| IED ID | IndEnz0002018510 |
| Enzyme Type ID | protease018510 |
| Protein Name |
Glutathione hydrolase 5 proenzyme EC 3.4.19.13 Gamma-glutamyl leukotrienase GGL Gamma-glutamyl transpeptidase-related enzyme GGT-rel 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 | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAWGHRTTVCLVLLGVSLGLAIIVLAVVLPHHQASCRPDAFTRAAVAADSKICSDIGRVILQQQGSPVDAAIAALICTGVVNPQSMGLGGGVVFTIYNASTGKVEVINARETVPASHDQRLLDQCTNALPLCTGAQWIGVPGELRGYAEAHRRYGRLPWAQLFQPTIALLREGFRVPPILSQFLNTSFLQPCLNSSTLRQLFFNGTETLRSQDPLPWPALANTLETVAKEGAEVLYTGKLGQTLVEDIAWQGSQLTVQDLAAFRPKVVEPLEMALGNYTLYSPPPPAGGAILSFILNVLKGFNFSAETVAGPEGKVNMYHHLVEALKFAVGQRWRLWDPYSHPGIQNISQDLLRETLAQHIRQQIDGRGDHQLSHYNLSGVRGNSMGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGILLNNELLDLCWRHKPGSTVTPPPVPGEQPPSSMVPSILINEVQGSKLVIGGAGGELIISAVTQAIVNKLWLGFSLTDAIAAPILHVNSKGHVEYEPKFNQEVRKGLQDRGQSQSQSQRPVFLNSVQAVFQEGPCVYAASDLRKAGKASGY |
| Enzyme Length | 572 |
| Uniprot Accession Number | Q9QWE9 |
| Absorption | |
| Active Site | ACT_SITE 388; /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 406; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 427; /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:0000250|UniProtKB:P36269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564; Evidence={ECO:0000250|UniProtKB:P36269}; 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. Converts leukotriene C4 (LTC4), a glutathione-S-conjugate, to leukotriene D4 (LTD4). Does not cleave 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. {ECO:0000250|UniProtKB:P36269}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. {ECO:0000250|UniProtKB:Q9Z2A9}.; PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P36269}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (3); Chain (2); Glycosylation (8); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;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:0000250|UniProtKB:Q9Z2A9}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Z2A9}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250|UniProtKB:P19440}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9Z2A9}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,569 |
| 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 |