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evolution
Q62WE3
Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) belongs to N-terminal nucleophile hydrolase superfamily in which all inclusive members are synthetized as single-chain precursors, and then self-processed to form mature enzymes
evolution
gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
evolution
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
evolution
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
evolution
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
evolution
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the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
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evolution
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the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
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evolution
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the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
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evolution
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the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
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evolution
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the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
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evolution
-
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
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evolution
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gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
-
evolution
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Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) belongs to N-terminal nucleophile hydrolase superfamily in which all inclusive members are synthetized as single-chain precursors, and then self-processed to form mature enzymes
-
evolution
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gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
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malfunction
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deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans
malfunction
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
malfunction
human GGT protein without the N-terminal anchor domain is expressed as a soluble enzyme and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain
malfunction
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gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
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malfunction
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deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans
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malfunction
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gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
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malfunction
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gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
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malfunction
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gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
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malfunction
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gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
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physiological function
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cells overexpressing gamma-GT exhibit a low susceptibility to arsenic trioxide-induced apoptosis, associated with low reactive oxygen species induction and increased catalase activity
physiological function
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gamma glutamyltranspeptidase is a key enzyme involved in mediating cisplatin nephrotoxicity, which potentially acts to cleave cisplatin-GSH conjugates to a toxic metabolite
physiological function
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gamma glutamyltranspeptidase is a key enzyme involved in mediating cisplatin nephrotoxicity, which potentially acts to cleave cisplatin-GSH conjugates to a toxic metabolite
physiological function
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GGT is essential to the recovery of apoplasic glutathione provided exogenously or extruded by oxidative treatment. GGT activity helps to salvage extracellular glutathione and may contribute to redox control of the extracellular environment
physiological function
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the enzyme induces cell cycle arrest at the G1-S phase transition in AGS cells
physiological function
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the enzyme partakes in glutathione uptake by Helicobacter pylori
physiological function
enzyme gamma-glutamyl transpeptidase 1 (GGT1) cleaves extracellular gamma-glutamyl compounds and contributes to the pathology of asthma, reperfusion injury and cancer
physiological function
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gamma-glutamyl dipeptides (gamma-GPs) are responsible for the attractive Kokumi flavor of Parmesan cheese. They are synthesized by gamma-glutamyltransferase (GGT) from milk, most efficiently after 24 months of ripening (PC-24). GGT catalyzes the transfer of the gamma-glutamyl moiety of L-glutamine onto various acceptor amino acids released upon casein proteolysis. Microflora analysis in Parmesan cheese and GGT activity of Lactobacillus strains, overview. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the hydrolysis (EC 3.4.19.13) and transpeptidation of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione metabolism
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of gamma-glutamyl moiety from a donor molecule to an acceptor molecule by cleavage and subsequent formation of a gamma-amide bond. The acceptor can be an amino acid, a peptide or a water molecule. Under physiological conditions, GGT enzyme expression from wild strains of bacteria, such as Escherichia coli and Bacillus, is tightly regulated because of the involvement of the enzyme in various stress and starvation conditions
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
physiological function
gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme involved in glutathione metabolism and maintenance of redox homeostasis. High expression of GGT on tumor cells is associated with an increase of cell proliferation and resistance against chemotherapy. GGT catalyzes the cleavage of gamma-glutamyl compounds and the transfer of the gamma-glutamyl group to an acceptor substrate by a ping-pong mechanism. GSH, the most common physiological substrate of GGT, acts as the gamma-glutamyl donor in the initial reaction of hydrolysis (EC 3.4.19.13)
physiological function
gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme involved in glutathione metabolism and maintenance of redox homeostasis. High expression of GGT on tumor cells is associated with an increase of cell proliferation and resistance against chemotherapy. GGT catalyzes the cleavage of gamma-glutamyl compounds and the transfer of the gamma-glutamyl group to an acceptor substrate by a ping-pong mechanism. GSH, the most common physiological substrate of GGT, acts as the gamma-glutamyl donor in the initial reaction of hydrolysis (EC 3.4.19.13)
physiological function
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gamma-glutamyl transpeptidase (GGT) is a widely distributed enzyme from bacteria to plants and mammals that catalyzes the cleavage of the gamma-glutamyl linkage of gamma-glutamyl compounds, such as glutathione and transfer of the gamma-glutamyl residue either to amino acid or peptides (transpeptidation) or water (hydrolysis, EC 3.4.19.13). GGT catalyzes the release of the glutamic acid moiety from (S,S)-gamma-glutamyl-(cis-S-1-propenyl)-thioglycine, a flavor precursor found in Toona sinensis. Toona sinensis shoots and young leaves with unique aroma are consumed as a delicious seasonal vegetable in China. GGT may play an important role in the formation of volatile sulfur-containing compounds, including propene thiol which determines the characteristic aroma of Toona sinensis vegetables
physiological function
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
physiological function
gamma-glutamyltransferases (GGTs) are widespread, conserved enzymes that catalyze the transfer of the gamma-glutamyl moiety from a donor substrate to water (hydrolysis, EC 3.4.19.13) or to an acceptor amino acid (transpeptidation)through the formation of a gamma-glutamyl enzyme intermediate
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase is an organosulfur compound (GGT) and catalyzes the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water
physiological function
gamma-glutamyltranspeptidases (GGTs) catalyze the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water
physiological function
grapevine appears to contain only a single GGT gene, possessing all the key conserved residues needed for GGT activity. VvGGT3 has a proposed role in the formation of precursors of key varietal aromas in wine. These compounds are considered to be derived from the lipoxygenase/hydroperoxide lyase mediated breakdown of linolenic and linoleic C18 fatty acids to produce C6 hexanal and then its derivatives
physiological function
purified recombinant wild-type and inactive mutant enzymes both induce similar levels of osteoclastogenesis in Mus musculus mixed osteoblast and bone marrow-derived macrophage cell culture. Bacillus subtilis GGT possesses virulent bone-resorbing activity and its activity is probably independent of its enzymatic activity. The GGT heavy subunit shows strong activity of osteoclastogenesis while the light subunit fails to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. Since the GGT light subunit contains the catalytic pocket, enzymatic activity may not be required for this virulence activity. In addition, recombinant Bacillus subtilis GGT stimulates mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2) in mouse cells, while an osteoprotegerin inhibits the osteoclast formation induced by the GGT heavy subunit. Bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction
physiological function
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the function of this enzyme is not to degrade, but to produce, gamma-glutamyl compounds, which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures
physiological function
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the gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme that plays an essential central role in glutathione (GSH) homeostasis. Elevated serum GGT levels are a general marker of diseases affecting the liver
physiological function
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gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
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physiological function
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gamma-glutamyltransferases (GGTs) are widespread, conserved enzymes that catalyze the transfer of the gamma-glutamyl moiety from a donor substrate to water (hydrolysis, EC 3.4.19.13) or to an acceptor amino acid (transpeptidation)through the formation of a gamma-glutamyl enzyme intermediate
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physiological function
-
purified recombinant wild-type and inactive mutant enzymes both induce similar levels of osteoclastogenesis in Mus musculus mixed osteoblast and bone marrow-derived macrophage cell culture. Bacillus subtilis GGT possesses virulent bone-resorbing activity and its activity is probably independent of its enzymatic activity. The GGT heavy subunit shows strong activity of osteoclastogenesis while the light subunit fails to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. Since the GGT light subunit contains the catalytic pocket, enzymatic activity may not be required for this virulence activity. In addition, recombinant Bacillus subtilis GGT stimulates mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2) in mouse cells, while an osteoprotegerin inhibits the osteoclast formation induced by the GGT heavy subunit. Bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction
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physiological function
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gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
the enzyme induces cell cycle arrest at the G1-S phase transition in AGS cells
-
physiological function
-
the function of this enzyme is not to degrade, but to produce, gamma-glutamyl compounds, which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of gamma-glutamyl moiety from a donor molecule to an acceptor molecule by cleavage and subsequent formation of a gamma-amide bond. The acceptor can be an amino acid, a peptide or a water molecule. Under physiological conditions, GGT enzyme expression from wild strains of bacteria, such as Escherichia coli and Bacillus, is tightly regulated because of the involvement of the enzyme in various stress and starvation conditions
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
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the enzyme partakes in glutathione uptake by Helicobacter pylori
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additional information
active site structures of human GGT, overview
additional information
catalytic mechanism of human GGT, catalytic Thr381 within the active site, acts as a nucleophile and attacks the delta-carbon of the glutamate moiety, leading to the formation of a tetrahedral intermediate (gamma-glutamyl enzyme complex), stabilized by two conserved glycines (Gly473 and Gly474 in hGGT), overview
additional information
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catalytic mechanism of human GGT, catalytic Thr381 within the active site, acts as a nucleophile and attacks the delta-carbon of the glutamate moiety, leading to the formation of a tetrahedral intermediate (gamma-glutamyl enzyme complex), stabilized by two conserved glycines (Gly473 and Gly474 in hGGT), overview
additional information
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
additional information
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comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
additional information
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enzyme AngammaGT has little hydrolase activity (cf. EC 3.4.19.13)
additional information
functional role of the conserved glycine residues, Gly481 and Gly482, in gamma-glutamyltranspeptidase reaction. Several residues, including Arg109, Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482, are proposed to be involved in the binding of the substrate
additional information
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functional role of the conserved glycine residues, Gly481 and Gly482, in gamma-glutamyltranspeptidase reaction. Several residues, including Arg109, Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482, are proposed to be involved in the binding of the substrate
additional information
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
additional information
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GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
additional information
hGGT1 catalytic reaction mechanism, activation of the catalytic nucleophile that initiates the hGGT1 reaction, overview
additional information
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hGGT1 catalytic reaction mechanism, activation of the catalytic nucleophile that initiates the hGGT1 reaction, overview
additional information
Q62WE3
the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
additional information
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the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
additional information
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enzyme AngammaGT has little hydrolase activity (cf. EC 3.4.19.13)
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additional information
-
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
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additional information
-
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
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additional information
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the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
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additional information
-
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
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