Detail Information for IndEnz0002018509
IED ID IndEnz0002018509
Enzyme Type ID protease018509
Protein Name Glutathione hydrolase 5 proenzyme
EC 3.4.19.13
Gamma-glutamyl leukotrienase
GGL
Gamma-glutamyltransferase 5
GGT 5
EC 2.3.2.2
Gamma-glutamyltransferase-like activity 1
Gamma-glutamyltranspeptidase 5
Leukotriene-C4 hydrolase
EC 3.4.19.14

Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain
Gene Name Ggt5 Ggtla1
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAWGHRATVCLVLLGVGLGLVIVVLAAVLSPRQASCGPGAFTRAAVAADSKICSDIGRAILQQRGSPVDAAIAALVCTGVVNPQSMGLGGGVVFTIYNASTGKVEIINARETVPASYDQGLLNQCKNVLPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLREGFRVPFILSQFLNNSILRPHLSASTLRQLFFNGTETLRSQDPFPWPALANTLETVAKEGAEVLYTGRLGRMLVEDIAKQGSLLTVQDLAAFQPEVVEPLEMPLGNYTLYSPPPPAGGAILSFILNVLKGFNFSAETVARPGGEVNMYHHLVETLKFAVGQRWRLWDPSSHPGIQNISRDLLREDLAQRIRQQIDGRGDHHQLSHYNLTGVRGNRMGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGILLNNELLDLCWRHMPTSPITPPPVPGERPPSSMVPSILVNKGQGSKLVIGGAGGELIISAVAQTIMNKLWLGFDLTEAIASPILHVNSKGHVEYEPKFNQEVQKGLQDRGQIQSQSQRPVFLNAVQAVFQEGPCVYAASDLRKAGKASGY
Enzyme Length 573
Uniprot Accession Number Q9Z2A9
Absorption
Active Site ACT_SITE 389; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P19440
Activity Regulation ACTIVITY REGULATION: Inhibited by serine-borate. {ECO:0000250|UniProtKB:P36269}.
Binding Site BINDING 110; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 407; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 428; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000250|UniProtKB:P36269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905; Evidence={ECO:0000250|UniProtKB:P36269}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P36269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808; Evidence={ECO:0000250|UniProtKB:P36269}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P36269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469; Evidence={ECO:0000250|UniProtKB:P36269}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4; Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14; Evidence={ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373, ECO:0000269|PubMed:9774450};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564; Evidence={ECO:0000269|PubMed:12163373}; CATALYTIC ACTIVITY: Reaction=H2O + S-[(2E,6E,10E)-geranylgeranyl]-L-glutathione = L-glutamate + S-[(2E,6E,10E)-geranylgeranyl]-L-cysteinylglycine; Xref=Rhea:RHEA:65120, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:156326, ChEBI:CHEBI:156330; Evidence={ECO:0000250|UniProtKB:P36269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65121; Evidence={ECO:0000250|UniProtKB:P36269};
DNA Binding
EC Number 3.4.19.13; 2.3.2.2; 3.4.19.14
Enzyme Function FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione-S-conjugate (By similarity). Converts leukotriene C4 (LTC4), a glutathione-S-conjugate, to leukotriene D4 (LTD4) (PubMed:9774450, PubMed:11463821, PubMed:12163373). Does not cleaves gamma-glutamyl compounds such as gamma-glutamyl leucine. May also catalyze a transpeptidation reaction in addition to the hydrolysis reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Acts as a negative regulator of geranylgeranyl glutathione bioactivity by cleaving off its gamma-glutamyl group, playing a role in adaptive immune responses (By similarity). {ECO:0000250|UniProtKB:P36269, ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373, ECO:0000269|PubMed:9774450}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. {ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373, ECO:0000269|PubMed:9774450}.; PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P36269}.
nucleotide Binding
Features Active site (1); Alternative sequence (2); Binding site (3); Chain (2); Glycosylation (7); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1)
Keywords Acyltransferase;Alternative splicing;Glutathione biosynthesis;Glycoprotein;Hydrolase;Leukotriene biosynthesis;Membrane;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12163373}; Single-pass type II membrane protein {ECO:0000269|PubMed:12163373}.
Modified Residue
Post Translational Modification PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250|UniProtKB:P19440}.; PTM: Glycosylated. {ECO:0000269|PubMed:12163373}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10667344; 12466851; 14610273; 14681479; 16594735; 20096683; 21267068; 21677750; 27397680; 34088745;
Motif
Gene Encoded By
Mass 61,674
Kinetics
Metal Binding
Rhea ID RHEA:23904; RHEA:23905; RHEA:28807; RHEA:28808; RHEA:59468; RHEA:59469; RHEA:31563; RHEA:31564; RHEA:65120; RHEA:65121
Cross Reference Brenda 3.4.19.14;