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Identification
HMDB Protein ID HMDBP00819
Secondary Accession Numbers
  • 6100
Name Glutathione S-transferase Mu 4
Synonyms
  1. GST class-mu 4
  2. GST-Mu2
  3. GSTM4-4
Gene Name GSTM4
Protein Type Enzyme
Biological Properties
General Function Involved in glutathione transferase activity
Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1-chloro-2,4-dinitrobenzene.
Pathways
  • Chemical carcinogenesis
  • Drug metabolism - cytochrome P450
  • Glutathione metabolism
  • Metabolism of xenobiotics by cytochrome P450
Reactions
RX + Glutathione → HX + R-S-glutathione details
RX + Glutathione → Halide + R-S-Glutathione details
Naphthalene epoxide + Glutathione → (1R)-Hydroxy-(2R)-glutathionyl-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1R)-Glutathionyl-(2R)-hydroxy-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1S)-Hydroxy-(2S)-glutathionyl-1,2-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-glutathionyl-8-hydroxy-7,8-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-hydroxy-6-glutathionyl-5,6-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-glutathionyl-6-hydroxy-5,6-dihydronaphthalene details
Bromobenzene-3,4-oxide + Glutathione → 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene details
Bromobenzene-2,3-oxide + Glutathione → 2,3-Dihydro-2-S-glutathionyl-3-hydroxy bromobenzene details
Benzo[a]pyrene-4,5-oxide + Glutathione → 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene details
Benzo[a]pyrene-7,8-diol + Glutathione → 7,8-Dihydro-7-hydroxy-8-S-glutathionyl-benzo[a]pyrene + Water details
2,2-Dichloroacetaldehyde + Glutathione → S-(2,2-Dichloro-1-hydroxy)ethyl glutathione details
1,1-Dichloroethylene epoxide + Glutathione → 2-(S-Glutathionyl)acetyl chloride + Hydrochloric acid details
Chloroacetyl chloride + Glutathione → S-(2-Chloroacetyl)glutathione + Hydrochloric acid details
2-(S-Glutathionyl)acetyl chloride + Glutathione → 2-(S-Glutathionyl)acetyl glutathione + Hydrochloric acid details
Trichloroethylene + Glutathione → S-(1,2-Dichlorovinyl)glutathione + Hydrochloric acid details
1,2-Dibromoethane + Glutathione + Hydrogen Ion → Glutathione episulfonium ion + Bromide details
2-Bromoacetaldehyde + Glutathione → S-(Formylmethyl)glutathione + Bromide details
Aldophosphamide + Glutathione → 4-Glutathionyl cyclophosphamide + Water details
2,3-Epoxyaflatoxin B1 + Glutathione → Aflatoxin B1exo-8,9-epoxide-GSH details
GO Classification
Biological Process
glutathione metabolic process
xenobiotic catabolic process
Cellular Component
endoplasmic reticulum membrane
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
glutathione transferase activity
Molecular Function
glutathione binding
glutathione transferase activity
Process
metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 1
Locus 1p13.3
SNPs GSTM4
Gene Sequence
>657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTAGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
Protein Properties
Number of Residues 218
Molecular Weight 25561.095
Theoretical pI 5.89
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutathione S-transferase Mu 4
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
GenBank ID Protein 306819
UniProtKB/Swiss-Prot ID Q03013
UniProtKB/Swiss-Prot Entry Name GSTM4_HUMAN
PDB IDs
GenBank Gene ID M96234
GeneCard ID GSTM4
GenAtlas ID GSTM4
HGNC ID HGNC:4636
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed:8373352 ]
  4. Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed:8471052 ]
  5. Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed:10587441 ]
  6. Comstock KE, Johnson KJ, Rifenbery D, Henner WD: Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4. J Biol Chem. 1993 Aug 15;268(23):16958-65. [PubMed:8349586 ]
  7. Taylor JB, Oliver J, Sherrington R, Pemble SE: Structure of human glutathione S-transferase class Mu genes. Biochem J. 1991 Mar 1;274 ( Pt 2):587-93. [PubMed:2006920 ]
  8. Comstock KE, Widersten M, Hao XY, Henner WD, Mannervik B: A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Arch Biochem Biophys. 1994 Jun;311(2):487-95. [PubMed:8203914 ]