| IED ID | IndEnz0002015998 |
| Enzyme Type ID | protease015998 |
| Protein Name |
Glutathione hydrolase proenzyme EC 3.4.19.13 Gamma-glutamyltranspeptidase proenzyme Gamma-GTP EC 2.3.2.2 Cleaved into: Glutathione hydrolase large chain; Glutathione hydrolase small chain |
| Gene Name | ggt |
| Organism | Bacillus subtilis subsp. natto |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. natto |
| Enzyme Sequence | MKRTWNVCLTALLSVLLVAGSVPFHAEAKKPPKSYDEYKQVDVGKDGMVATAHALASEIGADVLKKGGNAIDAAVAIQFALNVTEPMMSGIGGGGFMMVYDGKTKDTTIIDSRERAPAGATPDMFLDENGKAIPFSERVTKGTAVGVPGTLKGLEEALDKWGTRSMKLLITLTIKLAEKGFPIDSVLADAISDYQEKLSRTAAKDVFLPNGEPLKEGDTLIQKDLAKTFKLIRSKGTDAFYKGKFAKTLSDTVQDFGGSMTEKDLENYDITIDEPIWGDYQGYQIATTPPPSSGGIFLLQMLKILDDFNLSQYDVRSWEKYQLLAETMHLSYADRASYAGDPEFVNVPLKGLLHPDYIKERQQLINLDQVNKKPKAGDPWKYQEGSANYKQVEQPKDKVEGQTTHFTVADRWGNVVSYTTTIEQLFGTGIMVPDYGVILNNELTDFDAIPGGANEVQPNKRPLSSMTPTILFKDDKPVLTVGSPGGATIISSVLQTILYHIEYGMGLKAAVEEPRIYTTSMSSYRYEDGVPKDVLSKLNGMGHRFGTSPVDIGNVQSISIDHENGTFKGVVISGSNDAAIGINLKRK |
| Enzyme Length | 587 |
| Uniprot Accession Number | P63186 |
| Absorption | |
| Active Site | ACT_SITE 403; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P54422 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by glucose. {ECO:0000305|PubMed:9339568}. |
| Binding Site | BINDING 113; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P54422; BINDING 421; /note=Glutamate; /evidence=ECO:0000250; BINDING 423; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P54422; BINDING 442; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P54422; BINDING 445; /note=Glutamate; /evidence=ECO:0000250|UniProtKB:P54422 |
| 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:0000269|PubMed:1371053}; 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; 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; |
| DNA Binding | |
| EC Number | 3.4.19.13; 2.3.2.2 |
| 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. Uses glutamine as a gamma-glutamyl donor and acceptor for gamma-polyglutamic acid synthesis. Dipeptides are better gamma-glutamyl acceptors than free amino acids (PubMed:1371053). {ECO:0000269|PubMed:1371053}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:1371053}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5 for transfer of p-nitroanilide from gamma-glutamyl-p-nitroanilide (gamma-GpNA) to glycylglycine (gly-gly). {ECO:0000269|PubMed:1371053}; |
| Pathway | PATHWAY: Sulfur metabolism; glutathione metabolism. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (5); Chain (2); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Acyltransferase;Direct protein sequencing;Glutathione biosynthesis;Hydrolase;Protease;Secreted;Signal;Transferase;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1371053}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and small subunit. {ECO:0000269|PubMed:1371053}. |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,070 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468 |
| Cross Reference Brenda |