Entry - *138380 - GLUTATHIONE S-TRANSFERASE, MU-2; GSTM2 - OMIM
 
* 138380

GLUTATHIONE S-TRANSFERASE, MU-2; GSTM2


Alternative titles; symbols

GLUTATHIONE S-TRANSFERASE 4; GST4
GLUTATHIONE S-TRANSFERASE M2
GST, MUSCLE; GSTM


HGNC Approved Gene Symbol: GSTM2

Cytogenetic location: 1p13.3     Genomic coordinates (GRCh38): 1:109,668,057-109,683,997 (from NCBI)


TEXT

Description

The glutathione S-transferases (GST; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens (Mannervik, 1985). This enzyme catalyzes the reaction of glutathione with a wide variety of organic compounds to form thioethers, a reaction that is sometimes a first step in a detoxification process leading to mercapturic acid formation.

Based on amino acid sequence similarities and antibody cross-reactivities, the mammalian cytosolic GSTs are divided into several classes, including alpha (e.g., 138359), mu (e.g., 138350), kappa (602321), theta (e.g., 600436), pi (134660), omega (605482), and zeta (603758). In addition, there is a class of microsomal GSTs (e.g., 138330). Each class is encoded by a single gene or a gene family.


Cloning and Expression

In muscle extracts, Van Cong et al. (1984) observed a novel GST band (called GST4, or GSTM2), which migrated between GST3 (GSTP1; 134660) and GST1 (GSTM1; 138350). No polymorphism was noted. The formation of heterodimeric bands with GSTM1 indicated that GSTM2 is a dimeric enzyme and that it is controlled by a separate gene. GSTM1, GSTM2, and GSTM3 (138390) are class mu isoenzymes. GSTM1 encodes an enzyme expressed in liver and peripheral blood, while the products of GSTM2 and GSTM3 are expressed in muscle and brain, respectively.

Vorachek et al. (1991) isolated a cDNA for GSTM2 from a human myoblast cDNA library and determined its sequence. The deduced 217-amino acid protein has a molecular mass of 25,599 Da. It shares 84.8% sequence identity with the GSTM1 protein.


Mapping

Taylor et al. (1991) demonstrated that GSTM2 and GSTM4 (138333) are located on the same cosmid. Pearson et al. (1993) isolated a YAC clone containing all 5 GSTM genes, GSTM1-5; using this clone, they mapped all of these genes to 1p13.3 by fluorescence in situ hybridization.


REFERENCES

  1. Mannervik, B. The isozymes of glutathione transferase. Adv. Enzymol. Relat. Areas Molec. Biol. 57: 357-417, 1985. [PubMed: 3898742, related citations] [Full Text]

  2. Pearson, W. R., Vorachek, W. R., Xu, S., Berger, R., Hart, I., Vannais, D., Patterson, D. Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am. J. Hum. Genet. 53: 220-233, 1993. [PubMed: 8317488, related citations]

  3. Taylor, J. B., Oliver, J., Sherrington, R., Pemble, S. E. Structure of human glutathione S-transferase class mu genes. Biochem. J. 274: 587-593, 1991. [PubMed: 2006920, related citations] [Full Text]

  4. Van Cong, N., Laisney, V., Gross, M. S., Frezal, J. Glutathione-S-transferases--tissues distribution, number of loci, polymorphism, chromosome localization. (Abstract) Cytogenet. Cell Genet. 37: 554 only, 1984.

  5. Vorachek, W. R., Pearson, W. R., Rule, G. S. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Nat. Acad. Sci. 88: 4443-4447, 1991. [PubMed: 2034681, related citations] [Full Text]


Creation Date:
Victor A. McKusick : 6/4/1986
carol : 11/21/2019
carol : 09/22/2008
alopez : 5/1/2003
psherman : 6/17/1998
alopez : 2/6/1998
alopez : 6/4/1997
carol : 5/11/1994
carol : 12/22/1993
carol : 12/20/1993
carol : 10/13/1993
supermim : 3/16/1992
carol : 2/17/1992

* 138380

GLUTATHIONE S-TRANSFERASE, MU-2; GSTM2


Alternative titles; symbols

GLUTATHIONE S-TRANSFERASE 4; GST4
GLUTATHIONE S-TRANSFERASE M2
GST, MUSCLE; GSTM


HGNC Approved Gene Symbol: GSTM2

Cytogenetic location: 1p13.3     Genomic coordinates (GRCh38): 1:109,668,057-109,683,997 (from NCBI)


TEXT

Description

The glutathione S-transferases (GST; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens (Mannervik, 1985). This enzyme catalyzes the reaction of glutathione with a wide variety of organic compounds to form thioethers, a reaction that is sometimes a first step in a detoxification process leading to mercapturic acid formation.

Based on amino acid sequence similarities and antibody cross-reactivities, the mammalian cytosolic GSTs are divided into several classes, including alpha (e.g., 138359), mu (e.g., 138350), kappa (602321), theta (e.g., 600436), pi (134660), omega (605482), and zeta (603758). In addition, there is a class of microsomal GSTs (e.g., 138330). Each class is encoded by a single gene or a gene family.


Cloning and Expression

In muscle extracts, Van Cong et al. (1984) observed a novel GST band (called GST4, or GSTM2), which migrated between GST3 (GSTP1; 134660) and GST1 (GSTM1; 138350). No polymorphism was noted. The formation of heterodimeric bands with GSTM1 indicated that GSTM2 is a dimeric enzyme and that it is controlled by a separate gene. GSTM1, GSTM2, and GSTM3 (138390) are class mu isoenzymes. GSTM1 encodes an enzyme expressed in liver and peripheral blood, while the products of GSTM2 and GSTM3 are expressed in muscle and brain, respectively.

Vorachek et al. (1991) isolated a cDNA for GSTM2 from a human myoblast cDNA library and determined its sequence. The deduced 217-amino acid protein has a molecular mass of 25,599 Da. It shares 84.8% sequence identity with the GSTM1 protein.


Mapping

Taylor et al. (1991) demonstrated that GSTM2 and GSTM4 (138333) are located on the same cosmid. Pearson et al. (1993) isolated a YAC clone containing all 5 GSTM genes, GSTM1-5; using this clone, they mapped all of these genes to 1p13.3 by fluorescence in situ hybridization.


REFERENCES

  1. Mannervik, B. The isozymes of glutathione transferase. Adv. Enzymol. Relat. Areas Molec. Biol. 57: 357-417, 1985. [PubMed: 3898742] [Full Text: https://doi.org/10.1002/9780470123034.ch5]

  2. Pearson, W. R., Vorachek, W. R., Xu, S., Berger, R., Hart, I., Vannais, D., Patterson, D. Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am. J. Hum. Genet. 53: 220-233, 1993. [PubMed: 8317488]

  3. Taylor, J. B., Oliver, J., Sherrington, R., Pemble, S. E. Structure of human glutathione S-transferase class mu genes. Biochem. J. 274: 587-593, 1991. [PubMed: 2006920] [Full Text: https://doi.org/10.1042/bj2740587]

  4. Van Cong, N., Laisney, V., Gross, M. S., Frezal, J. Glutathione-S-transferases--tissues distribution, number of loci, polymorphism, chromosome localization. (Abstract) Cytogenet. Cell Genet. 37: 554 only, 1984.

  5. Vorachek, W. R., Pearson, W. R., Rule, G. S. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Nat. Acad. Sci. 88: 4443-4447, 1991. [PubMed: 2034681] [Full Text: https://doi.org/10.1073/pnas.88.10.4443]


Creation Date:
Victor A. McKusick : 6/4/1986

Edit History:
carol : 11/21/2019
carol : 09/22/2008
alopez : 5/1/2003
psherman : 6/17/1998
alopez : 2/6/1998
alopez : 6/4/1997
carol : 5/11/1994
carol : 12/22/1993
carol : 12/20/1993
carol : 10/13/1993
supermim : 3/16/1992
carol : 2/17/1992