Detail Information for IndEnz0002018506
IED ID IndEnz0002018506
Enzyme Type ID protease018506
Protein Name Glutathione hydrolase proenzyme 2
EC 3.4.19.13
Gamma-glutamyltransferase 2
Gamma-glutamyltranspeptidase 2
EC 2.3.2.2

Cleaved into: Glutathione hydrolase 2 heavy chain; Glutathione hydrolase 2 light chain
Gene Name ggt2 SPAC56E4.06c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MSPTDTTPLLYSWDDQSRHQDPDWHKLRNYHGAWYRRISRRRFSQFIFAFGLMTLFVLVYSISSNLHTPTQFTGHKVRGRRGAVASEVPVCSDIGVSMLADGGNAVDAAIASTFCIGVVNFFSSGIGGGGFMLIKHPNETAQSLTFREIAPGNVSKHMFDKNPMLAQVGPLSIAIPGELAGLYEAWKSHGLLDWSKLLEPNVKLAREGFPVTRAMERVLKLPEMAHLLKDPIWQPILMPNGKVLRAGDKMFRPAYAKTLEIIANKGIEPFYRGELTNSMVKFIQDNGGIVTVEDFGNYSTVFADALHTSYRGHDVYTCTLPTSGPALIEGLNILDGYPLNTPSLAFPKRLHLEVEAMKWLSAGRTQFGDPDFLPLDHLDVVSKLLSKEFASQIRNNISLSKTYPWEHYNPSYDLPISHGTTHVSTVDSNNLAVSITSTVNLLFGSQLMDPVTGVVFNDQMDDFSIPGASNAFNLSPSPWNFIEPFKRPQSSSAPTILTDINGDFEMALGASGGSRIVTAVLDSIIKRIDMDYDIESMVASARPHHQLLPDILILESGFSKSVATRMKKYGHKVWRLKQHDTPLSQIQAVTRHHSEYYGMSDPRKYGQAAAY
Enzyme Length 611
Uniprot Accession Number O14194
Absorption
Active Site ACT_SITE 420; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 147; /note=Glutamate; /evidence=ECO:0000250; BINDING 438; /note=Glutamate; /evidence=ECO:0000250; BINDING 440; /note=Glutamate; /evidence=ECO:0000250; BINDING 459; /note=Glutamate; /evidence=ECO:0000250; BINDING 462; /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:0000305|PubMed:15920625}; 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: 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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15920625}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Sulfur metabolism; glutathione metabolism.
nucleotide Binding
Features Active site (1); Binding site (5); Chain (2); Glycosylation (4); Region (2); 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 and oxidative stress. {ECO:0000269|PubMed:16202243}.
Subcellular Location SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18337696; 20473289; 21712547; 22633491; 23697806; 30726745; 34250083;
Motif
Gene Encoded By
Mass 67,825
Kinetics
Metal Binding
Rhea ID RHEA:23904; RHEA:28807; RHEA:59468
Cross Reference Brenda 2.3.2.2;