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Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P54422
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2.3.2.2 gamma-glutamyltransferaseIUBMB Comments
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
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- 2.3.2.2
- aminotransferase
-
alt
- bilirubin
- cholesterol
- albumin
- triglyceride
- bile
- biliary
- women
- creatinine
- gsh
- transaminase
- hepatocytes
- cirrhosis
- fibrosis
- urinary
- cholestasis
- duct
-
uric
-
c-reactive
- steatosis
- aminopeptidase
- jaundice
-
drinkers
-
hepatotoxicity
-
non-alcoholic
-
intrahepatic
- nafld
-
nephrotoxicity
-
ursodeoxycholic
-
waist
-
ultrasonography
- diethylnitrosamine
-
circumference
-
corpuscular
-
hepatocarcinogenesis
-
abuse
-
hepatectomy
- hepatobiliary
- phenobarbital
-
preneoplastic
- alpha-fetoprotein
-
homa-ir
-
abstinence
- pruritus
- 2-acetylaminofluorene
-
n-acetyl-beta-d-glucosaminidase
- cholangitis
-
cholangiopancreatography
- pharmacology
-
elastography
- diagnostics
- nutrition
- food industry
- drug development
- analysis
- medicine
- synthesis
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
a (5-L-glutamyl)-peptide
+
=
+
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glutamyl transpeptidase
-
-
-
-
gamma-glutamyl peptidyltransferase
-
-
-
-
gamma-glutamyl transpeptidase
-
-
-
-
gamma-GPT
-
-
-
-
gamma-GT
-
-
-
-
gamma-GTP
-
-
-
-
glutamyl transpeptidase
-
-
-
-
glutamyltransferase, gamma-
-
-
-
-
L-gamma-glutamyl transpeptidase
-
-
-
-
L-gamma-glutamyltransferase
-
-
-
-
L-glutamyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
CAS REGISTRY NUMBER
COMMENTARY
9046-27-9
-
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
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
?
(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
chromogenic gamma-glutamyl-4-nitroanilide (GPNA) reacts as the donor substrate affording the gamma-glutamyl-enzyme intermediate through reaction with the catalytically active threonine residue at the N-terminus of the small subunit of the enzyme. In this step 4-nitroaniline (PNA) is liberated, which can be spectrophotometrically detected at 410 nm. The gamma-glutamyl-enzyme intermediate is then resolved by nucleophilic attack of the free amino group of glycylglycine, present in solution in excess amount. The transpeptidation product gamma-glutamylglycylglycine is formed and the enzyme is restored in its free state, able to start a new catalytic cycle. The reaction of the gamma-glutamyl enzyme intermediate with a nucleophile is the rate-determining step of the process, thus the rate of liberation of PNA is usually considered a measure of the rate of the transpeptidase activity
-
-
?
5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
best substrate
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
-
-
?
5-L-glutamine + 5-L-glutamine
5-poly-glutamic acid + glutamate
-
-
-
?
5-L-glutamyglycylglycine + acceptor
glycylglycine + 5-L-glutamyl-acceptor
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
-
113.6% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Asn
4-nitroaniline + 5-L-glutamyl-Asn
-
39.3% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
-
4.5% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
-
46.9% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + DL-Phe
4-nitroaniline + 5-L-glutamyl-DL-Phe
-
39.9% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
-
4.4% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + H2O
p-nitroaniline + Glu
-
in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
-
-
?
5-L-glutamyl-4-nitroanilide + His
4-nitroaniline + 5-L-glutamyl-His
-
82.9% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Ile
4-nitroaniline + 5-L-glutamyl-Ile
-
20.7% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Ala
4-nitroaniline + 5-L-glutamyl-L-Ala
-
9.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Arg
4-nitroaniline + 5-L-glutamyl-L-Arg
-
21.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Asn
4-nitroaniline + 5-L-glutamyl-L-Asn
-
24.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Asp
4-nitroaniline + 5-L-glutamyl-L-Asp
-
20.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Cys
4-nitroaniline + 5-L-glutamyl-L-Cys
-
11.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Gln
4-nitroaniline + 5-L-glutamyl-L-Gln
-
5.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Glu
4-nitroaniline + 5-L-glutamyl-L-Glu
-
8.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-His
4-nitroaniline + 5-L-glutamyl-L-His
-
35.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Ile
4-nitroaniline + 5-L-glutamyl-L-Ile
-
19.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Leu
4-nitroaniline + 5-L-glutamyl-L-Leu
-
21.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Lys
4-nitroaniline + 5-L-glutamyl-L-Lys
-
11.2% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Met
4-nitroaniline + 5-L-glutamyl-L-Met
-
50.6% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Phe
4-nitroaniline + 5-L-glutamyl-L-Phe
-
38.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Pro
4-nitroaniline + 5-L-glutamyl-L-Pro
-
12.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Ser
4-nitroaniline + 5-L-glutamyl-L-Ser
-
12.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Thr
4-nitroaniline + 5-L-glutamyl-L-Thr
-
34% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Trp
4-nitroaniline + 5-L-glutamyl-L-Trp
-
30.9% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-tyrosine
4-nitroaniline + 5-L-glutamyl-L-tyrosine
-
24.1% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + L-Val
4-nitroaniline + 5-L-glutamyl-L-Val
-
30.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Leu
4-nitroaniline + 5-L-glutamyl-Leu
-
21.3% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Lys
4-nitroaniline + 5-L-glutamyl-Lys
-
79.4% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
48.8% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Pro
4-nitroaniline + 5-L-glutamyl-Pro
-
13.8% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Ser
4-nitroaniline + 5-L-glutamyl-Ser
-
12.8% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + taurine
4-nitroaniline + 5-L-glutamyl-taurine
-
68.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Thr
4-nitroaniline + 5-L-glutamyl-Thr
-
27.3% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Tyr
4-nitroaniline + 5-L-glutamyl-Tyr
-
34.0% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Val
4-nitroaniline + 5-L-glutamyl-Val
-
30.2% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-L-His + Gly-Gly
L-His + 5-L-glutamyl-Gly-Gly
-
106% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-L-Met + Gly-Gly
L-Met + 5-L-glutamyl-Gly-Gly
-
114% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-L-Phe + Gly-Gly
L-Phe + 5-L-glutamyl-Gly-Gly
-
103% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-L-Trp + Gly-Gly
L-Trp + 5-L-glutamyl-Gly-Gly
-
127% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-L-Tyr + Gly-Gly
L-Tyr + 5-L-glutamyl-Gly-Gly
-
94.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-L-Val + Gly-Gly
L-Val + 5-L-glutamyl-Gly-Gly
-
113% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
involved in polyglutamic acid synthesis
-
-
?
GSH + Gly-Gly
?
-
98.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
-
-
-
?
L-Gln + Gly-Gly
NH3 + 5-L-glutamyl-Gly-Gly
-
78.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donors are Glu, alpha-L-Glu-L-Ala
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
dipeptides are better acceptors than free amino acids
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: autotranspeptidation with another donor molecule as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
acceptor specificity, overview
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor specificity, overview
-
?
5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
-
37.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
-
33.2% of the activity with Gly-Gly
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
-
-
?
poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end
-
-
?
poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
successive hydrolysis from the amino-terminal end
-
-
?
additional information
?
-
substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine
-
-
-
additional information
?
-
-
substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine
-
-
-
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
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
involved in polyglutamic acid synthesis
-
-
?
poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acivicin
i.e. L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
thermodynamics and kinetic analysis of free and immobilized recombinant enzymes, overview
-
0.579
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized modified wild-type enzyme MTWs-GGT-Phar, pH 8.0, 37°C
0.597
L-gamma-glutamyl-4-nitroanilide
-
recombinant free wild-type enzyme GGT, pH 8.0, 37°C
0.879
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized wild-type enzyme, MTWs-GGT, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.9
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 9.5
-
transpeptidation with 5-L-glutamyl-4-nitroanilide and glycylglycine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
50% of maximal activity within this range, recombinant wild-type free enzyme, over 80% of maximal activity within this range, recombinant wild-type immobilized enzyme modified MTWs-GGT-Phar, the activity of recombinant immobilized enzyme MTWs-GGT is abolished above pH 10.0
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: 65% of maximal activity
7.5 - 10
-
pH 7.5: about 40% of maximal activity, pH 10.0: about 35% of maximal activity, glutaminase activity of mutant enzyme D445A
7.5 - 9
-
about half-maximal activity at pH 7.5, about 90% of maximal activity at pH 9.0
8 - 11
8 - 11
-
pH 8.0: about 60% of maximal activity, pH 11: about 75% of maximal activity, transpeptidation with 5-L-glutamyl-4-nitroanilide and glycylglycine
8 - 11
-
pH 8.0: about 60% of maximal activity, pH 8.5-11: optimum, hydrolysis of 5-L-glutamyl-4-nitroanilide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
20°C: about 70% of maximal activity, 60°C: about 90% of maximal activity, 70°C: about 40% of maximal activity
45 - 80
-
about half-maximal activity at 45°C and about 70% of maximal activity at 80°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in wild-type the enzyme is synthesized only during the mid-stationary phase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
gamma-glutamyltransferases (GGTs) are widespread, conserved enzymes that catalyze the transfer of the gamma-glutamyl moiety from a donor substrate to water (hydrolysis, EC 3.4.19.13) or to an acceptor amino acid (transpeptidation)through the formation of a gamma-glutamyl enzyme intermediate
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
purified recombinant wild-type and inactive mutant enzymes both induce similar levels of osteoclastogenesis in Mus musculus mixed osteoblast and bone marrow-derived macrophage cell culture. Bacillus subtilis GGT possesses virulent bone-resorbing activity and its activity is probably independent of its enzymatic activity. The GGT heavy subunit shows strong activity of osteoclastogenesis while the light subunit fails to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. Since the GGT light subunit contains the catalytic pocket, enzymatic activity may not be required for this virulence activity. In addition, recombinant Bacillus subtilis GGT stimulates mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2) in mouse cells, while an osteoprotegerin inhibits the osteoclast formation induced by the GGT heavy subunit. Bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
dimer
heterodimer
heterodimer
one heavy subunit and one light subunit, the active site of GGT that catalyzes the transfer of gamma-glutamyl group, is located in the light subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with L-glutamate, hanging drop vapor diffusion method, using poly(ethylene glycol) 4000, 100 mM MES buffer (pH 7.0), 600 mM NaCl, and 5% (v/v) Jeffamine M-600
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D445A
-
mutation abolishes transpeptidation activity, specific activity for hydrolysis is 40.2% of that of the wild-type enzyme, salt tolerant like the wild-type enzyme
D445E
-
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
D445N
-
transpeptidation activity is 42% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
D445Y
-
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
R113K
-
transpeptidation activity is 72% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
additional information
additional information
GGT enzyme-defective Bacillus subtilis mutant strain 2288
additional information
-
GGT enzyme-defective Bacillus subtilis mutant strain 2288
additional information
-
immobilization of purified recombinant His-tagged enzyme on a mesoporous titania oxide whisker (MTWs) carrier further modified with PharmalyteMT (Phar) 8.0-10.5 to yield MTWs-GGT-Phar, method optimization and evaluation, overview. Modified MTWs-GGT-Phar exhibits a stable enzyme activity in the pH range of pH 6.0-11.0 and an optimum temperature 10°C higher than GGT. Its pH stability at pH 11.0 and thermalstability at 50°C are 23.7 times and 19.4 times higher, respectively, than those of free GGT. In addition, the affinity constant Km of MTWs-GGT-Phar towards GpNA is slightly lower than that of free GGT, indicating that Phar has a protective effect on the structure of GGT
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
pH stabilities of free GGT, immobilized MTWs-GGT, and immobilized modified MTWs-GGT-Phar, overview
756934
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is highly salt-tolerant, at pH 5.5 in presence of 18% NaCl, 49% of the transpeptidation activity and 86% of the hydrolysis activity remains, conversion of Gln to Glu shows 76% residual activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal His-tagged enzyme is purified by ammonium sulfate precipitation and Sephacryl S-200 gel filtration
recombinant extracellular C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant GGT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-pET22b by nickel affinity chromatography and dialysis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant GGTs in Escherichia coli strain BL21(DE3), recombinant overexpression of GGT in Bacillus subtilis strain MH2308 from plasmid pMH2312, semi-quantitative reverse-transcription PCR enzyme expression analysis
gene ggt, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-pET22b
-
GGT of Bacillus subtilis is synthesized only during the mid-stationary phase, which is inconvenient for industrial use, a strain overexpressing GGT for a sufficiently long period is generated to obtain large quantities of GGT. A plasmid vector, pHY300PLK, containing the ggt gene cloned from chromosomal DNA is introduced into a spo0A abrB double mutant strain, in which the level of GGT activity is high after the mid-stationary phase. The level of GGT activity in this strain increases steadily after the exponential phase, becoming 15fold higher than that in the parental strain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
synthesis
-
the enzyme can catalyze the transfer of L-glutamine to Gly-Gly to synthesize Gln-Gly-Gly, which is promising for the synthesis of valuable gamma-glutamyl peptides
nutrition
-
mutant enzyme D445A is suitable for fermentation of soy sauce and miso
nutrition
-
the enzyme is suitable for food fermentation under high salt conditions, e.g. the fermentation of soy sauce and miso
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogawa, Y.; Hosoyama, H.; Hamano, M.; Motai, H.
Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto)
Agric. Biol. Chem.
55
2971-2977
1991
Bacillus subtilis
Minami, H.; Suzuki, H.; Kumagai, H.
Salt-tolerant gamma-glutamyltranspeptidase from Bacillus subtilis 168 with glutaminase activity
Enzyme Microb. Technol.
32
431-438
2003
Bacillus subtilis, Bacillus subtilis 168
-
Minami, H.; Suzuki, H.; Kumagai, H.
A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity
FEMS Microbiol. Lett.
224
169-173
2003
Bacillus subtilis
Kimura, K.; Tran, L.S.; Uchida, I.; Itoh, Y.
Characterization of Bacillus subtilis gamma-glutamyltransferase and its involvement in the degradation of capsule poly-gamma-glutamate
Microbiology
150
4115-4123
2004
Bacillus subtilis (Q83XQ6), Bacillus subtilis, Bacillus subtilis NAFM5 (Q83XQ6), Bacillus subtilis NAFM5
Wu, Q.; Xu, H.; Zhang, L.; Yao, J.; Ouyang, P.
Production, purification and properties of gamma-glutamyltranspeptidase from a newly isolated Bacillus subtilis NX-2
J. Mol. Catal. B
43
113-117
2006
Bacillus subtilis, Bacillus subtilis NX-2
-
Wada, K.; Irie, M.; Suzuki, H.; Fukuyama, K.
Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket
FEBS J.
277
1000-1009
2010
Bacillus subtilis (P54422), Bacillus subtilis, Bacillus subtilis 168 (P54422)
Balakrishna, S.; Prabhune, A.
Gamma-glutamyl transferases: A structural, mechanistic and physiological perspective
Front. Biol.
9
51-65
2014
Homo sapiens (P19440), Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
-
Balakrishna, S.; Prabhune, A.
Effect of pH on the hydrolytic kinetics of gamma-glutamyl transferase from Bacillus subtilis
ScientificWorldJournal
2014
216270
2014
Bacillus subtilis
Calvio, C.; Romagnuolo, F.; Vulcano, F.; Speranza, G.; Morelli, C.
Data for the synthesis of oligo-gamma-glutamylglutamines as model compounds for gamma-glutamyltransferases (GGTs) and for normalization of activities of different GGTs
Data Brief
21
576-581
2018
Bacillus subtilis (P54422), Bacillus subtilis, Bacillus subtilis 168 (P54422)
Ni, F.; Zhang, F.; Yao, Z.; Ye, L.; Sun, Y.; Wang, H.; Zhou, Z.; Zhu, B.
Improving the catalytic properties and stability of immobilized gamma-glutamyltranspeptidase by post-immobilization with PharmalyteMT 8-10.5
Int. J. Biol. Macromol.
105
1581-1586
2017
Bacillus subtilis, Bacillus subtilis 168
Kim, J.; Jang, S.; Kim, A.; Su, H.; Gunawardhana, N.; Jeon, Y.; Bak, E.; Kim, J.; Cha, J.
Role of bacterial gamma-glutamyltranspeptidase as a novel virulence factor in bone-resorbing pathogenesis
J. Microbiol.
54
396-402
2016
Bacillus subtilis (P54422), Bacillus subtilis, Bacillus subtilis 168 (P54422)
Lee, J.; Lee, J.; Nam, G.; Son, B.; Jang, M.; Lee, S.; Hurh, B.; Kim, T.
Heterologous expression and enzymatic characterization of gamma-glutamyltranspeptidase from Bacillus amyloliquefaciens
J. Microbiol.
55
147-152
2017
Bacillus amyloliquefaciens (A0A1S5V3K5), Bacillus amyloliquefaciens, Bacillus velezensis (A7Z5E0), Bacillus subtilis (P54422), Bacillus subtilis, Bacillus licheniformis (Q65KZ6), Bacillus licheniformis, 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)
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