etal |title=Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases. |journal=Protein Sci. |volume=11 |issue= 9 |pages= 2208–17 |year= 2003 |pmid= 12192076 |doi=10.1110/ps.0208002  | pmc=2373595 }}
*{{cite journal | author=Coles BF, Anderson KE, Doerge DR, ''et al.'' |title=Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype. |journal=Cancer Res. |volume=60 |issue= 3 |pages= 573-9 |year= 2000 |pmid= 10676639 |doi= }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal | author=Luo JK, Hornby JA, Wallace LA, ''et al.'' |title=Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases. |journal=Protein Sci. |volume=11 |issue= 9 |pages= 2208-17 |year= 2003 |pmid= 12192076 |doi= }}
*{{cite journal   |vauthors=Ivarsson Y, Mackey AJ, Edalat M, etal |title=Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8733–8 |year= 2003 |pmid= 12486119 |doi= 10.1074/jbc.M211776200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=De Maria F, Pedersen JZ, Caccuri AM, etal |title=The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42283–93 |year= 2004 |pmid= 12871945 |doi= 10.1074/jbc.M305568200 }}
*{{cite journal | author=Ivarsson Y, Mackey AJ, Edalat M, ''et al.'' |title=Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8733-8 |year= 2003 |pmid= 12486119 |doi= 10.1074/jbc.M211776200 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=De Maria F, Pedersen JZ, Caccuri AM, ''et al.'' |title=The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42283-93 |year= 2004 |pmid= 12871945 |doi= 10.1074/jbc.M305568200 }}
*{{cite journal   |vauthors=Weng MW, Hsiao YM, Chiou HL, etal |title=Alleviation of benzo[a]pyrene-diolepoxide-DNA damage in human lung carcinoma by glutathione S-transferase M2. |journal=DNA Repair (Amst.) |volume=4 |issue= 4 |pages= 493–502 |year= 2005 |pmid= 15725629 |doi= 10.1016/j.dnarep.2004.12.006 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Weng MW, Hsiao YM, Chiou HL, ''et al.'' |title=Alleviation of benzo[a]pyrene-diolepoxide-DNA damage in human lung carcinoma by glutathione S-transferase M2. |journal=DNA Repair (Amst.) |volume=4 |issue= 4 |pages= 493-502 |year= 2005 |pmid= 15725629 |doi= 10.1016/j.dnarep.2004.12.006 }}
}}
}}
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{{refend}}
{{PDB Gallery|geneid=2946}}
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Latest revision as of 09:07, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Wikidata
View/Edit Human

Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene.[1][2][3]

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. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions 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.[3]

References

  1. ↑ Vorachek WR, Pearson WR, Rule GS (Jun 1991). "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 (10): 4443–7. doi:10.1073/pnas.88.10.4443. PMC 51676. PMID 2034681.
  2. ↑ Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I (Jul 1990). "A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes". J Biol Chem. 265 (16): 9188–93. PMID 2345169.
  3. ↑ 3.0 3.1 "Entrez Gene: GSTM2 glutathione S-transferase M2 (muscle)".

Further reading



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