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Enzyme Nomenclature
Information on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase
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EC Tree
3.4.19.13 glutathione gamma-glutamate hydrolaseSpecify your search results
Word Map
- 3.4.19.13
- medicine
-
hydroxyacyl
- halide
-
alpha-globin
-
formyl
-
dihalomethanes
- methanes
- phosphoglycolate
-
monoxide
-
decomposes
-
diverted
-
halogenated
- formaldehyde
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gamma-glutamyl transpeptidase
GGT
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a glutathione-S-conjugate + H2O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
(2)
-
-
-
glutathione + H2O = L-cysteinylglycine + L-glutamate
(1)
-
-
-
glutathione + H2O = L-cysteinylglycine + L-glutamate
ping-pong kinetics mechanism, in which an acyl enzyme intermediate is formed
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PATHWAY SOURCE
PATHWAYS
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S,S)-gamma-glutamyl-(cis-S-1-propenyl)-thioglycine + H2O
(S)-(cis-S-1-propenyl)thioglycine + L-glutamate
-
-
-
-
?
glutathione S-bimane + H2O
L-cysteinylglycyl S-bimane + L-glutamate
-
-
-
?
glutathione-S-monobromobimane conjugate + H2O
L-cysteinylglycine-S-monobrombimane conjugate + L-glutamate
-
-
-
?
reduced glutathione + H2O
L-cysteinylglycine + L-glutamate
-
-
-
?
S-(2-(4-chlorophenoxy)-2-methylpropanoyl)glutathione + H2O
S-(2-(4-chlorophenoxy)-2-methylpropanoyl)-L-cysteinylglycine + L-glutamate
-
i.e. clofibril-S-acylglutathione
the first step in the degradation of clofibril S-acylglutathione. complete degradation with formation of clofibryl-S-acyl-N-acetylcysteine and its disulfide, with no detection of clofibryl-S-acyl-cysteinylglycine thioester
-
?
S-(4-nitro-benzyl)glutathione + H2O
S-(4-nitro-benzyl)-L-cysteinylglycine + L-glutamate
-
-
-
?
S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)glutathione + H2O
S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)-L-cysteinylglycine + L-glutamate
-
-
the GGT-dependent metabolism of S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)glutathione in the V79 GGT cell line is associated with a considerable increase of cytotoxicity. The cytotoxic effect is dose- and time-dependent, with 100% cellular death at 200 mM S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)glutathione after 24 h incubation in V79 GGT cells
-
?
S-linked bis-GSH conjugate of 1,6-hexamethylene diisocyanate + H2O
bis(Cys-Gly)-1,6-hexamethylene diisocyanate + 2 L-glutamate
-
-
-
?
S-linked bis-GSH conjugate of 4,4'-methylene diphenyl diisocyanate + H2O
bis(Cys-Gly)-4,4'-methylene diphenyl diisocyanate + 2 L-glutamate
-
-
-
?
S-linked mono-GSH conjugate of 1,6-hexamethylene diisocyanate + H2O
(Cys-Gly)-1,6-hexamethylene diisocyanate + L-glutamate
-
-
-
?
S-linked mono-GSH conjugate of 4,4'-methylene diphenyl diisocyanate + H2O
(Cys-Gly)-4,4'-methylene diphenyl diisocyanate + L-glutamate
-
-
-
?
S-methylglutathione + H2O
S-methyl-L-cysteinylglycine + L-glutamate
-
-
-
?
7-(gamma-L-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-glutamate
-
-
-
-
?
7-(gamma-L-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-glutamate
-
-
-
-
?
diclofenac-S-acyl-glutathione + H2O
diclofenac-S-acyl-L-cysteinylglycine + L-glutamate
-
-
-
-
?
diclofenac-S-acyl-glutathione + H2O
diclofenac-S-acyl-L-cysteinylglycine + L-glutamate
-
-
-
-
?
gamma-glutamyl-p-nitroanilide + H2O
L-glutamate + p-nitroaniline
-
the enzyme has low hydrolase activity and high gamma-glutamyl transpeptidase activity
-
-
?
gamma-glutamyl-p-nitroanilide + H2O
L-glutamate + p-nitroaniline
hydrolytic activity
-
-
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
the reaction consists of two steps. First the active O atom of Thr391 attacks the carbonyl carbon atom of the gamma-glutamyl compound to form the gamma-glutamyl-enzyme intermediate, and then the gamma-glutamyl moiety is transferred to another substrate, i.e. reaction of EC 2.3.2.2, or the gamma-glutamyl-enzyme bond is hydrolyzed to reform the resting enzyme. The second step of the reaction, the hydrolysis of the intermediate, is much slower than the first reaction step
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid 4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid 4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid-(4-nitroanilide) + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid-(4-nitroanilide) + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid-(4-nitroanilide) + H2O
4-nitroaniline + L-glutamate
-
-
-
?
L-glutamic acid-(4-nitroanilide) + H2O
4-nitroaniline + L-glutamate
-
-
-
?
additional information
?
-
the enzyme also shows transpeptidase activity
-
-
?
additional information
?
-
the enzyme also shows transpeptidase activity
-
-
?
additional information
?
-
-
the enzyme also shows transpeptidase activity
-
-
?
additional information
?
-
residue Thr391, the N-terminal residue of the small subunit, is the nucleophile for the enzymatic reaction
-
-
?
additional information
?
-
protein additionally has EC 2.3.2.2, gamma-glutamyltransferase activity
-
-
?
additional information
?
-
protein additionally has EC 2.3.2.2, gamma-glutamyltransferase activity
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the reaction of EC 2.3.2.2, gamma-glutamyltransferase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S,S)-gamma-glutamyl-(cis-S-1-propenyl)-thioglycine + H2O
(S)-(cis-S-1-propenyl)thioglycine + L-glutamate
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2RS)-2-amino-4-((R)-1-[N-(carboxymethyl)carbamoyl]-2-chloroethyl(phenyl)-phosphono)butanoic acid
-
potent and irreversible inhibitor of enzyme, second-order rate constant value 188 per M and s, and good mimic of the putative transition state
(2RS)-2-amino-4-((S)-1-[N-(carboxymethyl)carbamoyl]-2-phenylethyl(phenyl)-phosphono)butanoic acid
-
potent and irreversible inhibitor of enzyme, second-order rate constant value 389 per M and s, and good mimic of the putative transition state
(2RS)-2-amino-4-((S)-1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)-phosphono)butanoic acid
-
potent and irreversible inhibitor of human enzyme, second-order rate constant value 145 per M and s, and good mimic of the putative transition state
6-diazo-5-oxo-L-norleucine
pretreatment of cells completely abolishes the extracellular hydrolysis of lgutathione and glutamine
serine borate
competitive, 8fold less effective as an inhibitor of isoform GGT5 than of GGT1; competitive, 8fold less effective as an inhibitor of isoform GGT5 than of GGT1
additional information
neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates
-
2-amino-4-[[3-(carboxymethyl)phenoxy](methoxy)phosphoryl] butanoic acid
the mechanism-based inhibitor
2-amino-4-[[3-(carboxymethyl)phenoxy](methoxy)phosphoryl] butanoic acid
the mechanism-based inhibitor is a stable compound. It inactivates the human enzyme significantly faster than the other phosphonates, and does not inhibit a glutamine amidotransferase. The inhibitor shows no cytotoxicity toward human fibroblasts and hepatic stellate cells up to 1 mM. It serves as a non-toxic, selective and highly potent irreversible inhibitor that can be used for various in vivo as well as in vitro biochemical studies. Critical electrostatic interaction between the terminal carboxylate of the inhibitor and the active-site residue Lys562 of human enzyme for potent inhibition
acivicin
in cells treated with the xenobiotic monochlorobimane, application of acivicin leads to accumulation of glutathione S-bimane conjugates
acivicin
-
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0203
L-glutamic acid-(4-nitroanilide)
mutant T398S, pH 8.0, 25°C
0.57
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-V388, pH 8.0, 25°C
0.74
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-K394, pH 8.0, 25°C
0.76
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-P391, pH 8.0, 25°C
0.81
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I387, pH 8.0, 25°C
1.06
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I396, pH 8.0, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.09
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I396, pH 8.0, 25°C
3.01
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-K394, pH 8.0, 25°C
4.74
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-P391, pH 8.0, 25°C
24.41
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-V388, pH 8.0, 25°C
55.11
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I387, pH 8.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.97
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I396, pH 8.0, 25°C
4.09
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-K394, pH 8.0, 25°C
6.2
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-P391, pH 8.0, 25°C
43.03
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-V388, pH 8.0, 25°C
67.92
L-glutamic acid-(4-nitroanilide)
mutant DELTAY385-I387, pH 8.0, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.8
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C
31.06
5
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C
6.3
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C
6.7
purified recombinant His6-tagged enzyme, substrate L-gamma-glutamyl-4-nitroanilide, pH 9.0, 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
comparable activities at both pH 9.0 and pH 10.0. A similar pattern is observed for R109S
9
comparable activities at both pH 9.0 and pH 10.0. A similar pattern is observed for R109S. Mutant enzyme R109K shows a sharp pH-optimum at pH 9.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
optimum activity at pH 7.0, 80% of maximal activity at pH 6.5-8.0, and residual activity sharply decreased to less than 50% at above pH 10.0 or below pH 4.0
4 - 12
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
activity range, optimum activity at 70°C, relative activities at 30°C and 70°C are approximately 88.86% and 92.75% of the maximal activity, respectively
30 - 60
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang
UniProt
brenda
Bacillus amyloliquefaciens SMB469
Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2
UniProt
brenda
enzyme catalyses both gamma-glutamyl transfer, reaction of EC 2.3.2.2, and hydrolysis reactions at the same time
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
nontumorigenic cell line, low level of gamma-glutamyltranspeptidase
brenda
-
tumorigenic cell line, high level of gamma-glutamyl transpeptidase
brenda
isoform GGT3 is a major contributor to total enzymic activity in roots, but a relatively minor contributor in other tissues
brenda
additional information
isoform GGT3 is transcribed at relatively high levels in all parts of the plant. It is a major contributor to total enzymic activity in roots, but a relatively minor contributor in other tissues
brenda
-
fermentation broth of carbon stressed cultures
brenda
-
fermentation broth of carbon stressed cultures
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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
evolution
Halalkalibacterium halodurans
-
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
-
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
-
evolution
Bacillus amyloliquefaciens SMB469
-
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
-
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)
-
metabolism
-
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
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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-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
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (33603 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
40000
60000
x * 60000, proenzyme, x * 40000, large subunit, plus x * 20000, small subunit, SDS-PAGE
20000
x * 60000, proenzyme, x * 40000, large subunit, plus x * 20000, small subunit, SDS-PAGE
40000
x * 60000, proenzyme, x * 40000, large subunit, plus x * 20000, small subunit, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
?
x * 45000 + x * 22000, SDS-PAGE, all the enzyme variants are of the same molecular weight with large subunit located around 45 kDa and small subunit at 22 kDa
?
-
x * 45000 + x * 22000, SDS-PAGE, all the enzyme variants are of the same molecular weight with large subunit located around 45 kDa and small subunit at 22 kDa
-
?
-
x * 45000 + x * 22000, SDS-PAGE, all the enzyme variants are of the same molecular weight with large subunit located around 45 kDa and small subunit at 22 kDa
-
?
x * 60000, proenzyme, x * 40000, large subunit, plus x * 20000, small subunit, SDS-PAGE
heterodimer
1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
heterodimer
Bacillus amyloliquefaciens SMB469
-
1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
the two separate polypeptide chains of 45.7 and 19.7 kDa forming the GGT heterodimeric enzyme are generated via autocatalytic cleavage from a precursor
proteolytic modification
Bacillus amyloliquefaciens SMB469
-
the two separate polypeptide chains of 45.7 and 19.7 kDa forming the GGT heterodimeric enzyme are generated via autocatalytic cleavage from a precursor
-
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
-
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
enzymes undergoes autocatalytic processing. Crystallization data
proteolytic modification
the processing of a precursor of gamma-glutamyltranspeptidase is an intramolecular autocatalytic event. The catalytic nucleophile for the processing reaction is the oxygen atom of the side chain of Thr391, the N-terminal residue of the small subunit, which is also the nucleophile for the enzymatic reaction. Autocatalytic processing is not inhibited by protease inhibitors, gamma-glutathione hydrolase inhibitor acivicin, or substrate gamma-glutamyl 4-nitroanilide
proteolytic modification
enzyme is expressed as a 60-kDa inactive precursor that must undergo autocatalytic processing to generate a 40-kDa/20-kDa heterodimer with full gamma-glutamyl amide bond hydrolase activity. The new N-terminus of the processed enzyme, Thr380, is the catalytic nucleophile in both the autoprocessing and enzymatic reactions
proteolytic modification
protein is processed to subunits of 23000 and 40000 Da
proteolytic modification
-
protein is processed to subunits of 23000 and 40000 Da
-
proteolytic modification
protein is processed to subunits of 23000 and 40000 Da
proteolytic modification
-
protein is processed to subunits of 23000 and 40000 Da
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, X-ray diffraction data for the co-crystal of transpeptidase and acivicin at 1.45 A resolution. SUMO-tag renders high expression and solubility
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
mutant T391A, unable to undergo autocatalytic processing, at 2.55 A resolution. Structural comparison of the precursor and mature protein demonstrates that the structures of the core regions in the two proteins are unchanged, with marked differences near the active site. In the precursor, the segment corresponding to the C-terminal region of the L-subunit occupies the site where the loop, residues 438-449, forms the lid of the gamma-glutamyl group-binding pocket in the mature enzyme. Upon cleavage of the N-terminal peptide bond of Thr391, the newly produced C-terminus, residues 375390, flips out, allowing the 438-449 segment to form the gamma-glutamyl group-binding pocket. A water molecule is located near the carbonyl carbon atom of Gln-390. The spatial arrangement around the water and Thr391 relative to the scissile peptide bond appears suitable for the initiation of autocatalytic processing
to 1.95 A resolution. The enzyme has a stacked alphabetabetaalpha fold comprising the large and small subunits, similar to the folds seen in members of the N-terminal nucleophile hydrolase superfamily. The active site residue Thr391, the N-terminal residue of the small subunit, is located in the groove, from which the pocket for gamma-glutamyl moiety binding follows. The gamma-glutamyl-enzyme intermediate and the structure of the complex with L-glutamate reveal how the gamma-glutamyl moiety and L-glutamate are recognized by the enzyme. A water molecule is seen on the carbonyl carbon of the gamma-glutamyl-Thr391 O bond in the intermediate that is to be hydrolyzed. The residues essential for enzymic activity, i.e. Arg114, Asp433, Ser462, and Ser463, are all involved in the binding of the gamma-glutamyl moiety
X-ray crystallography of the enzyme in complex with inhibitor 2-amino-4-[[3-(carboxymethyl)phenoxy](methoyl)phosphoryl] butanoic acid
to 1.9 A resolution. The refined model contains two 40-kDa/20-kDa heterodimers in the asymmetric unit and has structural features comparable with other N-terminal nucleophile hydrolases. Autoprocessing of the enzyme leads to a large conformational change, with the loop preceding the catalytic residue Thr380 moving more than 35 A, thus relieving steric constraints that likely limit substrate binding. Cleavage of the proenzyme results in the formation of a threonine-threonine dyad comprised of Thr380 and Thr398. The hydroxyl group of Thr398 is located equidistant from the alpha-amino group and hydroxyl side chain of Thr380
crystals of are grown at room temperature by vapor diffusion with the hanging drop method. For crystallization studies, the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33, purified, and deglycosylated. Crystal structures of human enzyme, including the free enzyme, inhibitor-bound transition states, and glutamate-bound enzyme. Crystal structures of human gamma-glutamyl transpeptidase show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor bound tetrahedral transition states and finally to the glutamate bound structure prior to the release of this final product of the reaction. The structure of the apoenzyme shows flexibility within the active site. The serine-borate-bound enzyme crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state. The structure of 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid-bound enzyme reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAY385-E398
no autocatalytic processing, no catalytic activity
DELTAY385-I387
mutant is able to autoprocess itself, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows increase in catalytic efficiency
DELTAY385-I396
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-K394
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-P391
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-V388
mutant is able to autoprocess itself, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows increase in catalytic efficiency
T391A
T398A
mutation results in an enzyme that is fully capable of autoprocessing but is devoid of enzymatic activity
T398S
retains considerable enzymatic activity, but hydrolysis rates are reduced about 5fold relative to wild-type enzyme and overall catalyticefficiency is diminished by nearly an order of magnitude
T391A
processing-deficient mutant protein, molecular mass of 100000 Da
T391A
unable to undergo autocatalytic processing, crystallization data
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
purified native enzyme, the enzyme retains more than 88% of its activity at 20-70°C, but the enzyme activity is significantly decreased at temperatures above 70°C
40 - 60
thermal stability of BaGGT469 is extremely low and its residual activity is completely lost within 10 min at 60°C. But BaGGT469 is quite stable in the presence of substrate at 40°C
50
70.5
melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in BisTris buffer, pH 5.0
71
melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in bicine buffer, pH 10.0
75
melting temperature of the enzyme inactivated with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid in sodium citrate buffer, pH 6.7
additional information
inactivating the enzyme with 2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]-butanoic acid stabilizes the structure of the enzyme. It increases the melting temperature of the enzyme by about 20°C at all pH levels tested independent of the buffer
50
t1/2: 176 min (mutant enzyme R109M), 16.5 min (mutant enzyme R109S), 69.3 min (wild-type enzyme), 19.8 min (mutant enzyme R109K)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
mutant enzyme R109M shows high salt stability with almost no loss in activity even in the presence of 20% (w/v) NaCl whereas wild-type enzyme and mutant enzyme R109K retain only 50% of residual activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
for crystallization studies, the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33, purified, and deglycosylated
native enzyme 40.7fold from leaves by ammonium sulfate fractionation, dialysis, and gel filtration
-
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in in pET SUMO vector in the host Escherichia coli BL21 (DE3)
gene BaGGT469, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Bacillus subtilis strain KCTC 3135 and in Escherichia coli strain BL21(DE3)
gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
the natural variant V272A of the human enzyme is expressed in Pichia pastoris strain X-33
gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene BaGGT469, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcripts encoding Sclerotinia sclerotiorum gamma-glutamyl transpeptidase accumulate specifically during sclerotium, apothecium, and compound appressorium development
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
ultrasensitive detection of glutathione according to its hydrolysis by gamma-glutamyl transpeptidase and the as-prepared simple and robust LC-based sensing platform has potentials in the diagnosis of glutathione-related diseases, e.g. cancer, liver damage, and malignant neoplasms
medicine
pharmacology
medicine
-
pharmacokinetics of S-(2-(4-chlorophenoxy)-2-methylpropanoyl)glutathione, i.e. clofibryl-S-acyl-glutathione, in urine of rats. gamma-Glutamyltransferase-mediated degradation of S-(2-(4-chlorophenoxy)-2-methylpropanoyl)glutathione leads primarily to the formation and excretion of clofibryl-N-acyl-cysteine products rather than the S-acyl-N-acetylcysteine conjugate. Clofibryl-S-acyl-glutathione is degraded to clofibryl-N-acyl-cysteinylglycine, clofibril-N-acyl-cysteine and their respective S-methylated products. The mercapturic acid conjugate is found as a minor product
medicine
-
the metabolism of S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)glutathione in the V79 GGT cell line is associated with a considerable increase of cytotoxicity. The cytotoxic effect is dose- and time-dependent, with 100% cellular death at 200 mM S-(5-hydroxy-2-pentyltetrahydrofuran-3-yl)glutathione after 24 h incubation in V79 GGT cells
medicine
-
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
medicine
-
treatment of rats with diclofenac results in accumulation of diclofenac-N-acyl-cysteinylglycine and diclofenac-N-acyl-cysteine in bile, albeit only about 1% of the administered dose of diclofenac within 6 h
medicine
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
pharmacology
the enzyme is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target
pharmacology
the enzyme is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target
pharmacology
-
the enzyme is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target
-
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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
brenda
Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism
J. Biol. Chem.
282
2433-2439
2007
Escherichia coli (P18956)
brenda
Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate
Proc. Natl. Acad. Sci. USA
103
6471-6476
2006
Escherichia coli (P18956)
brenda
Grzam, A.; Martin, M.N.; Hell, R.; Meyer, A.J.
gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
FEBS Lett.
581
3131-3138
2007
Arabidopsis thaliana (Q9M0G0)
brenda
Ohkama-Ohtsu, N.; Oikawa, A.; Zhao, P.; Xiang, C.; Saito, K.; Oliver, D.J.
A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis
Plant Physiol.
148
1603-1613
2008
Arabidopsis thaliana (Q9M0G0)
brenda
Grillo, M.P.; Hua, F.; March, K.L.; Benet, L.Z.; Knutson, C.G.; Ware, J.A.
Gamma-glutamyltranspeptidase-mediated degradation of diclofenac-S-acyl-glutathione in vitro and in vivo in rat
Chem. Res. Toxicol.
21
1933-1938
2008
Bos taurus, Rattus norvegicus
brenda
Wickham, S.; West, M.; Cook, P.; Hanigan, M.
Gamma-glutamyl compounds: Substrate specificity of gamma-glutamyl transpeptidase enzymes
Anal. Biochem.
414
208-214
2011
Homo sapiens (P19440), Homo sapiens (P36269)
brenda
Enoiu, M.; Herber, R.; Wennig, R.; Marson, C.; Bodaud, H.; Leroy, P.; Mitrea, N.; Siest, G.; Wellman, M.
gamma-Glutamyltranspeptidase-dependent metabolism of 4-hydroxynonenal-glutathione conjugate
Arch. Biochem. Biophys.
397
18-27
2002
Homo sapiens
brenda
Accaoui, M.; Enoiu, M.; Mergny, M.; Masson, C.; Dominici, S.; Wellman, M.; Visvikis, A.
Gamma-glutamyltranspeptidase-dependent glutathione catabolism results in activation of NF-kB
Biochem. Biophys. Res. Commun.
276
1062-1067
2000
Homo sapiens
brenda
Hanigan, M.; Ricketts, W.
Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase
Biochemistry
32
6302-6306
1993
Homo sapiens
brenda
Hultberg, M.; Hultberg, B.
Glutathione turnover in human cell lines in the presence of agents with glutathione influencing potential with and without acivicin inhibition of gamma-glutamyltranspeptidase
Biochim. Biophys. Acta
1726
42-47
2005
Homo sapiens
brenda
Stark, A.; Zeiger, E.; Pagano, D.
Glutathione mutagenesis in Salmonella typhimurium is a gamma-glutamyltranspeptidase-enhanced process involving active oxygen species
Carcinogenesis
9
771-777
1988
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Grillo, M.; Benet, L.
Interaction of gamma-glutamyltranspeptidase with clofibryl-S-acyl-glutathione in vitro and in vivo in rat
Chem. Res. Toxicol.
14
1033-1040
2001
Rattus norvegicus
brenda
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)
brenda
Meredith, M.; Williams, G.
Intracellular glutathione cycling by gamma-glutamyl transpeptidase in tumorigenic and nontumorigenic cultured rat liver cells
J. Biol. Chem.
261
4986-4992
1986
Rattus norvegicus
brenda
Suzuki, H.; Kumagai, H.
Autocatalytic processing of gamma-glutamyltranspeptidase
J. Biol. Chem.
277
43536-43543
2002
Escherichia coli (P18956)
brenda
Boanca, G.; Sand, A.; Okada, T.; Suzuki, H.; Kumagai, H.; Fukuyama, K.; Barycki, J.J.
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad
J. Biol. Chem.
282
534-541
2007
Helicobacter pylori (O25743)
brenda
Shibayama, K.; Wachino, J.; Arakawa, Y.; Saidijam, M.; Rutherford, N.; Henderson, P.
Metabolism of glutamine and glutathione via gamma-glutamyltranspeptidase and glutamate transport in Helicobacter pylori: Possible significance in the pathophysiology of the organism
Mol. Microbiol.
64
396-406
2007
Helicobacter pylori (O25743)
brenda
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)
brenda
Kushwaha, N.; Srivastava, S.
Gamma-glutamyl transpeptidase from two plant growth promoting rhizosphere fluorescent pseudomonads
Antonie van Leeuwenhoek
105
45-56
2014
Pseudomonas protegens (L7Z147), Pseudomonas fluorescens (Q4KIM5), Pseudomonas fluorescens Pf-5 (Q4KIM5), Pseudomonas protegens PfT-1 (L7Z147)
brenda
Chi, M.C.; Lo, Y.H.; Chen, Y.Y.; Lin, L.L.; Merlino, A.
gamma-Glutamyl transpeptidase architecture: Effect of extra sequence deletion on autoprocessing, structure and stability of the protein from Bacillus licheniformis
Biochim. Biophys. Acta
1844
2290-2297
2014
Bacillus licheniformis (A9YTT0)
brenda
Nakajima, M.; Watanabe, B.; Han, L.; Shimizu, B.; Wada, K.; Fukuyama, K.; Suzuki, H.; Hiratake, J.
Glutathione-analogous peptidyl phosphorus esters as mechanism-based inhibitors of gamma-glutamyl transpeptidase for probing cysteinyl-glycine binding site
Bioorg. Med. Chem.
22
1176-1194
2014
Escherichia coli, Homo sapiens
brenda
Ito, R.; Ihara, H.; Okada, T.; Ikeda, Y.
1alpha,25-Dihydroxyvitamin D3 enhances gamma-glutamyl transpeptidase activity in LLC-PK1 porcine kidney epithelial cells
Mol. Med. Rep.
10
2111-2115
2014
Sus scrofa
brenda
Li, M.; Liang, X.; Rollins, J.
Sclerotinia sclerotiorum gamma-glutamyl transpeptidase (Ss-Ggt1) is required for regulating glutathione accumulation and development of sclerotia and compound appressoria
Mol. Plant Microbe Interact.
25
412-420
2012
Sclerotinia sclerotiorum
brenda
Zhang, G.; Ducatelle, R.; Pasmans, F.; DHerde, K.; Huang, L.; Smet, A.; Haesebrouck, F.; Flahou, B.
Effects of Helicobacter suis gamma-glutamyl transpeptidase on lymphocytes: modulation by glutamine and glutathione supplementation and outer membrane vesicles as a putative delivery route of the enzyme
PLoS ONE
8
e77966
2013
Helicobacter suis (D5LUP7)
brenda
Zhou, L.; Kang, Q.; Hu, O.; Yu, L.
Ultrasensitive detection of glutathione based on liquid crystals in the presence of gamma-glutamyl transpeptidase
Anal. Chim. Acta
1040
187-195
2018
Homo sapiens (P19440)
brenda
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 subtilis, Halalkalibacterium halodurans, Escherichia coli (P18956), Homo sapiens (P19440), Saccharomyces cerevisiae (Q05902), Bacillus anthracis (Q51693), Helicobacter pylori (Q9F5N9), Thermoplasma acidophilum (Q9HJH4), Bacillus subtilis BEST7613, Saccharomyces cerevisiae ATCC 204508 (Q05902), Escherichia coli K12 (P18956), Thermoplasma acidophilum ATCC 25905 (Q9HJH4)
brenda
Kamiyama, A.; Nakajima, M.; Han, L.; Wada, K.; Mizutani, M.; Tabuchi, Y.; Kojima-Yuasa, A.; Matsui-Yuasa, I.; Suzuki, H.; Fukuyama, K.; Watanabe, B.; Hiratake, J.
Phosphonate-based irreversible inhibitors of human gamma-glutamyl transpeptidase (GGT). GGsTop is a non-toxic and highly selective inhibitor with critical electrostatic interaction with an active-site residue Lys562 for enhanced inhibitory activity
Bioorg. Med. Chem.
24
5340-5352
2016
Escherichia coli (P18956), Homo sapiens (P19440), Escherichia coli K12 (P18956)
brenda
Terzyan, S.S.; Burgett, A.W.; Heroux, A.; Smith, C.A.; Mooers, B.H.; Hanigan, M.H.
Human gamma-glutamyl transpeptidase 1 structures of the free enzyme, inhibitor-bound tetrahedral transition states, and glutamate-bound enzyme reveal novel movement within the active site during catalysis
J. Biol. Chem.
290
17576-17586
2015
Homo sapiens (P19440)
brenda
Bindal, S.; Sharma, S.; Singh, T.P.; Gupta, R.
Evolving transpeptidase and hydrolytic variants of gamma-glutamyl transpeptidase from Bacillus licheniformis by targeted mutations of conserved residue Arg109 and their biotechnological relevance
J. Biotechnol.
249
82-90
2017
Bacillus licheniformis (A9YTT0), Bacillus licheniformis ER-15 (A9YTT0)
brenda
Spitzmller, Z.; Gonda, S.; Kiss-Szikszai, A.; Vasas, G.; Pocsi, I.; Emri, T.
Characterization of extracellular gamma-glutamyl transpeptidase from Aspergillus nidulans
Mycoscience
57
400-403
2016
Aspergillus nidulans, Aspergillus nidulans FGSC A26
-
brenda
Kumari, S.; Pal, R.K.; Gupta, R.; Goel, M.
High resolution X-ray diffraction dataset for Bacillus licheniformis gamma glutamyl transpeptidase-acivicin complex SUMO-Tag renders high expression and solubility
Protein J.
36
7-16
2017
Bacillus licheniformis (A9YTT0), Bacillus licheniformis ER-15 (A9YTT0)
brenda
Wisnewski, A.V.; Liu, J.; Nassar, A.F.
In vitro cleavage of diisocyanate-glutathione conjugates by human gamma-glutamyl transpeptidase-1
Xenobiotica
46
726-732
2016
Homo sapiens (P19440)
brenda
Liu, C.; Jia, J.; Wang, H.; Xue, L.; Kong, Y.; Wang, F.
Purification and characterization of a flavor-related enzyme, gamma-glutamyl-transpeptidase, from Toona sinensis leaves
J. Hortic. Sci. Biotechnol.
91
611-618
2016
Toona sinensis
-
brenda
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 velezensis (A7Z5E0), Bacillus subtilis (P54422), Bacillus licheniformis (Q65KZ6), Bacillus subtilis 168 (P54422), Bacillus licheniformis NCIMB 9375 (Q65KZ6), Bacillus licheniformis Gibson 46 (Q65KZ6), Bacillus licheniformis JCM 2505 (Q65KZ6), Bacillus licheniformis NRRL NRS-1264 (Q65KZ6), Bacillus velezensis BGSC 10A6 (A7Z5E0), Bacillus velezensis DSM 23117 (A7Z5E0), Bacillus amyloliquefaciens SMB469 (A0A1S5V3K5), Bacillus licheniformis NBRC 12200 (Q65KZ6), Bacillus licheniformis ATCC 14580 (Q65KZ6), Bacillus velezensis FZB42 (A7Z5E0), Bacillus licheniformis DSM 13 (Q65KZ6)
brenda
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