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Information on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q05902

for references in articles please use BRENDA:EC3.4.19.13
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.13 glutathione gamma-glutamate hydrolase
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Saccharomyces cerevisiae
UNIPROT: Q05902 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hp1118, more
PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
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enzyme additionally catalyzes the reaction of EC 2.3.2.2, gamma-glutamyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic analysis of gamma-glutamyltranspeptidase proteins from different organisms divides the gamma-glutamyltranspeptidases into various clades and offers several interesting insights into the evolution and relatedness of these gamma-glutamyltranspeptidases. The present study focuses on the residues that are highly specific to each gamma-glutamyltranspeptidase subfamily and underlines their importance in imparting unique functional properties to the gamma-glutamyltranspeptidase proteins of each clade. The present study highlights the clade specific variation in the GXXGG motif, where SP (XX) of bacterial gamma-glutamyltranspeptidases is substituted by VM, CA, AS in extremophilic bacteria, archaea, and eukaryotes respectively, which could explain the differences in rates of enzyme reaction in gamma-glutamyltranspeptidases of these clades as this motif is known to be involved in gamma-glutamyltranspeptidase-substrate complex intermediate formation and the rate of final product release. Many sites predicted to be contributing to type 2 functional divergence are quite often found lining the substrate binding cavity and are close to the highly conserved known functional residues. This implies that they may be affecting the biochemical environment of the binding cavity and influencing the catalytic residues, thereby contributing to the functional differences among gamma-glutamyltranspeptidase-like proteins of various clades
physiological function
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enzyme gamma-glutamyl transpeptidase and a L-Cys-Gly dipeptidase catalyse the complete hydrolysis of glutathione stored in the central vacuole of the yeast cell, prior to release of its constitutive amino acids L-glutamate, L-cysteine and glycine into the cytoplasm
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mehdi, K.; Thierie, J.; Penninckx, M.J.
gamma-Glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione
Biochem. J.
359
631-637
2001
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Verma, V.V.; Gupta, R.; Goel, M.
Phylogenetic and evolutionary analysis of functional divergence among Gamma glutamyl transpeptidase (GGT) subfamilies
Biol. Direct
10
49
2015
Bacillus anthracis (Q51693), Bacillus subtilis, Bacillus subtilis BEST7613, Escherichia coli (P18956), Escherichia coli K12 (P18956), Halalkalibacterium halodurans, Helicobacter pylori (Q9F5N9), Homo sapiens (P19440), Saccharomyces cerevisiae (Q05902), Saccharomyces cerevisiae ATCC 204508 (Q05902), Thermoplasma acidophilum (Q9HJH4), Thermoplasma acidophilum ATCC 25905 (Q9HJH4)
Manually annotated by BRENDA team