3.4.19.13: glutathione gamma-glutamate hydrolase
This is an abbreviated version!
For detailed information about glutathione gamma-glutamate hydrolase, go to the full flat file.
Word Map on EC 3.4.19.13
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3.4.19.13
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medicine
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hydroxyacyl
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halide
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alpha-globin
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formyl
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dihalomethanes
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methanes
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phosphoglycolate
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monoxide
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decomposes
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diverted
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halogenated
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formaldehyde
- 3.4.19.13
- medicine
-
hydroxyacyl
- halide
-
alpha-globin
-
formyl
-
dihalomethanes
- methanes
- phosphoglycolate
-
monoxide
-
decomposes
-
diverted
-
halogenated
- formaldehyde
Reaction
Synonyms
At4g29210, BaGGT42, BaGGT469, BlGGT13, BsGGT168, gamma-glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gamma-GT, GGT, GGT-1, GGT1, GGT3, GGT4, GGT5, hp1118, More
ECTree
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General Information
General Information on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase
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evolution
metabolism
physiological function
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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
evolution
Halalkalibacterium halodurans
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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
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
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
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
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
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
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
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
-
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
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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)
-
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
-
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
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evolution
Bacillus amyloliquefaciens SMB469
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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)
-
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
-
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
-
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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in the presence of 1alpha,25-dihydroxyvitamin D3, gamma-glutamyl transpeptidase activity is significantly increased in LLC-PK1 cells, with an increase in enzymic activity also found in the cell medium. While the stimulatory effect of 1-hydroxyvitamin D3 is similar to that of 1alpha,25-dihydroxyvitamin D3, vitamin D3 and 25-hydroxyvitamin D3 have no effect on activity. The increase in activity is due to prolonged turnover
metabolism
capacity of the enzyme to cleave GSH conjugates of both aromatic and aliphatic diisocyanates, suggesting a potential role in their metabolism
metabolism
the enzyme plays a role in asthma, reperfusion injury, and cancer
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construction of stably transfected NIH/3T3 mouse fibroblasts that express the enzyme in its proper orientation on the outer surface of the cell. NIH/3T3 fibroblasts require cysteine for growth and are unable to use extracellular glutathione as a source of cysteine. NIH/3T3 fibroblasts expressing the enzyme are able to grow in cysteine-free medium supplemented with glutathione. Cysteine derived from the cleavage of extracellular glutathione can be used to maintain intracellular levels of glutathione, and cells are able to replenish intracellular glutathione when incubated in cysteine-free medium containing glutathione
physiological function
enzyme calatyzes the first step in vacuolar degradation of glutathione conjugates. In Arabidopsis thaliana, degradation of glutathione S-conjugates strictly occurs by the ordered removal of Glu first and Gly second. Hydrolysis of glutathione S-bimane is blocked in enzyme null mutants
physiological function
enzyme catalyzes the obligate initial step in glutathione conjugate metabolism. Enzyme disruption plants grown on soil under normal conditions until they set seed do not display visible differences compared with wild-type plants
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
physiological function
enzyme is important in utilizing glutathione as the sole sulfur source in Bacillus subtilis. With glutathione as a sulfur source, the growth of enzyme deletion mutants is dramatically reduced compared to that of the wild type. Findings suggest that extracellular enzyme catalyzes the hydrolysis of the gamma-glutamyl linkage of exogenous glutathione and then cysteinylglycine is utilized as a sulfur source in the cell
physiological function
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extracellular cleavage of glutathione by the enzyme leads to reactive oxygen species production, depending on the generation and enhanced reactivity of cysteinylglycine. This production of reactive oxygen species induces the NF-kappaB-binding and transactivation activities. The induction mimicks the one observed by H2O2 and is inhibited by catalase
physiological function
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inhibition of gamma-glutamyltranspeptidase by acivicin causes extensive loss of intracellular glutathione from ARL-16T2 cells, which show a high level of gamma-glutamyl transpeptidase, but produces no effect on glutathione levels in ARL-15C1 cells, which show a low level of gamma-glutamyl transpeptidase. Acivicin treatment causes a transient increase in intracellular glutathione in the ARL-16T2 but not the ARL-15C1 cells, further suggesting that the enzyme catalyzes intracellular glutathione recycling to supply cysteine for cellular functions in the tumorigenic ARL-16T2 cell line
physiological function
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mutagenic effect of glutathione follows a model of an indirect mechanism, i.e. cleavage of glutathione by gamma-glutamyltranspeptidase, followed by facile autooxidation of the resulting cysteinylglycine, with the production of free radicals which lead to the (pen)ultimate mutagen, H2O2
physiological function
one of the principle physiological functions of the enzyme is to enable Helicobacter pylori cells to utilize extracellular glutamine and glutathione as a source of glutamate. Helicobacter pylori cells are unable to take up extracellular glutamine and glutathione directly. Instead, these substances are hydrolysed to glutamate by the action of the enzyme outside the cells
physiological function
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the relatively small increase of glutathione amount in the presence of oxidative and electrophilic agents such as hydrogen peroxide or N-ethylmaleimide compared to other thiol reactive agents is not due to increased gamma-glutamyltranspeptidase-mediated degradation of glutathione
physiological function
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gene deletion mutants overproduce sclerotial initials that are arrested in further development or eventually produce sclerotia with aberrant rind layers. During incubation for carpogenic germination, these sclerotia decay and fail to produce apothecia. Total glutathione accumulation is approximately 10fold higher and H2O2 hyperaccumulates in deletion mutant sclerotia compared with the wild type. Production of compound appressoria is also negatively affected. On host plants, these mutants exhibit a defect in infection efficiency and a delay in initial symptom development unless the host tissue is wounded prior to inoculation
physiological function
lysate from a gamma-glutamyl transpeptidase Ggt mutant strain shows a decrease of the capacity to inhibit Jurkat T cell proliferation. Incubation of Jurkat T cells with recombinantly expressed Ggt results in an impaired proliferation, and cell death is involved. A similar but more pronounced inhibitory effect is also seen on primary murine CD4+ T cells, CD8+ T cells, and CD19+ B cells. Supplementation with glutamine restores normal proliferation of the cells, whereas supplementation with reduced glutathione strengthens the enzyme-mediated inhibition of proliferation. Ggt treatment abolishes secretion of IL-4 and IL-17 by CD4+ T cells, without affecting secretion of IFN-gamma. Helicobacter suis outer membrane vesicles are a possible delivery route of Ggt to lymphocytes residing in the deeper mucosal layers
physiological function
gamma-glutamyl transpeptidase 1 is essential in cysteine homeostasis
physiological function
gamma-glutamyl transpeptidase plays a key role in the balance of glutathione by breaking down extracellular glutathione
physiological function
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it is proposed that 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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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, EC 2.3.2.2) or water (hydrolysis). 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-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 (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
-
enzyme is important in utilizing glutathione as the sole sulfur source in Bacillus subtilis. With glutathione as a sulfur source, the growth of enzyme deletion mutants is dramatically reduced compared to that of the wild type. Findings suggest that extracellular enzyme catalyzes the hydrolysis of the gamma-glutamyl linkage of exogenous glutathione and then cysteinylglycine is utilized as a sulfur source in the cell
-
physiological function
-
it is proposed that 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
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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
-
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
Bacillus amyloliquefaciens SMB469
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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
-
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
-