Detail Information for IndEnz0002018503
IED ID IndEnz0002018503
Enzyme Type ID protease018503
Protein Name Glutathione hydrolase 1 proenzyme
EC 3.4.19.13
Gamma-glutamyltransferase 1
Gamma-glutamyltranspeptidase 1
GGT 1
EC 2.3.2.2
Leukotriene-C4 hydrolase
EC 3.4.19.14
CD antigen CD224

Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain
Gene Name GGT1 GGT
Organism Sus scrofa (Pig)
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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MKKRYLLLALAAVALVLLILGLCLWLPSNSKPHNHVYPRAAVAADALRCSEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEIINAREVAPRLASASMFNSSEQSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIELASQGFPVGKGLAAALERSQDAIKRHPALCEVFCRNGNVLREGDLVTMPRLAKTYETLAVEGAQAFYNGSLTAQIVKDIQEAGGIVTAEDLNNYRAELIEQPLRISLGDAQLYAPNAPLSGPVLALILNILKGYNFSRASVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVNVTEVVRNMSSEFFADQLRARISDTTTHPDSYYEPEFYTPDDAGTAHLSVVSDDGSAVSATSTINLYFGSKVRSRISGILFNDEMDDFSSPNITNQFGVRPSPANFITPGKQPLSSMCPVIIVGEDGQVRMVVGASGGTQITTSTALAIIHSLWFGYDVKRAVEEPRLHNQLLPNTTTLEKGIDQAVAAALKTRHHYIQDASTFIGVVQAIVRTPSGWAAASDSRKGGEPAGY
Enzyme Length 568
Uniprot Accession Number P20735
Absorption
Active Site ACT_SITE 380; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P19440
Activity Regulation ACTIVITY REGULATION: Activated by autocatalytic cleavage. {ECO:0000250|UniProtKB:P19440}.
Binding Site BINDING 106; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 419; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 422; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 473; /note=Glutamate; via amide nitrogen; /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:P19440}; 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:P19440};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808; Evidence={ECO:0000250|UniProtKB:P19440}; 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:P19440};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469; Evidence={ECO:0000250|UniProtKB:P19440}; 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:P07314};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564; Evidence={ECO:0000250|UniProtKB:P19440};
DNA Binding
EC Number 3.4.19.13; 2.3.2.2; 3.4.19.14
Enzyme Function FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates and other gamma-glutamyl compounds, such as leukotriene C4 (LTC4). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4. {ECO:0000250|UniProtKB:P19440}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Sulfur metabolism; glutathione metabolism.
nucleotide Binding
Features Active site (1); Binding site (4); Chain (2); Disulfide bond (2); Glycosylation (8); Region (2); Topological domain (2); Transmembrane (1)
Keywords Acyltransferase;Cell membrane;Disulfide bond;Glutathione biosynthesis;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
Modified Residue
Post Translational Modification PTM: N-glycosylated on both chains. {ECO:0000250|UniProtKB:P19440}.; PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000250|UniProtKB:P19440}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 61,316
Kinetics
Metal Binding
Rhea ID RHEA:23904; RHEA:28807; RHEA:28808; RHEA:59468; RHEA:59469; RHEA:31563; RHEA:31564
Cross Reference Brenda