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Information on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase and Organism(s) Bacillus subtilis and UniProt Accession P54422

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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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Bacillus subtilis
UNIPROT: P54422 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hp1118, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
see also EC 2.3.2.2
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione + H2O
L-cysteinylglycine + L-glutamate
show the reaction diagram
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with acivicin, to 1.8 A resolution. Acivicin is bound covalently through its C3 atom with sp2 hybridization to Thr403 Ogamma, the catalytic nucleophile of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Minami, H.; Suzuki, H.; Kumagai, H.
gamma-Glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis
J. Bacteriol.
186
1213-1214
2004
Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
Manually annotated by BRENDA team
Ida, T.; Suzuki, H.; Fukuyama, K.; Hiratake, J.; Wada, K.
Structure of Bacillus subtilis ?-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue.
Acta Crystallogr. Sect. D
70
607-614
2014
Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
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
Lee, J.; Lee, J.; Nam, G.; Son, B.; Jang, M.; Lee, S.; Hurh, B.; Kim, T.
Heterologous expression and enzymatic characterization of gamma-glutamyltranspeptidase from Bacillus amyloliquefaciens
J. Microbiol.
55
147-152
2017
Bacillus amyloliquefaciens (A0A1S5V3K5), Bacillus amyloliquefaciens SMB469 (A0A1S5V3K5), Bacillus licheniformis (Q65KZ6), Bacillus licheniformis ATCC 14580 (Q65KZ6), Bacillus licheniformis DSM 13 (Q65KZ6), Bacillus licheniformis Gibson 46 (Q65KZ6), Bacillus licheniformis JCM 2505 (Q65KZ6), Bacillus licheniformis NBRC 12200 (Q65KZ6), Bacillus licheniformis NCIMB 9375 (Q65KZ6), Bacillus licheniformis NRRL NRS-1264 (Q65KZ6), Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422), Bacillus velezensis (A7Z5E0), Bacillus velezensis BGSC 10A6 (A7Z5E0), Bacillus velezensis DSM 23117 (A7Z5E0), Bacillus velezensis FZB42 (A7Z5E0)
Manually annotated by BRENDA team