Detail Information for IndEnz0002018500
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