| IED ID | IndEnz0002005476 |
| Enzyme Type ID | protease005476 |
| Protein Name |
Glutathione hydrolase proenzyme EC 3.4.19.13 CIK1 suppressor protein 2 Extracellular mutant protein 38 Gamma-glutamyltransferase EC 2.3.2.2 Gamma-glutamyltranspeptidase Gamma-GT Cleaved into: Glutathione hydrolase heavy chain; Glutathione hydrolase light chain |
| Gene Name | ECM38 CIS2 YLR299W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MLLCNRKVPKTLNTCFILHIFTLLTLGVLVSGMPSKMVSFASQETLQRINNLLRGSANRDVDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNLTINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKAPMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVGWQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGSVAPFYDPDHWIAKSMIDTVAKYNGIMNLQDVSSYDVHVTKPLSMKIRKGANFIPDNDMTVLTSSGSSSGAALLAALRIMDNFQNQEGGDYEKETTYHLLESMKWMASARSRLGDFEGEALPKHIEEVLDPEWALKAVKSIKRNSQDGNFKTLENWTLYDPAYDINNPHGTAHFSIVDSHGNAVSLTTTINLLFGSLVHDPKTGVIFNNEMDDFAQFNKSNSFELAPSIYNFPEPGKRPLSSTAPTIVLSELGIPDLVVGASGGSRITTSVLQTIVRTYWYNMPILETIAYPRIHHQLLPDRIELESFPMIGKAVLSTLKEMGYTMKEVFPKSVVNAIRNVRGEWHAVSDYWRKRGISSVY |
| Enzyme Length | 660 |
| Uniprot Accession Number | Q05902 |
| Absorption | |
| Active Site | ACT_SITE 470; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activity is decreased by glutathione and ammonium ion. {ECO:0000269|PubMed:1674526}. |
| Binding Site | BINDING 177; /note=Glutamate; /evidence=ECO:0000250; BINDING 488; /note=Glutamate; /evidence=ECO:0000250; BINDING 490; /note=Glutamate; /evidence=ECO:0000250; BINDING 509; /note=Glutamate; /evidence=ECO:0000250; BINDING 512; /note=Glutamate; /evidence=ECO:0000250 |
| 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:6102906, ECO:0000269|PubMed:6143552}; 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:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552}; 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:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552}; |
| DNA Binding | |
| EC Number | 3.4.19.13; 2.3.2.2 |
| Enzyme Function | FUNCTION: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation. {ECO:0000269|PubMed:11672438}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Sulfur metabolism; glutathione metabolism. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (5); Chain (2); Compositional bias (1); Glycosylation (6); Natural variant (2); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix;Vacuole |
| Interact With | |
| Induction | INDUCTION: Induced upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor. {ECO:0000269|PubMed:12529169, ECO:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552, ECO:0000269|PubMed:9202464}. |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552, ECO:0000269|PubMed:6143574}; Single-pass type II membrane protein {ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552, ECO:0000269|PubMed:6143574}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12406228; 12620619; 16857395; 18557947; 19345220; 19897216; 26227410; 9990050; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,180 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468 |
| Cross Reference Brenda | 3.4.19.13; |