Glutathione S-transferase Mu 4
Details
- Name
- Glutathione S-transferase Mu 4
- Synonyms
- 2.5.1.18
- GST class-mu 4
- GST-Mu2
- GSTM4-4
- Leukotriene C4 synthase GSTM4
- Gene Name
- GSTM4
- UniProtKB Entry
- Q03013Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0037082|Glutathione S-transferase Mu 4 MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
- Number of residues
- 218
- Molecular Weight
- 25561.095
- Theoretical pI
- 5.69
- GO Classification
- Functionsleukotriene-C4 synthase activityProcesseslong-chain fatty acid biosynthetic processComponentsintercellular bridge
- General Function
- Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:8203914, PubMed:8373352). Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 (PubMed:27791009). Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (PubMed:27791009)
- Specific Function
- enzyme binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019013|Glutathione S-transferase Mu 4 (GSTM4) ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
- Chromosome Location
- 1
- Locus
- 1p13.3
- External Identifiers
Resource Link UniProtKB ID Q03013 UniProtKB Entry Name GSTM4_HUMAN GenBank Protein ID 306819 GenBank Gene ID M96234 GeneCard ID GSTM4 GenAtlas ID GSTM4 HGNC ID HGNC:4636 PDB ID(s) 4GTU KEGG ID hsa:2948 NCBI Gene ID 2948 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Denson J, Xi Z, Wu Y, Yang W, Neale G, Zhang J: Screening for inter-individual splicing differences in human GSTM4 and the discovery of a single nucleotide substitution related to the tandem skipping of two exons. Gene. 2006 Sep 1;379:148-55. Epub 2006 May 25. [Article]
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- 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. [Article]
- 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. [Article]
- 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. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Glutathione S-transferase Mu 4 (Humans) protein primaryGlutathione S-transferases (Cytosolic) (Humans) protein - Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Glutathione approved, investigational, nutraceutical unknown target Details Glutathione sulfonic acid experimental unknown target Details S-octylglutathione experimental unknown target Details gamma-Glutamyl[S-(2-iodobenzyl)cysteinyl]glycine experimental unknown target Details S-Hexylglutathione experimental unknown target Details 1-Hydroxy-2-S-glutathionyl-3-para-nitrophenoxy-propane experimental unknown target Details Glutathione disulfide approved, experimental, investigational unknown target activator Details Deoxycholic acid approved unknown target inhibitor Details Amitriptyline approved unknown enzyme inhibitor Details Chlorambucil approved unknown enzyme substrate Details