| IED ID | IndEnz0002018500 |
| Enzyme Type ID | protease018500 |
| Protein Name |
Glutathione hydrolase proenzyme EC 3.4.19.13 Gamma-glutamyltransferase ARB_02921 EC 2.3.2.2 Gamma-glutamyltranspeptidase Gamma-GT Leukotriene-C4 hydrolase EC 3.4.19.14 Cleaved into: Glutathione hydrolase heavy chain; Glutathione hydrolase light chain |
| Gene Name | ARB_02921 |
| Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Enzyme Sequence | MAPAAMNLLCTVLYLLSSFAQVSDAAPWLFSRSIPASYHDGRLGAVASENSMCSEYGADMLKIGGNAADAVCIYRLSLFFAFLPYPALQEDRAMYHSGIGGGGFMLIRAPNGTYEFIDFRETAPAAAFQDMFKNNTSGSTSGGLASGVPGEVRGLEYLHKNYGKLPWKTVMEPAIRTARDGFRVTEDLSRIMLHSTKNGNFLAENAAWALDFAPQGTLLKVGDIITRRRYGDTLDKIAKYGADAFYTGPMAQAMVNALRAANGTMTLEDLKNYTVVSRPTAQIEYRGMTVTSTTAPSSGVVLLSILKLLNGYKNFFRMDPGPLSTHRMDEAIRFGYGQRTELGDPLFFSNLTDYQKKMISDEAANKNRMNISDEYTQDIAVYDPKGLESLNTPGTSHISTADRSGMAVSLTTTINLYFGSRVIVPETGIIMNNEMDDFSVPGRSNSFGYKPSPSNFIRPGKRPLSSICPTIITRPDGSLYFVSGAAGGSQIITGTLQSVINVMDRKMNVRQALKAPRLHDQLVPNVALMEDEFDKKTVDFMISRKHNVTREKSGSTVESIMRLKNGVFEASGEPRLANSGGVVV |
| Enzyme Length | 584 |
| Uniprot Accession Number | D4B387 |
| Absorption | |
| Active Site | ACT_SITE 395; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P19440 |
| Activity Regulation | |
| Binding Site | BINDING 120; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 413; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P19440; BINDING 434; /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: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}; 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}; 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: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. The metabolism of glutathione 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. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. {ECO:0000250|UniProtKB:P19440}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P19440}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (3); Chain (2); Glycosylation (7); Region (1); Signal peptide (1) |
| Keywords | Acyltransferase;Glutathione biosynthesis;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. |
| Modified Residue | |
| Post Translational Modification | 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 | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 63,768 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468; RHEA:31563 |
| Cross Reference Brenda |