IED ID | IndEnz0018000798 |
Enzyme Type ID | peroxidase000798 |
Protein Name |
Microsomal glutathione S-transferase 3 Microsomal GST-3 Glutathione peroxidase MGST3 EC 1.11.1.- LTC4 synthase MGST3 EC 4.4.1.20 Microsomal glutathione S-transferase III Microsomal GST-III |
Gene Name | MGST3 |
Organism | Homo sapiens (Human) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSIALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH |
Enzyme Length | 152 |
Uniprot Accession Number | O14880 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by MK-886 and leukotriene C4. {ECO:0000250|UniProtKB:D4ADS4}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:9278457}; CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000269|PubMed:9278457}; |
DNA Binding | |
EC Number | 1.11.1.-; 4.4.1.20 |
Enzyme Function | FUNCTION: Catalyzes oxydation of hydroxy-fatty acids (PubMed:9278457). Also catalyzes the conjugation of a reduced glutathione to leukotriene A4 in vitro (PubMed:9278457). May participate in the lipid metabolism (PubMed:9278457). {ECO:0000269|PubMed:9278457, ECO:0000303|PubMed:9278457}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Lipidation (2); Mutagenesis (2); Natural variant (2); Transmembrane (3) |
Keywords | Endoplasmic reticulum;Lipid metabolism;Lipoprotein;Lyase;Membrane;Microsome;Oxidoreductase;Palmitate;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
Interact With | Q9NRZ5; Q6RW13-2; P05090; Q9BQE5; P29972; Q96PS8; Q92482; Q15041; Q8N6S5; O15155; O95393; Q96F05; Q06432; P24863; O14735; P58418; Q96DZ9-2; Q96BA8; Q9BQA9; Q9UKR5; Q96IV6; Q9BWH2; Q9H0Q3; Q8WWP7; Q96F15; Q8TDT2; Q8TED1; Q14416; P30519; P11215; Q68G75; Q9UBY5; Q7Z4F1; Itself; P30301; Q6IN84; Q9H2K0; Q99519; Q9NZG7; Q16617; Q8N912; Q8IXM6; P42857; O75459; P26678; P60201-2; Q04941; Q5VZY2; Q59EV6; O00767; Q9NY72; O75396; P43003; P22732; P78382; Q9NUM3; P30825; Q9NRQ5; Q5SQN1; Q6UX34; Q13277; O15400; Q9UNK0; Q8N2H4; Q00059; P02786; Q6UX40; Q9BVC6; A0PK00; Q9NV12; Q8NBD8; Q9H2L4; Q8N661; Q9Y320; O95859; O60636; Q86UF1; Q5BVD1; Q9Y5Z9; Q53HI1; Q15836; O75379; O95070; O95159 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane {ECO:0000269|PubMed:9278457}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11904223; 16169070; 19064610; 19343046; 19536175; 20360068; 20379614; 25280473; 25416956; 26496610; 26638075; 3372534; 8703034; 8812420; |
Motif | |
Gene Encoded By | |
Mass | 16,516 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:9278457}; |
Metal Binding | |
Rhea ID | RHEA:48620; RHEA:17617 |
Cross Reference Brenda |