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Information on EC 2.3.2.2 - gamma-glutamyltransferase
for references in articles please use BRENDA:EC2.3.2.2
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.2 gamma-glutamyltransferase
IUBMB 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].
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 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
Reaction Schemes
showa (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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase
alpha-glutamyl transpeptidase
-
-
-
-
AngammaGT
BaGGT
BaGGT42
BaGGT469
BlGGT
BlGGT13
BsGGT168
Cgl0954
gamma-glutamyl peptidyltransferase
-
-
-
-
gamma-glutamyl transferases
gamma-glutamyl transpeptidase
gamma-glutamyltransferase
gamma-glutamyltranspeptidase
gamma-GPT
-
-
-
-
gamma-GT
gamma-GTP
-
-
-
-
gammaGT
GGT
GGT1
GGT2
GGT3
GGT4
GGT5
ggtB
glutamyl transpeptidase
-
-
-
-
glutamyltransferase, gamma-
-
-
-
-
L-gamma-glutamyl transpeptidase
-
-
-
-
L-gamma-glutamyltransferase
-
-
-
-
L-glutamyltransferase
-
-
-
-
PnGGT
SBLGGT
additional information
gamma-glutamyl transpeptidase
-
-
-
-
gamma-GT
-
-
-
-
GGT
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
almost the entire glutamyl moiety is necessary for recognition in the binding site of the donor substrate
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic mechanism, pH-dependence
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site on small subunit
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site on small subunit
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
ping-pong bi bi mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
the enzyme binds glutathione as donor substrate and initially forms a gamma-glutamyl enzyme that can then react with a water molecule or an acceptor substrate (usually an amino acid or a dipeptide) to form glutamate or a product containing a new gamma-glutamyl isopeptide bond, respectively, thus regenerating the free enzyme
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
the Escherichia coli enzyme is a nonselective enzyme that accommodates substrates without specifically recognizing the C-terminal carboxy group of the Cys-Gly moiety of gamma-glutamyl compounds or the acceptor molecules
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
in the human enzyme, a specific residue in the Cys-Gly binding site plays a critical role in recognizing the Cys-Gly moiety or the acceptor molecules by interacting with the C-terminal carboxy group, whereas the Cys side chain and the Cys-Gly amide bond are not recognized significantly
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic mechanism, pH-dependence
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site on small subunit
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
kinetic study
-
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
gamma-glutamyl cycle, hypoglycin biosynthesis, leukotriene biosynthesis, peptido-conjugates in tissue regeneration biosynthesis
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9046-27-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
(S,S)-gamma-glutamyl-(cis-S-1-propenyl)-thioglycine + ?
(S)-(cis-S-1-propenyl)thioglycine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-(Cys-Gly) + L-Glu-Gly-Gly
-
Substrates: -
Products: -
Products: -
?
4,4'-diphenylmethane diisocyanate linked GSH-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + L-Glu-Gly-Gly
-
Substrates: -
Products: -
Products: -
?
5-D-glutamyl 3-carboxy-4-nitroanilide + glycylglycine
5-D-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-D/L-glutamyl-phenylhydrazine + acceptor
phenylhydrazine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: product is cytotoxic
Products: product is cytotoxic
ir
5-L-glutamine + 5-L-glutamine
5-poly-glutamic acid + glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyglycylglycine + acceptor
glycylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl 3-carboxy-4-nitroanilide + glucana
5-amino-2-nitrobenzoic acid + N-(3-carboxy-4-nitrophenyl)-L-glutaminyl-L-glutamic acid
-
Substrates: -
Products: -
Products: -
ir
5-L-glutamyl 3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine
5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine
5-L-glutamyl 4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
Substrates: in the standard GGT assay with gamma-glutamyl p-nitroanilide as substrate, GGT1 accounts for 80% to 99% of the activity in all tissues except seeds where GGT2 is 50% of the activity
Products: -
Products: -
?
5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
5-L-glutamyl-3-carboxy-4-nitroanilide + 5-L-glutamyl-3-carboxy-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-3-carboxy-4-nitroanilide + 3-carboxy-4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
5-L-glutamyl-4-methoxy-2-naphthylamide + glycylglycine
5-L-glutamyl-glycylglycine + 4-methoxy-2-naphthylamine
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate
4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine
5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid
4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid
5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
5-L-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Ala-Ala-Ala
4-nitroaniline + 5-L-glutamyl-Ala-Ala-Ala
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Asn
4-nitroaniline + 5-L-glutamyl-Asn
-
Substrates: 39.3% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + DL-Phe
4-nitroaniline + 5-L-glutamyl-DL-Phe
-
Substrates: 39.9% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + ethylamine
N-ethyl-L-glutamine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Gly-Gly-Ala
4-nitroaniline + 5-L-glutamyl-Gly-Gly-Ala
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Gly-Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly-Gly
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycyl-glycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycyl-L-proline
4-nitroaniline + 5-L-glutamyl-glycyl-L-proline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
p-nitroaniline + Glu
-
Substrates: in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Ala
4-nitroaniline + 5-L-glutamyl-L-Ala
-
Substrates: 9.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanylglycine
4-nitroaniline + 5-L-glutamyl-L-alanylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Arg
4-nitroaniline + 5-L-glutamyl-L-Arg
-
Substrates: 21.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Asn
4-nitroaniline + 5-L-glutamyl-L-Asn
-
Substrates: 24.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Asp
4-nitroaniline + 5-L-glutamyl-L-Asp
-
Substrates: 20.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Cys
4-nitroaniline + 5-L-glutamyl-L-Cys
-
Substrates: 11.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Gln
4-nitroaniline + 5-L-glutamyl-L-Gln
-
Substrates: 5.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Glu
4-nitroaniline + 5-L-glutamyl-L-Glu
-
Substrates: 8.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-His
4-nitroaniline + 5-L-glutamyl-L-His
-
Substrates: 35.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-hydroxyproline
4-nitroaniline + 5-L-glutamyl-L-hydroxyproline
5-L-glutamyl-4-nitroanilide + L-Ile
4-nitroaniline + 5-L-glutamyl-L-Ile
-
Substrates: 19.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Leu
4-nitroaniline + 5-L-glutamyl-L-Leu
-
Substrates: 21.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-leucyl-L-alanine
4-nitroaniline + 5-L-glutamyl-L-leucyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Lys
4-nitroaniline + 5-L-glutamyl-L-Lys
-
Substrates: 11.2% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methioninamide
4-nitroaniline + 5-L-glutamyl-L-methioninamide
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionyl(2,2,2-trifluoroethylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(2,2,2-trifluoroethylamide)
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionyl(2-fluoroethylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(2-fluoroethylamide)
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionyl(3,3,3-trifluoropropylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(3,3,3-trifluoropropylamide)
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionylethylamide
4-nitroaniline + 5-L-glutamyl-L-methionylethylamide
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionylpropylamide
4-nitroaniline + 5-L-glutamyl-L-methionylpropylamide
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Phe
4-nitroaniline + 5-L-glutamyl-L-Phe
-
Substrates: 38.4% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
5-L-glutamyl-4-nitroanilide + L-Pro
4-nitroaniline + 5-L-glutamyl-L-Pro
-
Substrates: 12.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Ser
4-nitroaniline + 5-L-glutamyl-L-Ser
-
Substrates: 12.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Thr
4-nitroaniline + 5-L-glutamyl-L-Thr
-
Substrates: 34% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Trp
4-nitroaniline + 5-L-glutamyl-L-Trp
-
Substrates: 30.9% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-tyrosine
4-nitroaniline + 5-L-glutamyl-L-tyrosine
-
Substrates: 24.1% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Val
4-nitroaniline + 5-L-glutamyl-L-Val
-
Substrates: 30.5% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Leu
4-nitroaniline + 5-L-glutamyl-Leu
-
Substrates: 21.3% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Pro
4-nitroaniline + 5-L-glutamyl-Pro
-
Substrates: 13.8% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + S-alkylcysteine sulfoxide
4-nitroaniline + 5-L-glutamyl-S-alkylcysteine sulfoxide
-
Substrates: best substrates
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Ser
4-nitroaniline + 5-L-glutamyl-Ser
-
Substrates: 12.8% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + taurine
4-nitroaniline + 5-L-glutamyl-taurine
-
Substrates: 68.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Tyr
4-nitroaniline + 5-L-glutamyl-Tyr
-
Substrates: 34.0% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Val
4-nitroaniline + 5-L-glutamyl-Val
-
Substrates: 30.2% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
5-L-glutamyl-cis-3-amino-L-proline + acceptor
5-L-glutamyl-acceptor + cis-3-amino-L-proline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-L-alanine + 5-L-glutamyl-L-alanine
L-glutamine + 5-L-glutamyl-L-glutamyl-L-alanine
-
Substrates: shows also hydrolase activity with this substrate
Products: -
Products: -
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5-L-glutamyl-L-His + Gly-Gly
L-His + 5-L-glutamyl-Gly-Gly
-
Substrates: 106% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
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5-L-glutamyl-L-leucine + glycylglycine
L-Leu + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
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5-L-glutamyl-L-lysine + acceptor
L-lysine + 5-L-glutamyl-acceptor
-
Substrates: shows also hydrolase activity with this substrate
Products: -
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5-L-glutamyl-L-Phe + Gly-Gly
L-Phe + 5-L-glutamyl-Gly-Gly
-
Substrates: 103% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
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5-L-glutamyl-L-Tyr + Gly-Gly
L-Tyr + 5-L-glutamyl-Gly-Gly
-
Substrates: 94.7% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
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5-L-glutamylaniline + 5-L-glutamylaniline
aniline + 5-L-glutamyl-5-L-glutamylaniline
-
Substrates: -
Products: -
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5-L-glutamylaniline + H2O
aniline + L-glutamic acid
-
Substrates: -
Products: -
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5-L-glutamylaniline + S-methyl-L-cysteine
aniline + 5-L-glutamyl-S-methyl-L-cysteine
-
Substrates: -
Products: -
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a (5-L-glutamyl)-peptide + L-cysteinylglycine
?
-
Substrates: -
Products: -
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D-gamma-glutamyl-S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + glycylglycine
S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + L-Glu-Gly-Gly
-
Substrates: -
Products: -
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D-Gln + Ala
D-Glu-Ala + NH3
-
Substrates: 6.2% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + Cys
D-Glu-Cys + NH3
-
Substrates: 19.3% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + ethylamine
?
Substrates: 1.3% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
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D-Gln + Glu
D-Glu-Glu + NH3
-
Substrates: 8.1% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + Gly
D-Glu-Gly + NH3
-
Substrates: 20.1% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + His
D-Glu-His + NH3
-
Substrates: 116% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + L-Val
D-Glu-Val + NH3
-
Substrates: 8.1% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + Met
D-Glu-Met + NH3
-
Substrates: 352% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + Phe
D-Glu-Phe + NH3
-
Substrates: 144% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + taurine
D-Glu-taurine + NH3
-
Substrates: 422% of the activity with D-Gln and Gly-Gly
Products: -
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D-Gln + Trp
D-Glu-Trp + NH3
-
Substrates: 558% of the activity with D-Gln and Gly-Gly
Products: -
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diclofenac-S-acyl-glutathione + Gly
diclofenac-S-acyl-cysteinylglycine + ?
-
Substrates: -
Products: -
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gamma-Glu-Cys + Gly-Gly
Cys + 5-L-glutamyl-Gly-Gly
-
Substrates: -
Products: -
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gamma-Glu-L-Tyr + ethylamine
?
Substrates: 5.2% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
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gamma-Glu-Leu + ethylamine
?
Substrates: 3.4% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
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gamma-glutamyl-7-amido-4-methylcoumarin + H2O
L-glutamine + 7-amido-4-methylcoumarin
Substrates: -
Products: -
Products: -
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gamma-glutamyl-D,L-phenylthioglycylglycine + acceptor
gamma-glutamyl-acceptor + alpha-phenylthioglycyl-glycine
-
Substrates: -
Products: -
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gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + glycylglycine
(5R,20S)-5,20-diamino-4,8,17,21-tetraoxo-7,18-dithia-3,9,16,22-tetraazatetracosane-1,24-dioic acid + L-Glu-Gly-Gly
-
Substrates: -
Products: -
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gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine
L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
glutamic acid gamma methyl ester + ethylamine
theanine + ethanol
-
Substrates: -
Products: -
Products: -
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glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
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glutathione + 1-aminocyclopropane-1-carboxylic acid
L-cysteinylglycine + 5-L-glutamyl-1-aminocyclopropane-1-carboxylic acid
-
Substrates: isoforms I and II
Products: -
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glutathione + amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: Ggt1 initiates enzymatic breakdown of GSH by cleavage of the gamma-glutamyl bond and release of cysteinylglycine. Second, the thiol group of the released dipeptide reduces ferric to ferrous iron. A combination of kinetic properties of both reactions results in efficient iron reduction over a broad pH range
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glutathione + daunomycin
L-cysteinylglycine + 5-L-glutamyl-daunomycin
-
Substrates: detoxification of daunomycin by transpeptidation
Products: -
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glutathione + Gly-Gly
L-cysteinylglycine + 5-L-glutamyl-Gly-Gly
-
Substrates: -
Products: -
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glutathione + leukotriene D
cysteinylglycine + leukotriene C
-
Substrates: -
Products: -
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GS-bimane + Gly-Gly
?
-
Substrates: GS-bimane is the conjugate of GSH and monobromobimane
Products: -
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GSH + ethylamine
?
Substrates: 56.7% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
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GSH + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
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GSSG + ethylamine
?
Substrates: 10.6% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
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GSSG + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
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hexane-1,6-diyldicarbamic acid linked GSH-GSH + glycylglycine
gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + L-Glu-Gly-Gly
-
Substrates: -
Products: -
Products: -
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hypoglycin A + GSH
hypoglycin B + cysteinylglycine
-
Substrates: -
Products: -
Products: -
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L-alpha-methyl-5-glutamyl-L-alpha-aminobutyrate + acceptor
L-alpha-methyl-5-glutamyl acceptor + L-2-aminobutyrate
L-gamma-glutamyl-3-carboxy-4-nitroanilide + H2O
3-carboxy-4-nitroaniline + L-glutamate
Substrates: assay at pH 8
Products: -
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L-gamma-glutamyl-4-nitroanilide + ethylamine
4-nitroaniline + 5-L-glutamyl-ethylamine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + glycine methylester
4-nitroaniline + 5-L-glutamyl-glycyl methylester
Substrates: very low activity
Products: -
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L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
L-gamma-glutamyl-4-nitroanilide + glycylglycine methylester
4-nitroaniline + 5-L-glutamyl-glycylglycine methylester
Substrates: low activity
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
Substrates: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
Substrates: low activity
Products: -
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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-proline
4-nitroaniline + 5-L-glutamyl-L-proline
Substrates: very low activity
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
L-gamma-glutamyl-S-[(6-aminohexyl)carbamoyl]-D-cysteinylglycine + glycylglycine
[[(2R)-2-amino-3-[[(6-aminohexyl)carbamoyl]sulfanyl]propanoyl]amino]acetic acid + L-Glu-Gly-Gly
-
Substrates: -
Products: -
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L-Gln + ethylamine
?
Substrates: 18.8% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
Products: -
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L-Gln + Gly-Gly
NH3 + 5-L-glutamyl-Gly-Gly
-
Substrates: 78.1% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
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L-Glu-gamma-3-carboxy-4-hydroxy-anilide + ethylamine
?
Substrates: 3.9% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
Products: -
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L-Glu-gamma-monohydroxamate + ethylamine
?
Substrates: 0.5% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
Products: -
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L-glutamine + glycylglycine
NH3 + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
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L-glutamine + L-leucine
gamma-glutamyl-L-leucine + NH3
-
Substrates: optimum conditions for a biocatalytic synthesis of gamma-Glu-Leu are determined to be 200 mM glutamine, 200 mM leucine, 50 mM Tris-HCl, pH 9.0, and enzyme BlGGT at a working concentration of 2.0 U/ml. Upon a 5-h incubation of the reaction mixture at 50°C, the product yield reaches approximately 52%. The preparative synthesis of gamma-Glu-Leu by BlGGT is done under optimal conditions at millimolar scale level
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L-glutamyl-gamma-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + L-glutamyl-glycylglycine
-
Substrates: -
Products: -
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L-glutamylhydrazine + methylamine
gamma-L-glutamylmethylamide + hydrazine
Substrates: recombinant enzyme, method optimmization and evaluation, overview
Products: -
Products: -
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leukotriene C4 + glycylglycine
leukotriene D4 + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
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S-(4-nitro-benzyl)glutathione + glycylglycine
?
Substrates: -
Products: -
Products: -
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S-methyl-glutathione + ethylamine
?
Substrates: 1.8% of the activity with 5-L-glutamyl-4-nitroanilide
Products: -
Products: -
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S-methylglutathione + acceptor
S-methyl-L-cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: shows also hydrolase activity with this substrate
Products: -
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S-nitroso-glutathione + glycyl-glycine
S-nitroso-cysteinylglycine + gamma-L-glutamyl-glycyl-glycine
-
Substrates: -
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best acceptors: free amino acids
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best acceptors: free amino acids
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best donor: glutamate
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best acceptors: free amino acids
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best donor: glutamate
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best acceptors: free amino acids
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donors are Glu, alpha-L-Glu-L-Ala
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: dipeptides are better acceptors than free amino acids
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best donor: glutamate
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: isozyme A prefers basic and aromatic amino acids as acceptors
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
487903, 487956, 487897, 487898, 487901, 487902, 487904, 487906, 487909, 487933, 487935, 487937, 487939, 487940, 487941, 487961, 487963
Substrates: -
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor binding site reacts with L- and to a lesser extent D-enantiomer
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-3-sulfonic-4-nitroanilide
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: GSH S-substituted derivatives
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-naphthylamide
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: strict L-stereospecificity of 5-Glu-acceptor site
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: S-acetophenoneglutathione
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: S-acetylglutathione
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: best acceptors: free amino acids
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: stereospecificity
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
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(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor binding site reacts with L- and to a lesser extent D-enantiomer
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: strict L-stereospecificity of 5-Glu-acceptor site
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donors are Glu, alpha-L-Glu-L-Ala
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: stereospecificity
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor binding site reacts with L- and to a lesser extent D-enantiomer
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: strict L-stereospecificity of 5-Glu-acceptor site
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
Oncornavirus
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-3-sulfonic-4-nitroanilide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: GSH S-substituted derivatives
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-naphthylamide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: stereospecificity
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: stereospecificity
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: imino acids are no substrates
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
487899, 487905, 487912, 487914, 487915, 487917, 487918, 487919, 487920, 487957, 487958, 487960, 487964, 487969
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: poor substrates are beta-substituted amino acids
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor binding site reacts with L- and to a lesser extent D-enantiomer
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-3-sulfonic-4-nitroanilide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: GSH S-substituted derivatives
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
Products: -
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors are amino acids or dipeptides
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donors: ophthalmic acid, poly-5-Glu-derivatives, L-5-Glu-7-amino-4-methylcoumarin
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-naphthylamide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: strict L-stereospecificity of 5-Glu-acceptor site
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: leukotriene C
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: S-acetophenoneglutathione
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: GSH S-substituted derivatives
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is 5-L-Glu-4-nitroanilide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: autotranspeptidation with another donor molecule as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reaction: hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione S-conjugates
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: alpha-aminoisobutyric acid is no donor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor specificity, overview
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: acceptors: L-methionine, L-tryptophan, L-alanine, 1-aminocyclopropane-1-carboxylic acid, glutathione
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donors: 5-ethyl-Glu and beta-benzyl-Glu, hydrolyzed by pig enzyme
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donors: ophthalmic acid, poly-5-Glu-derivatives, L-5-Glu-7-amino-4-methylcoumarin
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: 5-L-Glu-naphthylamide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: leukotriene C
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: Glu-donor is GSH
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: glutathione disulfide
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: donor: S-acetophenoneglutathione
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: L-cysteine is no substrate
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: the enzyme plays an important role on the growth of Helicobacter pylori. Higher GGT activity provides an advantage to the growth of Helicobacter pylori in vitro
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: the enzyme plays an important role on the growth of Helicobacter pylori. Higher GGT activity provides an advantage to the growth of Helicobacter pylori in vitro
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: quantitative measurement of release of 4-nitroaniline
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
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Substrates: the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-p-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: quantitative measurement of release of 4-nitroaniline
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: 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
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: -
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: 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
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(gamma-L-glutamyl)-4-nitroanilide + glycylglycine
4-nitroaniline + gamma-glutamylglycylglycine
Substrates: -
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5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
Substrates: -
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5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
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Substrates: -
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5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
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Substrates: -
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5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
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Substrates: -
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5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine
5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine
5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-2-naphthylamide + glycylglycine
5-L-glutamyl-glycylglycine + 2-naphthylamine
Substrates: -
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5-L-glutamyl-2-naphthylamide + glycylglycine
5-L-glutamyl-glycylglycine + 2-naphthylamine
Substrates: -
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5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
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Substrates: -
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5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
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Substrates: -
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5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
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Substrates: -
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5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate
4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine
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Substrates: beta-enantiomer of aminobutyrate
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5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate
4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine
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Substrates: alpha-enantiomer of aminobutyrate
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5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate
4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine
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Substrates: alpha-enantiomer of aminobutyrate
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5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid
4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid
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Substrates: 161% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid
4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid
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Substrates: 176% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid
4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid
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Substrates: 8% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid
4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid
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Substrates: 8% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: autotranspeptidase
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: autotranspeptidation, L- or, to a lesser extent, D-enantiomer
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 113.6% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 113.6% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 124% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 169% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 44% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Arg
4-nitroaniline + 5-L-glutamyl-Arg
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Substrates: 44% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
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Substrates: 4.5% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
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Substrates: 144% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
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Substrates: 140% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
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Substrates: 13% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Asp
4-nitroaniline + 5-L-glutamyl-Asp
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Substrates: 13% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + citrulline
4-nitroaniline + 5-L-glutamyl-citrulline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + citrulline
4-nitroaniline + 5-L-glutamyl-citrulline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
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Substrates: 46.9% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
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Substrates: 7% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
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Substrates: 7% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
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Substrates: 7% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Cys
4-nitroaniline + 5-L-glutamyl-Cys
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Substrates: 7% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + Cys-Gly
4-nitroaniline + 5-L-glutamyl-Cys-Gly
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Substrates: 16% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Cys-Gly
4-nitroaniline + 5-L-glutamyl-Cys-Gly
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Substrates: 15% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Cys-Gly
4-nitroaniline + 5-L-glutamyl-Cys-Gly
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Substrates: 36% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Cys-Gly
4-nitroaniline + 5-L-glutamyl-Cys-Gly
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Substrates: 36% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + ethylamine
theanine + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + ethylamine
theanine + 4-nitroaniline
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
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Substrates: 4.4% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
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Substrates: 13% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
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Substrates: 11% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
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Substrates: 13% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Glu
4-nitroaniline + 5-L-glutamyl-Glu
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Substrates: 13% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 37.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 33.2% of the activity with Gly-Gly
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 48% of the activity with Gly-Gly, enzyme form GGT I
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 43% of the activity with Gly-Gly, enzyme form GGT II
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 14% of the activity with Gly-Gly, enzyme form GGT A
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5-L-glutamyl-4-nitroanilide + Gly
4-nitroaniline + 5-L-glutamyl-Gly
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Substrates: 14% of the activity with Gly-Gly, enzyme form GGT B
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: 19% activity the rate of the reaction with glycylglycine, glycyl-tri- to hexapeptides can act as acceptors
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
Oncornavirus
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Substrates: 19% viral enzyme
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: 19% activity the rate of the reaction with glycylglycine, glycyl-tri- to hexapeptides can act as acceptors
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
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Substrates: glutamyl transfer at 17.2%
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: best acceptor
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
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Substrates: -
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5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: GGT activity
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
Oncornavirus
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: 4-nitroaniline is cytotoxic
Products: 4-nitroaniline is cytotoxic
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
Substrates: substrate for isoform GGT1
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + Glu
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + Glu
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + Glu
-
Substrates: ping-pong mechanism
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
Substrates: hydrolase reaction
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
Substrates: hydrolase reaction
Products: -
Products: -
ir
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
-
Substrates: hydrolase reaction
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + His
4-nitroaniline + 5-L-glutamyl-His
-
Substrates: 82.9% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + His
4-nitroaniline + 5-L-glutamyl-His
-
Substrates: 82.9% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Ile
4-nitroaniline + 5-L-glutamyl-Ile
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Ile
4-nitroaniline + 5-L-glutamyl-Ile
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Ile
4-nitroaniline + 5-L-glutamyl-Ile
-
Substrates: 20.7% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: L-Ala or D-Ala
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
Substrates: glutamyl transfer at 32% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
Substrates: glutamyl transfer at 30% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
Substrates: glutamyl transfer at 8.6% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteinylglycine
4-nitroaniline + glutathione
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteinylglycine
4-nitroaniline + glutathione
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteinylglycine
4-nitroaniline + glutathione
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cysteinylglycine
4-nitroaniline + glutathione
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: best acceptor, low molecular weight enzyme variant
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: best acceptor, high molecular weight enzyme variant
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: glutamyl transfer at 43% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: L-methionine and L-glutamine are best acceptors
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
Substrates: glutamyl transfer at 8.6% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-hydroxyproline
4-nitroaniline + 5-L-glutamyl-L-hydroxyproline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-hydroxyproline
4-nitroaniline + 5-L-glutamyl-L-hydroxyproline
-
Substrates: glutamyl transfer at 17% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
Substrates: glutamyl transfer at 17% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
Substrates: glutamyl transfer at 20% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
Substrates: glutamyl transfer at 26% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Met
4-nitroaniline + 5-L-glutamyl-L-Met
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-Met
4-nitroaniline + 5-L-glutamyl-L-Met
-
Substrates: 50.6% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: best acceptor
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: 44% activity, viral enzyme
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Oncornavirus
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: 44% the rate of the reaction with glycylglycine, L-Met or D-Met
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: glutamyl transfer at 39% the rate with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: L-methionine and glutamine are best acceptors
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
Substrates: glutamyl transfer at 26% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-proline
4-nitroaniline + 5-L-glutamyl-L-proline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-proline
4-nitroaniline + 5-L-glutamyl-L-proline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-proline
4-nitroaniline + 5-L-glutamyl-L-proline
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
Substrates: glutamyl transfer at 28% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
-
Substrates: glutamyl transfer at 20% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
Substrates: glutamyl transfer at 20% the rate of the reaction with glycylglycine
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Lys
4-nitroaniline + 5-L-glutamyl-Lys
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Lys
4-nitroaniline + 5-L-glutamyl-Lys
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Lys
4-nitroaniline + 5-L-glutamyl-Lys
-
Substrates: 79.4% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Lys
4-nitroaniline + 5-L-glutamyl-Lys
-
Substrates: 79.4% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 48.8% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 48.8% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 141% of the activity with Gly-Gly, enzyme form GGT I
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 137% of the activity with Gly-Gly, enzyme form GGT II
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 43% of the activity with Gly-Gly, enzyme form GGT A
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Met
4-nitroaniline + 5-L-glutamyl-Met
-
Substrates: 43% of the activity with Gly-Gly, enzyme form GGT B
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Thr
4-nitroaniline + 5-L-glutamyl-Thr
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Thr
4-nitroaniline + 5-L-glutamyl-Thr
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-4-nitroanilide + Thr
4-nitroaniline + 5-L-glutamyl-Thr
-
Substrates: 27.3% of the activity with Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
Substrates: acceptors are amino acids and peptides, overview
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
Substrates: glycylglycine is best acceptor
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
Substrates: acceptors are amino acids and peptides, overview
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
5-L-glutamyl-L-Met + Gly-Gly
L-Met + 5-L-glutamyl-Gly-Gly
-
Substrates: 114% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-L-Met + Gly-Gly
L-Met + 5-L-glutamyl-Gly-Gly
-
Substrates: 114% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-L-Trp + Gly-Gly
L-Trp + 5-L-glutamyl-Gly-Gly
-
Substrates: 127% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-L-Trp + Gly-Gly
L-Trp + 5-L-glutamyl-Gly-Gly
-
Substrates: 127% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-L-Val + Gly-Gly
L-Val + 5-L-glutamyl-Gly-Gly
-
Substrates: 113% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
5-L-glutamyl-L-Val + Gly-Gly
L-Val + 5-L-glutamyl-Gly-Gly
-
Substrates: 113% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
7-(N-gamma-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + ?
-
Substrates: -
Products: -
Products: -
?
7-(N-gamma-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + ?
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Bacillus amyloliquefaciens SMB469
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
A0A415J2H1
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
gamma-glutamyl-4-nitroanilide + hydroxamate
4-nitroaniline + gamma-L-glutamylhydroxamate
Substrates: -
Products: -
Products: -
?
gamma-glutamyl-4-nitroanilide + hydroxamate
4-nitroaniline + gamma-L-glutamylhydroxamate
Substrates: -
Products: -
Products: -
?
gamma-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + gamma-L-glutamyl-Gly-Gly
Substrates: the enzyme also catalyzes the hydrolase reaction: gamma-L-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline
Products: -
Products: -
?
gamma-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + gamma-L-glutamyl-Gly-Gly
Picrophilus oshimae DSM 9790
Substrates: the enzyme also catalyzes the hydrolase reaction: gamma-L-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline
Products: -
Products: -
?
gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine
L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
-
Substrates: GSH
Products: -
Products: -
?
gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine
L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
-
Substrates: GSH
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: acceptor: amino acids
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: acceptor: hydroxylamine
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: acceptor: amino acids
Products: -
Products: -
r
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: acceptor: amino acids
Products: -
Products: -
r
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
Oncornavirus
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
r
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: acceptor: amino acids
Products: -
Products: -
r
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: best donor
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: -
Products: -
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
Substrates: best donor
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
ir
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
Substrates: initial step of glutathione degradation
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in polyglutamic acid synthesis
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: ectoenzyme protects the epithelial cells against oxidants by replenishing intracellular glutathione
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: -
Products: -
Products: -
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
Products: -
Products: -
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
r
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
r
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
r
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
r
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
Substrates: autotranspeptidation
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: L-glutamate is transferred to H2O, c.f. EC 3.4.19.9
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
ir
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
ir
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
ir
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
ir
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: hydrolase reaction, concurrent to (auto-)transpeptidation
Products: -
Products: -
?
glutathione + L-cysteinylglycine
L-cysteinylglycine + glutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + L-cysteinylglycine
L-cysteinylglycine + glutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + L-cysteinylglycine
L-cysteinylglycine + glutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + L-cysteinylglycine
L-cysteinylglycine + glutathione
-
Substrates: -
Products: -
Products: -
?
glutathione disulfide + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
Substrates: GSSG
Products: -
Products: -
?
glutathione disulfide + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
Substrates: GSSG
Products: -
Products: -
?
GSH + Gly-Gly
?
-
Substrates: 98.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
GSH + Gly-Gly
?
-
Substrates: 98.8% of the transpeptidase activity with 5-L-glutamyl-4-nitroanilide and Gly-Gly
Products: -
Products: -
?
L-alpha-methyl-5-glutamyl-L-alpha-aminobutyrate + acceptor
L-alpha-methyl-5-glutamyl acceptor + L-2-aminobutyrate
-
Substrates: acceptor specificity, overview
Products: -
Products: -
?
L-alpha-methyl-5-glutamyl-L-alpha-aminobutyrate + acceptor
L-alpha-methyl-5-glutamyl acceptor + L-2-aminobutyrate
-
Substrates: hydrolysis in the absence of acceptor, methyl group at alpha-C prevents autotranspeptidation
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
Substrates: very low activity
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Bacillus amyloliquefaciens SMB469
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Q62WE3
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
A0A415J2H1
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Q62WE3
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: best substrate
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
-
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: low activity
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
Substrates: -
Products: -
Products: -
?
L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Bacillus amyloliquefaciens SMB469
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
A0A415J2H1
Substrates: the synthetic substrate L-gamma-Glu-4-nitroanilide is used as a gamma-glutamyl donor, biocatalytic synthesis of gamma-Glu-Phe, reaction via formation of a gamma-glutamyl-enzyme intermediate. The intermediate can then react with water to release glutamate in a hydrolysis reaction or with amino acids or peptides to produce other gamma-glutamyl compounds in a transpeptidation reaction. Product analysis by thin layer chromatography
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
A0A415J2H1
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
Substrates: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Bacillus amyloliquefaciens SMB469
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Bacillus amyloliquefaciens SMB469
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-tryptophan
4-nitroaniline + 5-L-glutamyl-L-tryptophan
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
Products: -
Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
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Products: -
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L-gamma-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
Substrates: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
Substrates: L-Glu-4-nitroanilide is a suicide substrate
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
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Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
Products: -
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L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
Substrates: -
Products: -
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L-Glu-gamma-monomethyl ester + ethylamine
?
Substrates: 4.3% of the activity with 5-L-glutamyl-4-nitroanilide
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L-Glu-gamma-monomethyl ester + ethylamine
?
Substrates: 1.9% of the activity with 5-L-glutamyl-4-nitroanilide
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L-glutamine + ethylamine
NH3 + gamma-glutamylethylamine
-
Substrates: GGT transfers the gamma-glutamyl moiety from L-Gln to ethylamine to form the product gamma-glutamylethylamine (L-theanine), product identification by mass spectrometry, optimization of reaction conditions, overview
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L-glutamine + ethylamine
NH3 + gamma-glutamylethylamine
-
Substrates: GGT transfers the gamma-glutamyl moiety from L-Gln to ethylamine to form the product gamma-glutamylethylamine (L-theanine), product identification by mass spectrometry, optimization of reaction conditions, overview
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L-glutamine + ethylamine
NH3 + gamma-glutamylethylamine
Substrates: formation of gamma-glutamylethylamine (L-theanine)
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L-glutamine + ethylamine
NH3 + gamma-glutamylethylamine
-
Substrates: formation of gamma-glutamylethylamine (L-theanine)
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L-glutamine + ethylamine
NH3 + gamma-glutamylethylamine
Substrates: formation of gamma-glutamylethylamine (L-theanine)
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lentinic acid + amino acid
desglutamyl lentinic acid + 5-L-glutamylamino acid
-
Substrates: best acceptor is S-alkylcysteine sulfoxide
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lentinic acid + amino acid
desglutamyl lentinic acid + 5-L-glutamylamino acid
-
Substrates: function in aroma evolution from lentinic acid
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leukotriene C4 + acceptor
leukotriene D4 + glutamyl-acceptor
-
Substrates: i.e. glutathione containing derivative of arachidonic acid, acceptors are H2O, amino acids or dipeptides
Products: -
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leukotriene C4 + acceptor
leukotriene D4 + glutamyl-acceptor
-
Substrates: -
Products: -
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leukotriene C4 + acceptor
leukotriene D4 + glutamyl-acceptor
-
Substrates: i.e. glutathione containing derivative of arachidonic acid, acceptors are H2O, amino acids or dipeptides
Products: -
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: 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
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: successive hydrolysis from the amino-terminal end
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: 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
Products: -
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: successive hydrolysis from the amino-terminal end
Products: -
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additional information
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-
-
Substrates: the enzyme is unlikely to function as a gamma-glutamyl hydrolase in vivo. It is possible that it could catalyze transpeptidation of precursors such as S-methyl glutathione during S-alkyl cysteine sulfoxide biosynthesis
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additional information
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-
Substrates: the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline
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additional information
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-
-
Substrates: the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline
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additional information
?
-
Substrates: the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline
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additional information
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-
-
Substrates: the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline
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additional information
?
-
Substrates: gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
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additional information
?
-
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Substrates: gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
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additional information
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Substrates: GGT3 catalyzes the obligate initial step in GSH conjugate metabolism, and has an important role in protecting plants from some xenobiotic chemicals
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additional information
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-
O65652
Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
?
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Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
?
-
Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
?
-
Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
?
-
-
Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
?
-
-
Substrates: in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
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additional information
?
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Substrates: in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
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additional information
?
-
-
Substrates: the enzyme utilizes Gln, glutathione, and less efficiently oxidized glutathione as gamma-glutamyl donors (beside of gamma-glutamyl-4-nitroanilide) and utilizes amino-acids and peptides (including Glu, Cys, Met, Gly-Gly and Cys-Gly), but not hydroxylamine, as gamma-glutamyl acceptors
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additional information
?
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline, poor activity with glycine
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additional information
?
-
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline, poor activity with glycine
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additional information
?
-
Substrates: the enzyme must undergo autocatalytic processing before it has enzymatic activity
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additional information
?
-
-
Substrates: the enzyme must undergo autocatalytic processing before it has enzymatic activity
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additional information
?
-
-
Substrates: mass spectrometric and NMR analysis of reaction products
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additional information
?
-
Substrates: both free and immobilized enzymes specifically convert glutamine to glutamic acid in a mixture of amino acids
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additional information
?
-
Substrates: GGT is known to catalyze three types of reactions: (a) transpeptidation- when the acceptor is an NH2- group containing compound to which GGT can transfer the gamma-glutamyl moiety, (b) hydrolysis- when gamma-glutamyl moiety is transferred to a water molecule and glutamic acid is released as a product and (c) auto-transpeptidation- when the free NH2- group of a donor acts as an acceptor itself. Amino acid acceptor substrate specificity, overview
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additional information
?
-
-
Substrates: GGT is known to catalyze three types of reactions: (a) transpeptidation- when the acceptor is an NH2- group containing compound to which GGT can transfer the gamma-glutamyl moiety, (b) hydrolysis- when gamma-glutamyl moiety is transferred to a water molecule and glutamic acid is released as a product and (c) auto-transpeptidation- when the free NH2- group of a donor acts as an acceptor itself. Amino acid acceptor substrate specificity, overview
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additional information
?
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine
Products: -
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additional information
?
-
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with glycine
Products: -
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additional information
?
-
A0A415J2H1
Substrates: the recombinantly expressed BlGGT confers the ability to catalyze the synthesis of gamma-L-glutamyl-S-allyl-L-cysteine, gamma-glutamyl-L-phenylalanine, and gamma-glutamyl-L-leucine. The transpeptidation activity of recombinant enzyme BlGGT and mutants N450D and N450Q is assayed in triplicate with L-gamma-glutamyl-4-nitroanilide and Gly-Gly as the substrates. Preparative biocatalytic synthesis of L-theanine from a reaction mixture of L-Gln, ethanolamine, and borate buffer, pH 10.5, 37°C. Use of L-theanine as one kind of gamma-glutamyl donor for the transpeptidation action by the enzyme. The L-theanine production by wild-type BlGGT, mutant N450D, and mutant N450Q at pH 10.5 results in the individual yields of 56, 88, and 61%, respectively
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additional information
?
-
Substrates: the enzyme must undergo autocatalytic processing before it has enzymatic activity
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additional information
?
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine
Products: -
Products: -
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additional information
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-
-
Substrates: substrate specificity for gamma-glutamyl acceptors with L-gamma-glutamyl-4-nitroanilide as gamma-glutamyl donor, overview. No activity with L-proline and glycine
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?
additional information
?
-
-
Substrates: quantitation of gamma-glutamyl dipeptides by means of HPLC-MS/MS: quantification of gamma-Glu-Gly, gamma-Glu-Ala, gamma-Glu-Val, gamma-Glu-Thr, gamma-Glu-Asp, gamma-Glu-Lys, gamma-Glu-Glu, gamma-Glu-Trp, gamma-Glu-Leu, gamma-Glu-Ile, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-His, gamma-Glu-Phe, and gamma-Glu-Tyr in cheese samples after 13, 24, and 30 months of ripening (PC-13, PC-24, and PC-30), respectively, and in raw and heated cow milk, overview. gamma-Glu-Ala-[13C3] is used as the internal standard. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
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additional information
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-
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Substrates: although gamma-glutamyltransferase activity of Campylobacter jejuni is not required for initial colonization of 1-day-old chicks, the enzyme is required for persistant colonization of the avian gut
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additional information
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Substrates: L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13
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additional information
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-
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Substrates: L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13
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additional information
?
-
-
Substrates: enzyme does not show any transpeptidase activity
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?
additional information
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-
-
Substrates: GGT is sufficient for inhibition of T-cell proliferation by Helicobacter pylori because the inhibitory effect is completely abolished in GGT-deficient mutants of the bacteria
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additional information
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-
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Substrates: S-thiolating activity of membrane gamma-glutamyltransferase, the formation of CG-containing mixed disulfides may have a regulatory function, similar to the case of S-glutathionylation
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?
additional information
?
-
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Substrates: development of a methods for the indirect evaluation of donor substrate affinity and stereospecificity
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additional information
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-
-
Substrates: intracellular effects of the soluble enzyme: supply of precursor amino acids for GSH resynthesis, modulation of protein S-thiolation status (S-glutathionylation, S-cysteyl-glycylation), redox effects on propliferative/apoptotic balance. Extracellular effects: consumption of GSH and generation of cysteinyl-glycine, reduction of metal cations (e.g. iron, including transferrin- and ferritin-bound iron) and stimulation of metal redox-cycling, thiol oxidation and modulation of S-thiolation status of extracellular proteins, promotion of oxidative processes (e.g. lipid peroxidation), catabolism of S-nitroso-glutathione, metabolism of leukotriene C4 to leukotriene D4
Products: -
Products: -
?
additional information
?
-
-
Substrates: contribution of GGT in the mechanisms of drug resistance
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?
additional information
?
-
Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
Products: -
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additional information
?
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Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
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additional information
?
-
-
Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
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?
additional information
?
-
-
Substrates: using human BEAS-2B cells transfected with GGT cDNA, as well as wild-type cells exposed to ELF-like GGT concentrations, shows that much higher (5-10 fold) levels of ascorbic acid accumulates in the presence of GSH and active gamma-glutamyltransferase
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additional information
?
-
Substrates: in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione
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additional information
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-
-
Substrates: in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione
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?
additional information
?
-
-
Substrates: isoform GGT5 does not cleave 5-L-glutamyl-4-nitroanilide and gamma-glutamyl leucine
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?
additional information
?
-
Substrates: isoform GGT5 does not cleave 5-L-glutamyl-4-nitroanilide and gamma-glutamyl leucine
Products: -
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?
additional information
?
-
Substrates: GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation)
Products: -
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additional information
?
-
-
Substrates: GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation)
Products: -
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?
additional information
?
-
Substrates: GGT not only catalyzes the transfer of gamma-glutamyl group of gamma-Glu-PNA to acceptors, but also hydrolyzes the gamma-glutamyl bond of gamma-Glu-PNA to give glutamate and 4-nitroaniline (EC 3.4.19.13)
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?
additional information
?
-
-
Substrates: GGT not only catalyzes the transfer of gamma-glutamyl group of gamma-Glu-PNA to acceptors, but also hydrolyzes the gamma-glutamyl bond of gamma-Glu-PNA to give glutamate and 4-nitroaniline (EC 3.4.19.13)
Products: -
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?
additional information
?
-
-
Substrates: the ggh gene is a pseudogene that is transcriptionally active but phenotypically silent
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?
additional information
?
-
-
Substrates: the donor substrate determines the acceptor specificity
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additional information
?
-
Substrates: the gamma-glutamyltranspeptidase (GGT) from Pseudomonas nitroreducens strain IFO12694 (PnGGT) has a unique preference for primary amines as gamma-glutamyl acceptors over standard L-amino acids and peptides, detection of the structural basis of PnGGT's hydrolysis and transpeptidation reactions, overview. Key interactions between three residues Trp385, Phe417, and Trp525 distinguish PnGGT from other GGTs, the aromatic side chains of Trp385, Phe417, and Trp525 are involved in the recognition of acceptor substrates. Local structures of substrate binding sites
Products: -
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additional information
?
-
-
Substrates: the gamma-glutamyltranspeptidase (GGT) from Pseudomonas nitroreducens strain IFO12694 (PnGGT) has a unique preference for primary amines as gamma-glutamyl acceptors over standard L-amino acids and peptides, detection of the structural basis of PnGGT's hydrolysis and transpeptidation reactions, overview. Key interactions between three residues Trp385, Phe417, and Trp525 distinguish PnGGT from other GGTs, the aromatic side chains of Trp385, Phe417, and Trp525 are involved in the recognition of acceptor substrates. Local structures of substrate binding sites
Products: -
Products: -
?
additional information
?
-
Substrates: the gamma-glutamyltranspeptidase (GGT) from Pseudomonas nitroreducens strain IFO12694 (PnGGT) has a unique preference for primary amines as gamma-glutamyl acceptors over standard L-amino acids and peptides, detection of the structural basis of PnGGT's hydrolysis and transpeptidation reactions, overview. Key interactions between three residues Trp385, Phe417, and Trp525 distinguish PnGGT from other GGTs, the aromatic side chains of Trp385, Phe417, and Trp525 are involved in the recognition of acceptor substrates. Local structures of substrate binding sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: the gamma-glutamyltranspeptidase (GGT) from Pseudomonas nitroreducens strain IFO12694 (PnGGT) has a unique preference for primary amines as gamma-glutamyl acceptors over standard L-amino acids and peptides, detection of the structural basis of PnGGT's hydrolysis and transpeptidation reactions, overview. Key interactions between three residues Trp385, Phe417, and Trp525 distinguish PnGGT from other GGTs, the aromatic side chains of Trp385, Phe417, and Trp525 are involved in the recognition of acceptor substrates. Local structures of substrate binding sites
Products: -
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?
additional information
?
-
-
Substrates: ester and amide derivatives of L-Glu-4-nitroanilide are no substrates, overview
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?
additional information
?
-
-
Substrates: activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
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additional information
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-
-
Substrates: the enzyme is implicated in cellular detoxification, the biosynthesis of leukotrienes and control of the physiological concentration of glutathione. It also plays important roles in Parkinsons disease, diabetes, apoptosis inhibition and cancer drug resistance
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additional information
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-
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Substrates: the mechanism of the deacylation step of GGT-mediated transpeptidation using L-methionine derivatives as acceptor substrates is consistent with the observed Bronsted linear free energy relationship, pH-rate profile, and solvent kinetic isotope effects. It is proposed that in the rate-limiting step these acceptor substrates carry out a nucleophilic attack on the acyl-enzyme intermediate, with simultaneous deprotonation of the nucleophilic amino group, to form a tetrahedral intermediate. At the transition state, nucleophilic attack is more advanced than deprotonation of the amine, leading to significant development of positive charge on the nucleophilic nitrogen
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additional information
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-
-
Substrates: in vivo expreriments in rat kidney, liver, heart, or brain. gamma-Glu-[1-13C]Gly is hyperpolarized using the TEMPOL nitroxyl radical (4-hydroxy-2,2,6,6-tetramethylpiperidine-N-oxyl), and the resulting 13C polarization at the time of injection is 9%, overview. A spectral peak corresponding to [1-13C]Gly is readily detected in the kidney
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additional information
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-
-
Substrates: enzyme GGT catalyzes the cleavage of the gamma-peptide bond between the glutamyl and cysteinyl residues of GSH and related molecules, either hydrolyzing the bond or ligating the free alpha-amine of an amino acid or peptide, cf. glutathione hydrolase, EC 3.4.19.13. Development of a HP-GGT probe for hyperpolarized (HP) MR measurements for dissolution dynamic nuclear polarization (DNP), a versatile method to hyperpolarize nuclear spins. It can temporarily increase the signal from NMR-active nuclei by as much as 4 or 5 orders of magnitude, which has enabled the detection of metabolic transformations in real-time with high sensitivity using NMR spectroscopy and imaging. Design and preparation of an HP molecular probe targeting GGT activity, gamma-Glu-[1-13C]Gly. gamma-Glu-[1-13C]Gly fulfills the requirements of an HP molecular probe, and the probe can monitor real-time GGT activity in vivo. Detection of enzyme bound-gamma-Glu and radiolabeled Gly from hydrolysis. Method, overview
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additional information
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-
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Substrates: enzyme activates the yeast cadmium factor 1, responsible for glutathione import into the vacuole
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additional information
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-
Substrates: the GGTII protein is involved in uptake and regeneration of GSH and indirectly in the response against various agents causing oxidative stress
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additional information
?
-
-
Substrates: the GGTII protein is involved in uptake and regeneration of GSH and indirectly in the response against various agents causing oxidative stress
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additional information
?
-
-
Substrates: purified recombinant enzyme added to Porphyromonas gingivalis results in H2S, ammonia and pyruvate release in this bacterium
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additional information
?
-
-
Substrates: L-Glu-4-nitroanilide competes with glutathione and inhibits production of H2S, ammonia and pyruvate
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-D/L-glutamyl-phenylhydrazine + acceptor
phenylhydrazine + 5-L-glutamyl-acceptor
-
Substrates: -
Products: product is cytotoxic
Products: product is cytotoxic
ir
glutathione + amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: Ggt1 initiates enzymatic breakdown of GSH by cleavage of the gamma-glutamyl bond and release of cysteinylglycine. Second, the thiol group of the released dipeptide reduces ferric to ferrous iron. A combination of kinetic properties of both reactions results in efficient iron reduction over a broad pH range
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?
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
Substrates: L-Glu-4-nitroanilide is a suicide substrate
Products: -
Products: -
?
lentinic acid + amino acid
desglutamyl lentinic acid + 5-L-glutamylamino acid
-
Substrates: function in aroma evolution from lentinic acid
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
Products: -
Products: -
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
Products: -
Products: -
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: the enzyme plays an important role on the growth of Helicobacter pylori. Higher GGT activity provides an advantage to the growth of Helicobacter pylori in vitro
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
Substrates: the enzyme plays an important role on the growth of Helicobacter pylori. Higher GGT activity provides an advantage to the growth of Helicobacter pylori in vitro
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Bacillus amyloliquefaciens SMB469
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
A0A415J2H1
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
Products: -
Products: -
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
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Substrates: -
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a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Substrates: -
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a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
Substrates: -
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
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glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
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Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
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Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in polyglutamic acid synthesis
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: involved in 5-L-glutamyl cycle of glutathione metabolism
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: ectoenzyme protects the epithelial cells against oxidants by replenishing intracellular glutathione
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
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Substrates: initial step of glutathione degradation
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
Substrates: -
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glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
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Substrates: initial step of glutathione degradation
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: 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
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poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
Substrates: 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
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additional information
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-
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Substrates: the enzyme is unlikely to function as a gamma-glutamyl hydrolase in vivo. It is possible that it could catalyze transpeptidation of precursors such as S-methyl glutathione during S-alkyl cysteine sulfoxide biosynthesis
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additional information
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Substrates: gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
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additional information
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-
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Substrates: gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
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additional information
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Substrates: GGT3 catalyzes the obligate initial step in GSH conjugate metabolism, and has an important role in protecting plants from some xenobiotic chemicals
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additional information
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O65652
Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
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Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
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Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
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Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
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-
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Substrates: the rosettes of GGT1 knockouts show premature senescence after flowering
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additional information
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-
-
Substrates: in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
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additional information
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Substrates: in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
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additional information
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-
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Substrates: quantitation of gamma-glutamyl dipeptides by means of HPLC-MS/MS: quantification of gamma-Glu-Gly, gamma-Glu-Ala, gamma-Glu-Val, gamma-Glu-Thr, gamma-Glu-Asp, gamma-Glu-Lys, gamma-Glu-Glu, gamma-Glu-Trp, gamma-Glu-Leu, gamma-Glu-Ile, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-His, gamma-Glu-Phe, and gamma-Glu-Tyr in cheese samples after 13, 24, and 30 months of ripening (PC-13, PC-24, and PC-30), respectively, and in raw and heated cow milk, overview. gamma-Glu-Ala-[13C3] is used as the internal standard. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
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additional information
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Substrates: although gamma-glutamyltransferase activity of Campylobacter jejuni is not required for initial colonization of 1-day-old chicks, the enzyme is required for persistant colonization of the avian gut
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additional information
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Substrates: GGT is sufficient for inhibition of T-cell proliferation by Helicobacter pylori because the inhibitory effect is completely abolished in GGT-deficient mutants of the bacteria
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additional information
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Substrates: S-thiolating activity of membrane gamma-glutamyltransferase, the formation of CG-containing mixed disulfides may have a regulatory function, similar to the case of S-glutathionylation
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additional information
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Substrates: intracellular effects of the soluble enzyme: supply of precursor amino acids for GSH resynthesis, modulation of protein S-thiolation status (S-glutathionylation, S-cysteyl-glycylation), redox effects on propliferative/apoptotic balance. Extracellular effects: consumption of GSH and generation of cysteinyl-glycine, reduction of metal cations (e.g. iron, including transferrin- and ferritin-bound iron) and stimulation of metal redox-cycling, thiol oxidation and modulation of S-thiolation status of extracellular proteins, promotion of oxidative processes (e.g. lipid peroxidation), catabolism of S-nitroso-glutathione, metabolism of leukotriene C4 to leukotriene D4
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additional information
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-
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Substrates: contribution of GGT in the mechanisms of drug resistance
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additional information
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Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
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additional information
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Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
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additional information
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-
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Substrates: GGT1 hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. It has a critical function in the metabolism of glutathione and in the conversion of the leukotriene LTC4 to LTD4
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additional information
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Substrates: using human BEAS-2B cells transfected with GGT cDNA, as well as wild-type cells exposed to ELF-like GGT concentrations, shows that much higher (5-10 fold) levels of ascorbic acid accumulates in the presence of GSH and active gamma-glutamyltransferase
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additional information
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Substrates: in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione
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additional information
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-
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Substrates: in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione
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additional information
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Substrates: GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation)
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additional information
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Substrates: GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation)
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additional information
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Substrates: the ggh gene is a pseudogene that is transcriptionally active but phenotypically silent
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additional information
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Substrates: activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
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additional information
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Substrates: the enzyme is implicated in cellular detoxification, the biosynthesis of leukotrienes and control of the physiological concentration of glutathione. It also plays important roles in Parkinsons disease, diabetes, apoptosis inhibition and cancer drug resistance
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additional information
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Substrates: in vivo expreriments in rat kidney, liver, heart, or brain. gamma-Glu-[1-13C]Gly is hyperpolarized using the TEMPOL nitroxyl radical (4-hydroxy-2,2,6,6-tetramethylpiperidine-N-oxyl), and the resulting 13C polarization at the time of injection is 9%, overview. A spectral peak corresponding to [1-13C]Gly is readily detected in the kidney
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additional information
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Substrates: enzyme activates the yeast cadmium factor 1, responsible for glutathione import into the vacuole
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additional information
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Substrates: the GGTII protein is involved in uptake and regeneration of GSH and indirectly in the response against various agents causing oxidative stress
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additional information
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Substrates: the GGTII protein is involved in uptake and regeneration of GSH and indirectly in the response against various agents causing oxidative stress
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additional information
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Substrates: purified recombinant enzyme added to Porphyromonas gingivalis results in H2S, ammonia and pyruvate release in this bacterium
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additional information
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Substrates: L-Glu-4-nitroanilide competes with glutathione and inhibits production of H2S, ammonia and pyruvate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
K+
Li+
Mg2+
Mn2+
Na+
additional information
additional information
no significant effect by Mn2+, Zn2+, Ca2+, and Mg2+ at 2 mM
additional information
-
no significant effect by Mn2+, Zn2+, Ca2+, and Mg2+ at 2 mM
additional information
no significant effect by Ca2+ and Zn2+ at 2 mM
additional information
Mn2+ has no effect on the immobilized enzyme at 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2RS,RPSP)-2-amino-4-[(3-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[(4-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[bis[(3-carboxymethy)lphenoxy]phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(2-carboxyethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(carbamoylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(ethoxycarbonylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-nitrophenoxy](methoxy)phosphoryl]butanoic acid
-
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl)butanoic acid
-
competitive
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfonyl)butanoic acid
-
-
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)thio)butanoic acid
-
competitive
(2S)-2-amino-4-((4-(((carboxymethyl)amino)carbonyl)benzyl)sulfinyl)butanoic acid
-
competitive
1,10-phenanthroline
slight inhibition of free and immobilized enzyme
1,2,3,4-tetrahydroisoquinoline
-
the inhibitors can enhance cytostatic action of doxorubicin and cisplatin, which may permit clinicians to decrease their doses thereby alleviating side effects
2-amino-4-[(3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl]butanoic acid
-
-
2-mercaptoethanol
slight inhibition of free and immobilized enzyme
5-(L-gamma-glutamylamino)-2-nitrobenzoic acid
-
enzyme from human tissues, not serum
6-diazo-4 oxonorleucine
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
6-diazo-5-oxo norisoleucine
-
specific inhibitor of gamma-glutamyl transpeptidase. 1 mM, completely abolishes gamma-glutamyl transpeptidase activity
-
brefeldin A
-
inhibition of recombinant mutant enzyme secretion into cell culture medium from Sf21 cells, accumulation in the cells
Cd2+
inhibits the free enzyme by about 75% and the immobilized enzyme by about 20% at 5 mM
GGsTop
a glutamate analog that inactivates hGGT1 by forming one covalent and 11 hydrogen bonds with the enzyme, increasing the melting temperature by 20°C
iodoacetic acid
slight inhibition of free and immobilized enzyme
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
i.e. OU749. Competitive towards glycyclglycine, 150fold less toxic towards dividing cells than inhibitor acivicin. Inhibitory both to enzyme from 786-O cells and to human enzyme expressed in mouse fibroblast
phenylmethylsulfonyl fluoride
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
tosyl fluoride
-
inhibition by tosyl fluoride only in presence of maleate
Urea
-
complete inactivation of wild-type and mutant at 6 M, low activity at 4 M
(2S)-2-amino-2-[(5S)-3-chloro-4,5-dihydro-1,2-oxazol-5-yl]acetic acid
i.e. acivicin
(2S)-2-amino-2-[(5S)-3-chloro-4,5-dihydro-1,2-oxazol-5-yl]acetic acid
i.e. acivicin
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 610/per mol * s
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 5.0/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 120/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.4/per mol * s
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop, weak inhibition, structure-activity relationship, Escherichia coli enzyme GGT in complex with the inhibitor, Lys562 is the probable residue for the recognition of negative charge at C-terminal of GGsTop
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop. GGsTop shows no cytotoxicity toward human fibroblasts and hepatic stellate cells up to 1 mM. GGsTop serves as a non-toxic, selective and highly potent irreversible GGT inhibitor that can be used for various in vivo as well as in vitro biochemical studies. Lys562 of human GGT is the key residue for the recognition of the negatively charged GGsTop. The active site Lys562 of human GGT enhances the inhibitory activity of GGsTop by 128fold. GGsTop does not induce cytotoxicity for mammalian cells at up to 1 mM
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop, a potent and selective, nontoxic, and irreversible inhibitor of human gamma-glutamyl transpeptidase. GGsTop consists of four stereoisomers due to the presence of two stereogenic centers, i.e. the alpha-carbon atom of the glutamate mimic (L/D) and the phosphorus atom (RP/SP), stereoselective synthesis of the 4 isomers. With respect to the configuration of the alpha-carbon atom of the glutamate mimic, the L-isomer is about 8fold more potent than the D-isomer. In contrast, the configuration of the phosphorus atom is critical for GGT inhibitory activity. Based on a molecular modeling approach, the absolute configuration of the phosphorus atom of the active GGsTop isomers is postulated to be SP. The SP-isomers inhibits human GGT, while the RP-isomers are inactive even at concentrations of 0.1 mM
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
peptidyl phosphonate inhibitor GGsTop, the hydroxy-2-oxoethylamino-oxidanylidene-butane moiety of the inhibitor mimicks an acceptor substrate
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
-
second-order rate constant for enzyme inactivation is 19/per mol * s
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
-
second-order rate constant for enzyme inactivation is 0.16/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 80/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 75/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 12000/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 46/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 24/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.24/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 16000/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 2400/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 35000/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 130/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 2900/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 12/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 150/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 51/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 210/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.33/per mol * s
4-nitroaniline
strong, competitive against glutathione
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
methionine protects in vivo; transpeptidation, competitive to the glutamyl-donor, kinetics
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-thiohistidine
50% inhibition at 0.015 mM, mechanism of 5-thio driven inhibition of GGT, overview. Reversible inhibition mechanism
6-diazo-5-oxo-L-norleucine
i.e. DON, irreversible inhibition 50% inhibition at 0.282 mM
6-diazo-5-oxo-L-norleucine
-
S-methylglutathione; complete inactivation, accelerated by maleate, prevented by S-methylglutathione; i.e. DON, strong, irreversible modification of glutamyl-binding site of light subunit; maleate accelerates inactivation
6-diazo-5-oxo-L-norleucine
-
5-glutamyl-donor, protect transpeptidase and hydrolase activity, not 5-carbon derivative; i.e. DON, strong, irreversible modification of glutamyl-binding site of light subunit
6-diazo-5-oxo-L-norleucine
i.e. DON, a glutamate analogue, irreversible inhibitor of hGGT1, but also inhibits many essential glutamine metabolizing enzymes rendering it too toxic for use in the clinic as a GGT1 inhibitor. Binding structure analysis with human gamma-glutamyl transpeptidase 1, and molecular mechanism of hGGT1 inactivation by DON, overview. The crystal structure of DON-inactivated hGGT1 contains a molecule of DON without the diazo-nitrogen atoms in the active site. The overall structure of the hGGT1-DON complex resembles the structure of the apo-enzyme. The structure of hGGT1-DON complex reveals two covalent bonds between the enzyme and inhibitor which are part of a six membered ring. The ring includes the OG atom of Thr381, the reactive nucleophile of hGGT1 and the alpha-amine of Thr381. The mechanism of inactivation by DON differs from its inactivation of other glutamine metabolizing enzymes
6-diazo-5-oxo-L-norleucine
-
irreversible inactivation of pancreatic enzyme, S-methylglutathione prevents at 10 mM, maleate increases inhibition at 0.25-1 M
acivicin
i.e. L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
acivicin
-
the inhibitors can enhance cytostatic action of doxorubicin and cisplatin, which may permit clinicians to decrease their doses thereby alleviating side effects
acivicin
i.e. L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
azaserine
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
Co2+
inhibits the free enzyme by about 70% and the immobilized enzyme by about 15% at 5 mM
ergothioneine
a natural trimethyl-2-thiohistidine, 50% inhibition at 0.297 mM. Reversible inhibition mechanism
ergothioneine
a natural trimethyl-2-thiohistidine, reversible inhibition mechanism
glycylglycine
-
high concentration, with L-Glu-4-nitroanilide, not glutathione as donor
iodoacetamide
-
inhibition of transpeptidase reaction is more efficient than that of autotranspeptidase reaction
L- or D-Serine/borate
-
formation of a tetrahedral complex at the active site
-
L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazolacetic acid
-
i.e. acivicin; in vivo inhibition and accumulation of glutathione; kinetics; strong, irreversible, reacts with glutamyl binding site
L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazolacetic acid
-
i.e. acivicin; strong, irreversible, reacts with glutamyl binding site
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
i.e. AT-125; strong, irreversible, 1 mM
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
i.e. AT-125; strong, irreversible
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
i.e. AT-125; strong, irreversible
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
i.e. AT-125; strong, irreversible
L-azaserine
-
irreversible inactivation; not 5-carbon derivative; transpeptidase and hydrolase reaction, glutamyl-donor protects
NaCl
about 45% inhibition of the free enzyme at 2-18% w/v NaCl, about 20% inhibition of the immobilized enzyme
NaCl
at 10% NaCl, GgtBCg still retains 70% of its initial activity. Further addition of NaCl to concentrations of 15%, 20%, and 22.5% reduces the activity to 30%, 27%, and 20%, respectively. For all tested salt concentrations, activity is higher in the presence of glycyl-glycine than in its absence
Ni2+
inhibits the free enzyme by about 25% and the immobilized enzyme by about 20% at 5 mM
Pb2+
inhibits the free enzyme by about 65% and the immobilized enzyme by about 25% at 5 mM
Phenobarbital
-
active site-directed, irreversible inactivation, optimal at pH 9.0, serine/borate or GSH protects, maleate protects slightly, kinetics
serine-borate
10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity
serine-borate
competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5; competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5
Thiobarbituric acid
-
active site-directed, irreversible inactivation, optimal at pH 9.5, serine/borate or GSH protects, maleate protects slightly, kinetics
Zn2+
inhibits the free enzyme by about 85% and the immobilized enzyme by about 5% at 5 mM
additional information
immobilized enzyme CMS-GGT is 10-20% less susceptibile to inhibition by PMSF, N-bromosuccinamide and GGT specific inhibitors azaserine and 6-diazo-5-oxo-L-norleucine as compared to free enzyme
-
additional information
-
inhibition by diverse amino acids, overview
-
additional information
-
L-threonine is a poor gamma-glutamyl acceptor but facilitates the generation of gamma-Glu-Gln-[13C10], whereas L-phenylalanine is a good gamma-glutamyl acceptor but seemed to suppress the generation of gamma-Glu-Gln-[13C10], indicating an inhibitory effect as reported for glutathione
-
additional information
identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON). Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
-
additional information
no inhibition of recombinant enzyme by 200 mM L-glutamylhydrazine
-
additional information
evaluation of a phosphonate-based irreversible inhibitor, 2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid (GGsTop) and its analogues as a mechanism-based inhibitor of human GGT. GGsTop is a stable compound, but inactivates the human enzyme significantly faster than the other phosphonates, and importantly does not inhibit a glutamine amidotransferase. Structure-activity relationships, overview
-
additional information
-
evaluation of a phosphonate-based irreversible inhibitor, 2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid (GGsTop) and its analogues as a mechanism-based inhibitor of human GGT. GGsTop is a stable compound, but inactivates the human enzyme significantly faster than the other phosphonates, and importantly does not inhibit a glutamine amidotransferase. Structure-activity relationships, overview
-
additional information
synthesis and evaluation of the inhibitory activity of the four stereoisomers of inhibitor GGsTop, binding structures of RP-isomer of L-GGsTop and of the SP-isomer of L-GGsTop to GGT active site, modeling, overview
-
additional information
identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON), and are not toxic for human embryonic cells. Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
-
additional information
-
identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON), and are not toxic for human embryonic cells. Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
-
additional information
-
no inhibition by arsenite, citrate, cyanide and borate
-
additional information
-
not affected by Ni2+, K+, phtalate, pyruvate and fumarate
-
additional information
the enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of most of divalent cations like Ba2+, Ca2+, Co2+, Cd2+, Fe2+, Hg2+, Mg2+, Mn2+ and Zn2+. The enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of 10 mM chelating agents like EDTA, EGTA and 1,10-phenanthroline and is not inhibited by N-bromosuccinimide and iodoacetic acid. Reducing agents like dithiothreitol and 2-mercaptoethanol have no significant effect on the activity
-
additional information
-
no inhibition by phorbol ester, polyamines, cAMP
-
additional information
-
no inhibition: 2-amino-3-(S-methylsulfonimidoyl)propanoic acid, 2-amino-4-(methylsulfonyl)butanoic acid, 5-hydroxy-DL-lysine
-
additional information
-
not affected by KCl, KNO3, KBr, NaCl, CaCl2, MgCl2, MnCl2, CoCl2, ZnCl2, DTT, EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Subtilisin
-
subtilisin enhances transpeptidase activity of the 30000 Da and 67000 Da enzyme forms by nearly 1.5 and 2fold, respectively
-
hippurate
-
stimulates hydrolase reaction, inhibits transpeptidation
Maleate
-
stimulates hydrolase reaction 3fold, inhibits transpeptidase reaction, with L-Glu as substrate
additional information
-
nitrogen starvation induces enzyme activity
-
additional information
-
gamma-GT activity is regulated by the balance between the cytoplasmic and vacuolar level of glutathione
-
additional information
-
no effects by KCl, KNO3, KBr, NaCl, CaCl2, MgCl2, MnCl2, CoCl2, ZnCl2, DTT, EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0334
5-L-glutamyl-L-leucine
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0346
glutathione sulfonic acid
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0751
glutathionesulfonic acid
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.046
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T413P
0.048
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T463S
0.054
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, wild-type enzyme
0.0109
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, transpeptidase reaction with Gly-Gly
0.024
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.046
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
0.08
5-L-glutamyl-4-nitroanilide
in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40°C
0.22
5-L-glutamyl-4-nitroanilide
-
monomeric 30-kDa enzyme, at pH 11.0, in the presence of subtilisin, at 80°C
0.25
5-L-glutamyl-4-nitroanilide
-
heterodimeric 67-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C
0.84
5-L-glutamyl-4-nitroanilide
-
reaction in the presence of 20 mM glycylglycine
4.3
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
4.4
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
5.2
5-L-glutamyl-4-nitroanilide
-
monomeric 30-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C
0.038
gamma-Glu-Cys
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.0143
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S
0.025
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N
0.025
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S
0.067
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N
0.1
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme
0.0105
GSH
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0106
GSH
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.008
GSSG
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0426
GSSG
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.123
L-gamma-glutamyl-4-nitroanilide
pH 9.6, 37°C, recombinant enzyme
0.2
L-gamma-glutamyl-4-nitroanilide
-
pH 8.0, 37°C, native extracellular enzyme
0.214
L-gamma-glutamyl-4-nitroanilide
-
recombinant extracellular enzyme, pH 9.0, 40°C
0.3
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109F, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant wild-type enzyme, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109S, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109E, pH 9.0, 60°C
0.42
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant wild-type enzyme, pH 9.0, 40°C
0.579
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized modified wild-type enzyme MTWs-GGT-Phar, pH 8.0, 37°C
0.58
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450Q, pH 9.0, 40°C
0.58
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450D, pH 9.0, 40°C
0.597
L-gamma-glutamyl-4-nitroanilide
-
recombinant free wild-type enzyme GGT, pH 8.0, 37°C
0.69
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450A, pH 9.0, 40°C
0.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109K, pH 9.0, 60°C
0.76
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450K, pH 9.0, 40°C
0.879
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized wild-type enzyme, MTWs-GGT, pH 8.0, 37°C
8.2
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109L, pH 9.0, 60°C
10.6
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109M, pH 9.0, 60°C
0.13 - 0.18
L-Glu-4-nitroanilide
-
with L-Cys-bis-glycine, rat kidney enzyme
0.0102
leukotriene C4
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0108
leukotriene C4
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0131
S-(4-nitro-benzyl)glutathione
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0148
S-(4-nitro-benzyl)glutathione
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0099
S-Methylglutathione
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0182
S-Methylglutathione
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
additional information
additional information
-
Km-values for several acceptors in diabetic and control rats, female and male, with donors L-Glu-4-nitroanilide and L-5-glutamyl-(7-amido-4-methylcoumarin)
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
kinetic study of renatured large subunit
-
additional information
additional information
-
enzyme from seminal plasma, kidney, prostate, and testis
-
additional information
additional information
-
biphasic kinetics in transpeptidase reaction with 1-aminocyclopropane-1-carboxylic acid as acceptor, Km-values
-
additional information
additional information
-
thermodynamics and kinetic analysis of free and immobilized recombinant enzymes, overview
-
additional information
additional information
steady-state kinetics of purified free enzyme BLGGT and purified immobilized enzyme CMS-GGT
-
additional information
additional information
enzyme kinetics analysis is done according to the ping-pong mechanism when both the substrates L-gamma-glutamyl-4-nitroanilide and glycyl-glycine are used
-
additional information
additional information
-
enzyme kinetics analysis is done according to the ping-pong mechanism when both the substrates L-gamma-glutamyl-4-nitroanilide and glycyl-glycine are used
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics with L-gamma-glutamyl-4-nitroanilide as substrate, native extracellular enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, wild-type enzyme
0.38
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T463S
0.41
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T413P
15
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
16
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
38
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
39
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
97
5-L-glutamyl-4-nitroanilide
in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40°C
1.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109E, pH 9.0, 60°C
1.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109F, pH 9.0, 60°C
8.3
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109L, pH 9.0, 60°C
8.93
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450K, pH 9.0, 40°C
16.04
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant wild-type enzyme, pH 9.0, 40°C
21.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109M, pH 9.0, 60°C
21.74
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450Q, pH 9.0, 40°C
95
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109S, pH 9.0, 60°C
106.7
L-gamma-glutamyl-4-nitroanilide
recombinant wild-type enzyme, pH 9.0, 60°C
123.65
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450A, pH 9.0, 40°C
175.52
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450D, pH 9.0, 40°C
305
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109K, pH 9.0, 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.01
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, wild-type enzyme
7.88
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T463S
8.83
(gamma-L-glutamyl)-4-nitroanilide
pH 10.0, 37°C, mutant enzyme T413P
1245
5-L-glutamyl-4-nitroanilide
in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40°C
25
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N
39.3
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme
101
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S
172.8
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S
182.3
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N
1.01
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109L, pH 9.0, 60°C
2.05
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109M, pH 9.0, 60°C
4.25
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109E, pH 9.0, 60°C
5.67
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109F, pH 9.0, 60°C
11.75
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450K, pH 9.0, 40°C
37.48
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450Q, pH 9.0, 40°C
38.19
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant wild-type enzyme, pH 9.0, 40°C
179.02
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450A, pH 9.0, 40°C
237.5
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109S, pH 9.0, 60°C
266.75
L-gamma-glutamyl-4-nitroanilide
recombinant wild-type enzyme, pH 9.0, 60°C
302.62
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450D, pH 9.0, 40°C
435.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109K, pH 9.0, 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl)butanoic acid
-
-
3.5
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfonyl)butanoic acid
-
-
0.52
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)thio)butanoic acid
-
-
0.23
(2S)-2-amino-4-((4-(((carboxymethyl)amino)carbonyl)benzyl)sulfinyl)butanoic acid
-
-
0.053
2-amino-4-[(3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl]butanoic acid
-
-
0.0287
4-chloro-N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
0.0743
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]-4-nitrobenzenesulfonamide
-
-
4.2
serine-borate
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
41.6
serine-borate
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
additional information
additional information
-
Ki-values for derivatives of 4-acrboxybutyramide, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine: Ki values in different tissues, overview
-
additional information
additional information
inhibition kinetics, overview
-
additional information
additional information
inhibition kinetics, overview
-
additional information
additional information
-
inhibition kinetics, overview
-
additional information
additional information
inhibition kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
-
mutant derived from truncation of 132 bp at the 5' end, pH 8.0, 40°C
0.59
0.8
-
mutant derived from truncation of 129 bp at the 5' end, pH 8.0, 40°C
1.3
10.4
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C
12
12.9
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C
120
15
16
16.1
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C
17
about, recombinant enzyme mutant F417Y, pH 10.5, 30°C, transpeptidation activity
17.8
purified recombinant His6-tagged enzyme, substrates L-gamma-glutamyl-4-nitroanilide and glycylglycine, pH 9.0, 40°C
18
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats with tumor
20
measured in jejunal mucosa after treatment with dietary glutamine in normal rats
25
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats without tumor
250.09
purified free enzyme, pH and temperature not specified in the publication
4.8
truncation mutant lacking 17 amino acids at the N-terminus, pH 9.0, 40°C
4.9
truncation mutant lacking 11 amino acids at the N-terminus, pH 9.0, 40°C
55
-
purified recombinant extracellular enzyme, pH 9.0, 40°C, substrate L-gamma-glutamyl-4-nitroanilide
7.1
about, recombinant wild-type enzyme, pH 10.5, 30°C, transpeptidation activity
additional information
1.3
-
mutant derived from truncation of 36 bp at the 5' end, pH 8.0, 40°C
15
about, recombinant enzyme mutant W385T, pH 10.5, 30°C, transpeptidation activity
16
about, recombinant enzyme mutant W525A, pH 10.5, 30°C, transpeptidation activity
additional information
quantitation of dipeptides and amino acids by HPLC in whole-cell assays
additional information
-
quantitation of dipeptides and amino acids by HPLC in whole-cell assays
additional information
-
poor comparability of routine gamma-glutamyltransferase activity measurement. gamma-Glutamyltransferase assays are standardized by intermethod calibration. Effect on determining common reference limits
additional information
-
activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
additional information
-
activity during developmental stages in lung epithelial cells type I and II
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10.5
6 - 8
7.4
7.5
7.5 - 8
7.6
8.2
8.2 - 8.5
8.5
8.6
8.8
8.8 - 9
9 - 9.5
9.5
additional information
8
-
monomeric 30-kDa enzyme and heterodimeric 67000-Da enzyme, in the absence of subtilisin
9 - 9.5
-
transpeptidation with 5-L-glutamyl-4-nitroanilide and glycylglycine
additional information
-
several isozymic forms with different content of sialic acid
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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 - 10
BaGGT469 shows the highest activity towards L-gamma-glutamyl-4-nitroanilide with diglycine acceptor in 50 mM borate-NaOH buffer at pH 10.0. The enzymatic activity at the alkaline pH range of pH 8.0-9.0 is 92.6-95.9% relative to that at optimum pH. BaGGT469 is much less active in the acidic pH range from pH 4.0-6.0
4 - 11
4 - 13
pH 4.0: about 50% of maximal activity, pH 13: about 40% of maximal activity
4 - 9
more than 40% of maximal activity, hydrolysis of gamma-glutamyl-4-nitroanilide
5 - 11
5 - 12
5.5 - 12
activity range, over 60% of maximal activity at pH 7.5-10.5, profile overview
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
6 - 9
6.5 - 9
-
pH 6.5: about 50% of maximal activity, pH 9.0: about 90% of maximal activity
7 - 10
7 - 11
7 - 9
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
8.1 - 9.6
-
about 70% of maximal activity at pH 8.1, about 75% of maximal activity at pH 9.6
5 - 11
-
46/75/64% relative activity at pH 7.0/8.0/10.0, respectively, recombinant enzyme, profile overview
5 - 11
over 40% of maximal activity within this range for the free enzyme, profile overview
5 - 12
over 60% of maximal activity within this range for the immobilized enzyme, profile overview
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 70% of maximal activity, hydrolysis of 5-L-glutamyl-4-nitroanilide
6 - 9
-
pH 6.0, about 55% of maximal activity, pH 9.0: about 80% of maximal activity, enzyme form GGT A
6 - 9
-
pH 6.0, about 55% of maximal activity, pH 9.0: about 80% of maximal activity, enzyme form GGT B
7 - 10
-
no significant activities are detected below pH 7.0 or above pH 10.0
7 - 10
-
pH 7.0: about 55% of maximal activity, pH 10.0: about 60% of maximal activity
7 - 11
-
about 35% activity at pH 7.0, about 55% activity at pH 8.0, about 85% activity at pH 9.0, 100% acitivity at pH 10.0, about 75% activity at pH 11.0
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: 65% of maximal activity
7 - 9
-
pH 7.0, about 50% of maximal activity, pH 9.0: about 80% of maximal activity, enzyme form GGT I
7 - 9
-
pH 7.0, about 50% of maximal activity, pH 9.0: about 80% of maximal activity, enzyme form GGT II
8 - 11
-
pH 8.0: about 60% of maximal activity, pH 8.5-11: optimum, hydrolysis of 5-L-glutamyl-4-nitroanilide
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
45
50
60
70
37
-
assay at
60
-
monomeric 30-kDa enzyme and heterodimeric 67000-Da enzyme, in the absence of subtilisin
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
22 - 60
the optimal temperature of GgtBCg is 45°C. The enzyme exhibits 85% and 60% of the maximal activity at 37°C and 22°C, respectively. Whereas GgtBCg retains 50% activity at 60°C, it is completely inactivated at 70°C, recombinant enzyme
30 - 50
30 - 70
30 - 80
over 50% of maximal activity within this range, profile overview
35 - 55
-
about 70% activity at 35°C, about 80% activity at 40°C, 100% activity at 45°C, about 85% activity at 50°C, about 45% activity at 55°C
40 - 60
more than 40% of maximal activity, hydrolysis of gamma-L-glutamyl-4-nitroanilide
40 - 80
about 60% of maximal activity at 40°C for free and immobilized enzyme, 30% of maximal activity at 80°C for the free enzyme, 75% for the immbilized enzyme, profile overview
45 - 80
-
about half-maximal activity at 45°C and about 70% of maximal activity at 80°C
20 - 70
-
40/56/34/20/6% relative activity at 20/30/50/60/70°C, respectively, recombinant enzyme, profile overview
20 - 70
-
20°C: about 70% of maximal activity, 60°C: about 90% of maximal activity, 70°C: about 40% of maximal activity
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 - 50
30°C: about 85% of maximal activity, 50°C: about 80% of maximal activity
30 - 50
-
30°C: about 60% of maximal activity, 50°C: about 80% of maximal activity
30 - 70
activity range, 8.9% of maximal activity at 70°C, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus amyloliquefaciens SMB469
Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang
UniProt
brenda
Picrophilus oshimae DSM 9790
enzyme displays both glutathione hydrolase, EC 3.4.19.13, and gamma-glutamyl transpeptidase activity
UniProt
brenda
enzyme displays both glutathione hydrolase, EC 3.4.19.13, and gamma-glutamyl transpeptidase activity
UniProt
brenda
Bacillus amyloliquefaciens strain SMB469 with high GGT activity is isolated from a Korean traditional fermented soy food, Doenjang
UniProt
brenda
-
487897, 487898, 487901, 487902, 487903, 487904, 487906, 487909, 487932, 487933, 487934, 487935, 487937, 487938, 487939, 487940, 487941, 487942, 487949, 487961, 487963
-
-
brenda
-
659102, 671385, 672422, 675806, 677259, 684237, 684407, 684743, 684782, 684787, 684788, 684804, 684806, 684807, 685119, 685956, 686109, 686110, 686146, 686152, 686156, 686163, 686165, 686273, 686301, 686307, 686309, 686311, 686312, 686313, 686319, 686321, 686346, 686496, 686498, 686500, 686578, 686914, 687000, 687004, 687012, 687148, 687153, 687197, 687997, 688133, 688145, 688775, 688810, 688817, 689280, 689283, 689332, 690044, 690163, 695962, 702160, 702533, 703806, 704637, 705830, 717083
-
-
brenda
Swiss albino and RIII strain, both infected with mammary tumour virus, uninfected: C57BL strain
-
-
brenda
-
487899, 487905, 487912, 487929, 487930, 487931, 487932, 487936, 487938, 487957, 487958, 487966, 487971, 657955, 658282, 659787, 660051, 672838, 672853, 675805, 676350, 686893, 703189, 703401, 706842, 755785
-
-
brenda
wild-type and enzyme-deficient strain, nitrogen starvation-induced
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
upreglation of gamma-glutamyl transpeptidase is induced by suboptimal concentrations of the serum and modification of intracellular cAMP level by dibutyryl cAMP. Up-regulation of gamma-glutamyl transpeptidase can contribute to adaption of astrocytic cells to metabolic and/or oxidative perturbances occuring under various pathological conditions, including radiation- and drug-induced toxicity
brenda
-
gamma-glutamyltransferase is upregulated after oxidative stress through the Ras signal transduction pathway in rat colon carcinoma cells
brenda
-
decrease in the hippocampal GGT decreases 2 h after the intravenous injection of 0.005 mg IL-1beta, increaes after 24 h and returns to control levels after 96 h. No significant changes in the hippocampal GGT activity are observed at 2 h and 24 h following the intracerebroventricular infusion of 50 ng IL-1beta
brenda
-
GGT-overexpression in melanoma cells is associated with resistance to oxidative stress produced by prooxidant agents such as hydrogen peroxide and ascorbic acid
brenda
-
the enzyme is present in granules and released upon cell activation
brenda
-
ATCC CRL-1932, a GGT-positive renal cell adenocarcinoma line
brenda
GGT1 accounts for nearly 100% of the activity in rosettes
brenda
-
gamma-glutamyl transpeptidase of Aphidius ervi venom induces apoptosis in the ovaries of host aphids
brenda
additional information
skin and pulp of mature berries, across whole berry development, VvGGT3 demonstrates a general pattern of increasing in transcript abundance
brenda
protein is present at equal abundance in the skin, pulp, and seed of mature berries
brenda
-
from individuals with no alcohol-related problems (NARP), individuals presenting alcohol abuse (AA) or individuals with alcohol dependence (AD). The highest gamma-glutamyltransferase values are seen in the AD group
brenda
-
the mean values of the gamma-glutamyltransferase in chronic dialysis patients and renal transplant recipients with hepatitis C virus infection are 3 or 4times above the reference limit and a greater frequency of patients evolve with values persistently elevated
brenda
-
dyslipidemic patients exhibiting metabolic syndrome are characterized by elevated GGT activity which is associated with perturbed metabolism of thiol compounds
brenda
-
in a general population of children, overweight and abdominal fat distribution are associated with increased GGT. GGT activity is higher in boys than in girls as puberty starts
brenda
-
elevated GGT is significantly associated with increased cancer risk in men
brenda
-
plasma layer stratification might occur in primary lithium-heparin tubes for a limited number of routine clinical chemistry tests, introducing a statistically significant bias in the measurement of gamma-glutamyltransferase, lactate dehydrogenase, triglycerides and C-reactive protein in the upper vs. the bottom section. When delayed testing is necessary for these parameters, plasma should be separated after centrifugation and appropriately mixed before delayed/repeated analysis or aliquoting
brenda
-
four GGT fractions of different molecular weight are detected in all subjects of both genders: b-GGT, m-GGT, s-GGT (likely lipoprotein-bound, molecular masses >2000, 940, and 140 kDa, respectively), and a free fraction (f-GGT, 70 kDa). Higher total GGT activity in males is related mainly to f-GGT
brenda
-
elevated GGT in diabetic children could be due to release from apoptotic cells
brenda
-
pattern of changes in gamma-glutamyltransferase catalytic activity and total antioxidant status concentration might be indicative of a certain role of thrombocytosis during treatment in patients with community-acquired pneumonia
brenda
-
higher serum gamma-glutamyltransferase levels are associated with prehypertension in a nationally representative sample of US adults, free of cardiovascular disease and hypertension
brenda
-
strong interaction between serum gamma-glutamyltransferase and obesity on the risk of prevalent type 2 diabetes
brenda
-
gamma-glutamyltransferase is associated with mortality in both men and women, especially in patients younger than 30 years. Even high-normal gamma-glutamyltransferase is a risk factor for all-cause mortality
brenda
-
increased GGT activities are independently associated with a more atherogenic lipid profile in general population
brenda
-
GSTM1- and GSTM1-/GSTT1- genotypes may be a genetic risk factor for the increase of GGT in Japanese epileptic patients treated with valproic acid patients. It is not possible to clarify whether the GGT increase is caused by valproic acid-induced hepatotoxicity or not
brenda
-
subjects are divided into four groups according to their level of alcohol consumption: nondrinkers, light drinkers (1-188 ml/week), intermediate drinkers (189-377 ml/week), and heavy drinkers (more than 378 ml/week). The frequency of subjects with an fasting plasma glucose of 110 mg/dl or more rises significantly as alcohol consumption increases, from 6.7% in non-drinkers to 10.1% in intermediate drinkers and 12.1% in heavy drinkers. When only the subjects with a gamma-glutamyltransferase level of less than 40 IU/l are analyzed, no difference is observed in the frequency of subjects with an FPG level of 110 mg/dl or more among the four groups
brenda
-
GGT is closely related with insulin resistance and the increased number of components of metabolic syndrome. Among components of metabolic syndrome, serum GGT may be more associated with dyslipidemia and abnormal glucose tolerance, suggesting that serum GGT has more relationship with hepatic insulin resistance regardless of non-alcoholic fatty liver disease
brenda
-
serum GGT is specifically associated with the visceral fat area, but not with the subcutaneous fat area, suggests that the serum GGT may be useful as a convenient indicator of visceral fat area in the clinical treatment of obesity
brenda
-
association between serum gamma-glutamyltransferase and type 2 diabetes
brenda
-
habitual coffee consumption is associated with lower incidence of type II diabetes particularly in those with higher baseline serum GGT levels
brenda
-
high serum gamma-glutamyltransferase is associated with an increased risk of liver cancer
brenda
-
associations of gamma-glutamyltransferase with fasting glucose and HbA1c are stronger in women with diabetes compared to women without diabetes. gamma-Gutamyltransferase is associated with fasting insulin to the same extent in all women, irrespective of diabetes status. Results excluding hyperinsulinemic women, i.e., in the highest fourth of the fasting insulin distribution, are similar to those obtained for all non-diabetic women as are results excluding women in the highest quartile of the alcohol consumption distribution and for women with alanine aminotransferase and gamma-glutamyltransferase levels within the normal range
brenda
-
gamma-glutamyltransferase level is related to adiponectin level in nonalcoholic women without liver disease
brenda
-
gamma-glutamyltransferase is independently associated with an increased level of C-reactive protein in both males and females. In addition, in males, gamma-glutamyltransferase is related to an increased level of arterial stiffness
brenda
-
GGT level has positive correlation with family history of liver disease
brenda
-
serum GGT activity is increased in patients with calcific aortic stenosis. These increases seem to occur in advanced rather than milder forms of calcific aortic valve disease
brenda
-
serum gamma-glutamyltransferase levels are positively associated with peripheral arterial disease among men (peripheral arterial disease) but not women
brenda
-
association between serum gamma-glutamyltransferase levels and coronary microvascular function in hypertensive patients
brenda
-
serum GGT within its normal range can predict cardiovascular diseases mortality in those aged less than 70 years, but may have limited usefulness for risk assessment in older adults
brenda
-
GGT activities from 1147 moderate drinkers and 449 abstainers are classified according to body mass index are compared with those of 208 heavy drinkers admitted for detoxification. GGT upper normal limits, defined based on normal weight abstainers are lower than those based on moderate drinkers. The relative increases in GGT activities in male moderate drinkers with overweight (54%) or obesity (125%) exceedes the corresponding changes found in women (25% and 75%, respectively). The BMI-dependent variation on the sensitivity of GGT for correctly classifying heavy drinkers ranges from 29% to 67%. The rates of false-positive values in the subgroups from low to high BMI varies from 0% to 27%, respectively
brenda
-
GGT levels are increased significantly in Alzheimers disease patients
brenda
-
gamma-glutamyltransferase can be used as a marker related with oxidative stress
brenda
-
presence in plaques of a serum-like gamma-glutamyltransferase protein, indicating that a direct contribution of serum gamma-glutamyltransferase to enzyme activity found within atherosclerotic lesions is possible. Occurrence of gamma-glutamyltransferase-mediated redox reactions within plaque environment might influence plaque progression
brenda
-
higher serum gamma-glutamyltransferase levels are independently associated with impaired coronary microvascular function in patients with dilated cardiomyopathy
brenda
-
elevated gamma-glutamyltransferase is associated with significantly increased risk of stroke, fatal coronary heart disease events and cardiovascular disease mortality independent of established cardiovascular disease risk factors and may be a useful additional marker for long-term cardiovascular disease
brenda
-
treatment with 1,2,3,4-tetrahydroisoquinolone affects the enzymatic activity of gamma-glutamyl transpeptidase in the dopaminergic structures of brain
brenda
-
the activity of gamma-glutamyl transpeptidase increases during cold storage whereas it declines during warm storage. gamma-Glutamyl transpeptidase is involved in garlic greening
brenda
-
in wild-type the enzyme is synthesized only during the mid-stationary phase
brenda
-
in wild-type the enzyme is synthesized only during the mid-stationary phase
-
brenda
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
brenda
-
the role of high gamma-glutamyltransferase activity in Hep-G2 cells can be connected with production of reactive oxygen species and with S-thiolation with Cys and Cys-Gly that can influence activity of caspase 3
brenda
-
-
brenda
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
brenda
-
tissue, serum and bile contain multiple enzyme forms of different molecular weights
brenda
-
icreased levels of gamma-glutamyltransferase during hepato-biliary dysfunction
brenda
-
normal and induced enzyme activity, not expression level, by streptozotocin diabetes induced in rats
brenda
-
hyperplastic hepatic nodules, primary and Yoshida ascites (AH 13) hepatomas
brenda
-
80-90% of activity in biliary tract, distribution in liver tissues
brenda
-
mammary cell products formed by exocytosis: mammary tumour virus
brenda
Oncornavirus
-
mammary cell products formed by exocytosis: mammary tumour virus
brenda
-
in milk of virus infected and uninfected mice, milk fat-globule membrane
brenda
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
brenda
GGT1 accounts for greater than 80% of the activity in stems and roots
brenda
-
high activity in root apical region. Protein is anchored to root cell wall components
brenda
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
brenda
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
brenda
GGT1 accounts for greater than 80% of the activity in stems and roots
brenda
-
gamma-glutamyl transpeptidase, and N-acetyl-beta-D-glucosaminidase are significantly higher in daytime samples than in overnight samples
brenda
additional information
O65652
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
brenda
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
brenda
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
brenda
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
brenda
additional information
-
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
brenda
additional information
O65652
GGT4 activity, if present in the roots and stems, is near the limit of detection
brenda
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
brenda
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
brenda
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
brenda
additional information
-
GGT4 activity, if present in the roots and stems, is near the limit of detection
brenda
additional information
-
accumulation of catalytically active enzyme in atherosclerotic lesion
brenda
additional information
activity of GGT1 is increased in liver disease, oxidative stress and metabolic syndrome
brenda
additional information
activity of GGT1 is increased in liver disease, oxidative stress and metabolic syndrome
brenda
additional information
-
activity of GGT1 is increased in liver disease, oxidative stress and metabolic syndrome
brenda
additional information
-
not detected in brain, skin, skeletal muscle, and peripheral nerves including the axon and myelin sheath
brenda
additional information
-
blood-brain-barrier-associated isozyme activity induces the cell to form three-dimensional structures in cell culture, inducible by angiogenic and astroglial factors, e.g. bFGF, formation is reduced by cAMP
brenda
additional information
-
the enzyme is widely expressed on the apical surface of epithelial-cell lining ducts, most prominently in the proximal tubules of the kidney and liver biliary ducts, and is also expressed on leukocytes and astrocytes. Non-invasive, real-time detection of GGT activity in vivo, overview
brenda
additional information
the VvGGT3 transcript is expressed in all tissues tested, i.e. roots, leaf, inflorescences, and tendril, and in the skin, pulp, and seed fractions of mature grape berries. The transcript abundance of VvGGT3 is the lowest in the tendril, followed by the root, with a 1.7 and 1.8fold increase in leaf and inflorescence compared to the tendril, respectively. Focusing on the relative VvGGT3 abundance in the skin, pulp, and seed fractions of mature grape berries, similar levels of transcript is observed in all three berry tissues, with these all being over 7fold higher than the tendril
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
recombinant enzyme is extracellular in transgenic tabacco plants
-
brenda
-
mutant lacking the membrane anchor domain, secretion into the medium of recombinant Sf21 cell culture
-
brenda
-
transfection of Me665/2/21 human melanoma cell, DU145 human prostatic carcinoma cell, and BEAS-2B human bronchial epithelial cell results in release of soluble enzyme whose activity increases in parallel with the cell growth. Released GGT presents a molecular weight of 2000 kDa, identical to the beta-GGT fraction of human plasma and corresponding to that of VLDL, but with higher density
-
brenda
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
brenda
-
polarized, outer apical surface alveolar epithelium
brenda
the functional VvGGT3 is probably associated with membrane-like structures. VvGGT3-GFP fusion protein does not localize to the vacuole in transformed Nicotiana benthamiana cells
brenda
-
cellular GGT is an ectoenzyme present on the outer aspect of plasma membrane, with active site externally oriented. The expression of the cellular GGT is often increased in tumor cells and during tumor progression. Release of the cellular enzyme in different molecular forms, depending on extracellular conditions
brenda
-
serum GGT is a solubkle enzyme, it forms complexes with distinct lipoprotein fractions
-
brenda
GGT1 is an extracellular enzyme that is anchored to the plasma membrane of cells
brenda
-
regulation of glutathione import into the vacuoles, kinetics
brenda
additional information
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
-
brenda
additional information
-
prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Q62WE3
Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) belongs to N-terminal nucleophile hydrolase superfamily in which all inclusive members are synthetized as single-chain precursors, and then self-processed to form mature enzymes
evolution
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
evolution
gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
evolution
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
evolution
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
evolution
-
Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) belongs to N-terminal nucleophile hydrolase superfamily in which all inclusive members are synthetized as single-chain precursors, and then self-processed to form mature enzymes
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases
-
evolution
-
gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily
-
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
-
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
-
evolution
-
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala)
-
evolution
-
the 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)
-
malfunction
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
malfunction
-
deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans
malfunction
human GGT protein without the N-terminal anchor domain is expressed as a soluble enzyme and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain
malfunction
-
frequently abnormal serum gamma-glutamyl transferase activity is associated with future development of fatty liver
malfunction
-
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
-
malfunction
-
deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans
-
malfunction
-
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
-
malfunction
-
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
-
malfunction
-
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
-
malfunction
-
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo
-
metabolism
-
the enzyme induces tissue factor expression in monocytes through a cytokine-like mechanism that involves the activation of TLR4/NF-kappaB signaling
metabolism
-
serum gamma-glutamyltranspeptidase activity is typically elevated in biliary atresia. In approximately 12%-25% of cases, gamma-glutamyltranspeptidase is normal or low. Normal or low gamma-glutamyltranspeptidase in patients with biliary atresia is associated with a worse prognosis
metabolism
-
the gamma-glutamyltransferase gene of Helicobacter pylori can promote gastric carcinogenesis by activating Wnt signal pathway through up-regulating ten-eleven translocation 1 (TET1)
metabolism
-
the abnormal gamma-glutamyl transferase in biliary cholangitis and cholestasis drug-induced liver injury is associated with cholestasis. In alcoholic liver disease, it is associated with both oxidative stress and cholestasis, and in non-alcoholic fatty liver disease, it is associated with oxidative stress. gamma-Glutamyl transferase levels have different characteristics in different liver diseases, which are closely related to the pathogenesis of liver diseases
physiological function
-
cells overexpressing gamma-GT exhibit a low susceptibility to arsenic trioxide-induced apoptosis, associated with low reactive oxygen species induction and increased catalase activity
physiological function
-
GGT is essential to the recovery of apoplasic glutathione provided exogenously or extruded by oxidative treatment. GGT activity helps to salvage extracellular glutathione and may contribute to redox control of the extracellular environment
physiological function
-
gamma glutamyltranspeptidase is a key enzyme involved in mediating cisplatin nephrotoxicity, which potentially acts to cleave cisplatin-GSH conjugates to a toxic metabolite
physiological function
-
gamma glutamyltranspeptidase is a key enzyme involved in mediating cisplatin nephrotoxicity, which potentially acts to cleave cisplatin-GSH conjugates to a toxic metabolite
physiological function
-
the enzyme induces cell cycle arrest at the G1-S phase transition in AGS cells
physiological function
-
the enzyme partakes in glutathione uptake by Helicobacter pylori
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of gamma-glutamyl moiety from a donor molecule to an acceptor molecule by cleavage and subsequent formation of a gamma-amide bond. The acceptor can be an amino acid, a peptide or a water molecule. Under physiological conditions, GGT enzyme expression from wild strains of bacteria, such as Escherichia coli and Bacillus, is tightly regulated because of the involvement of the enzyme in various stress and starvation conditions
physiological function
gamma-glutamyltranspeptidase is an organosulfur compound (GGT) and catalyzes the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water
physiological function
gamma-glutamyltranspeptidases (GGTs) catalyze the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water
physiological function
grapevine appears to contain only a single GGT gene, possessing all the key conserved residues needed for GGT activity. VvGGT3 has a proposed role in the formation of precursors of key varietal aromas in wine. These compounds are considered to be derived from the lipoxygenase/hydroperoxide lyase mediated breakdown of linolenic and linoleic C18 fatty acids to produce C6 hexanal and then its derivatives
physiological function
-
the gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme that plays an essential central role in glutathione (GSH) homeostasis. Elevated serum GGT levels are a general marker of diseases affecting the liver
physiological function
-
gamma-glutamyl dipeptides (gamma-GPs) are responsible for the attractive Kokumi flavor of Parmesan cheese. They are synthesized by gamma-glutamyltransferase (GGT) from milk, most efficiently after 24 months of ripening (PC-24). GGT catalyzes the transfer of the gamma-glutamyl moiety of L-glutamine onto various acceptor amino acids released upon casein proteolysis. Microflora analysis in Parmesan cheese and GGT activity of Lactobacillus strains, overview. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
physiological function
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
physiological function
-
gamma-glutamyl transpeptidase (GGT) is a widely distributed enzyme from bacteria to plants and mammals that catalyzes the cleavage of the gamma-glutamyl linkage of gamma-glutamyl compounds, such as glutathione and transfer of the gamma-glutamyl residue either to amino acid or peptides (transpeptidation) or water (hydrolysis, EC 3.4.19.13). GGT catalyzes the release of the glutamic acid moiety from (S,S)-gamma-glutamyl-(cis-S-1-propenyl)-thioglycine, a flavor precursor found in Toona sinensis. Toona sinensis shoots and young leaves with unique aroma are consumed as a delicious seasonal vegetable in China. GGT may play an important role in the formation of volatile sulfur-containing compounds, including propene thiol which determines the characteristic aroma of Toona sinensis vegetables
physiological function
purified recombinant wild-type and inactive mutant enzymes both induce similar levels of osteoclastogenesis in Mus musculus mixed osteoblast and bone marrow-derived macrophage cell culture. Bacillus subtilis GGT possesses virulent bone-resorbing activity and its activity is probably independent of its enzymatic activity. The GGT heavy subunit shows strong activity of osteoclastogenesis while the light subunit fails to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. Since the GGT light subunit contains the catalytic pocket, enzymatic activity may not be required for this virulence activity. In addition, recombinant Bacillus subtilis GGT stimulates mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2) in mouse cells, while an osteoprotegerin inhibits the osteoclast formation induced by the GGT heavy subunit. Bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
physiological function
gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme involved in glutathione metabolism and maintenance of redox homeostasis. High expression of GGT on tumor cells is associated with an increase of cell proliferation and resistance against chemotherapy. GGT catalyzes the cleavage of gamma-glutamyl compounds and the transfer of the gamma-glutamyl group to an acceptor substrate by a ping-pong mechanism. GSH, the most common physiological substrate of GGT, acts as the gamma-glutamyl donor in the initial reaction of hydrolysis (EC 3.4.19.13)
physiological function
gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme involved in glutathione metabolism and maintenance of redox homeostasis. High expression of GGT on tumor cells is associated with an increase of cell proliferation and resistance against chemotherapy. GGT catalyzes the cleavage of gamma-glutamyl compounds and the transfer of the gamma-glutamyl group to an acceptor substrate by a ping-pong mechanism. GSH, the most common physiological substrate of GGT, acts as the gamma-glutamyl donor in the initial reaction of hydrolysis (EC 3.4.19.13)
physiological function
-
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
enzyme gamma-glutamyl transpeptidase 1 (GGT1) cleaves extracellular gamma-glutamyl compounds and contributes to the pathology of asthma, reperfusion injury and cancer
physiological function
gamma-glutamyl transpeptidase (GGT) catalyzes the hydrolysis (EC 3.4.19.13) and transpeptidation of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione metabolism
physiological function
gamma-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
-
the enzyme is involved in the progression of atherosclerosis, since its enzymatic activity promotes the generation of reactive oxygen species
physiological function
putative physiological role in glutathione utilization as a source of amino acid and nitrogen under nutrient limiting conditions
physiological function
-
purified recombinant wild-type and inactive mutant enzymes both induce similar levels of osteoclastogenesis in Mus musculus mixed osteoblast and bone marrow-derived macrophage cell culture. Bacillus subtilis GGT possesses virulent bone-resorbing activity and its activity is probably independent of its enzymatic activity. The GGT heavy subunit shows strong activity of osteoclastogenesis while the light subunit fails to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. Since the GGT light subunit contains the catalytic pocket, enzymatic activity may not be required for this virulence activity. In addition, recombinant Bacillus subtilis GGT stimulates mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2) in mouse cells, while an osteoprotegerin inhibits the osteoclast formation induced by the GGT heavy subunit. Bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction
-
physiological function
-
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-glutamyltransferases (GGTs) are widespread, conserved enzymes that catalyze the transfer of the gamma-glutamyl moiety from a donor substrate to water (hydrolysis, EC 3.4.19.13) or to an acceptor amino acid (transpeptidation)through the formation of a gamma-glutamyl enzyme intermediate
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
-
physiological function
-
the enzyme induces cell cycle arrest at the G1-S phase transition in AGS cells
-
physiological function
-
the function of this enzyme is not to degrade, but to produce, gamma-glutamyl compounds, which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
the enzyme partakes in glutathione uptake by Helicobacter pylori
-
physiological function
-
putative physiological role in glutathione utilization as a source of amino acid and nitrogen under nutrient limiting conditions
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyltranspeptidase (GGT) catalyzes the cleavage of gamma-glutamyl compounds and the transfer of gamma-glutamyl moiety to water or to amino acid/peptide acceptors
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of gamma-glutamyl moiety from a donor molecule to an acceptor molecule by cleavage and subsequent formation of a gamma-amide bond. The acceptor can be an amino acid, a peptide or a water molecule. Under physiological conditions, GGT enzyme expression from wild strains of bacteria, such as Escherichia coli and Bacillus, is tightly regulated because of the involvement of the enzyme in various stress and starvation conditions
-
physiological function
-
gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety from donor compounds such as L-glutamine (Gln) and glutathione (GSH) to an acceptor
-
physiological function
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
-
additional information
Q62WE3
the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
additional information
-
the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
additional information
A0A415J2H1
functional role of the conserved glycine residues, Gly481 and Gly482, in gamma-glutamyltranspeptidase reaction. Several residues, including Arg109, Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482, are proposed to be involved in the binding of the substrate
additional information
-
functional role of the conserved glycine residues, Gly481 and Gly482, in gamma-glutamyltranspeptidase reaction. Several residues, including Arg109, Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482, are proposed to be involved in the binding of the substrate
additional information
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
additional information
-
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
additional information
catalytic mechanism of human GGT, catalytic Thr381 within the active site, acts as a nucleophile and attacks the delta-carbon of the glutamate moiety, leading to the formation of a tetrahedral intermediate (gamma-glutamyl enzyme complex), stabilized by two conserved glycines (Gly473 and Gly474 in hGGT), overview
additional information
-
catalytic mechanism of human GGT, catalytic Thr381 within the active site, acts as a nucleophile and attacks the delta-carbon of the glutamate moiety, leading to the formation of a tetrahedral intermediate (gamma-glutamyl enzyme complex), stabilized by two conserved glycines (Gly473 and Gly474 in hGGT), overview
additional information
-
enzyme AngammaGT has little hydrolase activity (cf. EC 3.4.19.13)
additional information
hGGT1 catalytic reaction mechanism, activation of the catalytic nucleophile that initiates the hGGT1 reaction, overview
additional information
-
hGGT1 catalytic reaction mechanism, activation of the catalytic nucleophile that initiates the hGGT1 reaction, overview
additional information
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
additional information
-
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
additional information
-
the binding of L-glutamate occurs in a concave site lined by residues Arg109,Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482. Asn450 interacts with Asp441 by a hydrogenbond and consequently binds with Arg109 and Glu438 through the hydrogen bond network to hold the substrate in the properposition, suggesting that this residue can be also important for the catalytic function of BlGGT. The putative active residue is Thr399. Superimposition of the catalytic environment of wild-type and mutant enzymes, overview
-
additional information
-
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
-
additional information
-
enzyme AngammaGT has little hydrolase activity (cf. EC 3.4.19.13)
-
additional information
-
GGT enzymes follow a ping-pong mechanism of enzyme catalysis wherein the second substrate binds only when the first substrate is already bound to the enzyme and forms an enzyme-substrate complex. The C-alpha carboxyl group interacts with Arg109, Ser460 and Ser461 and the C-alpha amino group forms contacts with Glu438 and Asp441 while the side chain carboxylic group is oriented towards Thr399, Gly481, and Gly482. Arg109 interacts with C-alpha carboxyl group of the substrate
-
additional information
-
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket
-
Show AA Sequence and Transmembrane Helices (19739 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
110000
120000
160000
20000
200000
2000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
21000
22000
23000
25000
250000
27000
28000
30000
38000
40000
41000
42000
43000
45000
47000
48000
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
50000
54000
55000
57000
58000
61000
62000
63000
64000
66000
68000
70000
71000
80000
86000
90000
additional information
20000
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
21000
-
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
23000
-
1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
250000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
38000
-
1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
40000
-
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
70000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
90000
-
PAGE in 8 M urea, after cross-linkage of subunits with dimethylsuberimidate
additional information
-
in the presence of Triton X-100: molecular aggregation
additional information
-
amino acid sequence alignment, enzyme gene family
additional information
amino acid sequence alignment, enzyme gene family
additional information
O65652
amino acid sequence alignment, enzyme gene family
additional information
amino acid sequence alignment, enzyme gene family
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
monomer
monomer or heterodimer
tetramer
additional information
dimer
-
1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
dimer
-
1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
-
dimer
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
dimer
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
-
heterodimer
-
probably has heterodimer structure with the larger subunit of 38900 Da
heterodimer
-
1 * 46000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
heterodimer
1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
heterodimer
-
1 * 46000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
-
heterodimer
Bacillus amyloliquefaciens SMB469
-
1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
-
heterodimer
Q62WE3
in the crystal structure of BlGGT, the large subunit contains a globular domain consisting of 14 alpha-helices, six small 310 helices and 11 beta-strands, and the small subunit comprises of 3 alpha-helices, two small 310 helices and 11 beta-strands. Furthermore, both subunits provide strands to a nearly flat beta-sheet that constitutes the core of the heterodimeric arrangement. Unlike their structural consistency, the primary structure of GGT enzymes displays a great degree of variability
heterodimer
1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
heterodimer
-
in the crystal structure of BlGGT, the large subunit contains a globular domain consisting of 14 alpha-helices, six small 310 helices and 11 beta-strands, and the small subunit comprises of 3 alpha-helices, two small 310 helices and 11 beta-strands. Furthermore, both subunits provide strands to a nearly flat beta-sheet that constitutes the core of the heterodimeric arrangement. Unlike their structural consistency, the primary structure of GGT enzymes displays a great degree of variability
-
heterodimer
-
1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
-
heterodimer
-
1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
-
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
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
-
heterodimer
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
heterodimer
-
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
-
heterodimer
-
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
-
heterodimer
-
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
-
heterodimer
-
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
-
heterodimer
-
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
-
monomer or heterodimer
-
two active enzyme forms of 30000 Da and 67000 Da
monomer or heterodimer
-
two active enzyme forms of 30000 Da and 67000 Da
-
tetramer
-
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
tetramer
-
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
-
additional information
-
protease solubilization leads to a reduced MW of the larger subunit
additional information
-
the enzyme is composed of two non-identical catalytically active subunits
additional information
-
the enzyme is composed of two non-identical catalytically active subunits
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
lipoprotein
proteolytic modification
glycoprotein
-
comparison of sugar content of enzymes from tumour and normal tissue source, overview
glycoprotein
autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95. The large subunit of the enzyme contains six N-glycosylation sites (Asn-95, -120, -230, -266, -297, and -344), and the small subunit contains a single site (Asn-511)
glycoprotein
-
post-translational multiple forms differing in sugar portion
lipoprotein
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
lipoprotein
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
lipoprotein
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
lipoprotein
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
lipoprotein
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
lipoprotein
-
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
-
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
Q62WE3
the enzyme is synthetized as single-chain precursor, and then self-processes to form the mature enzyme. Analysis of autocatalytic processing of recombinant mutant enzymes expressed in Escherichia coli strain M15
proteolytic modification
A0A415J2H1
maturation mechanism of autocatalytic processing of BlGGT proceeds with residue Thr417 functioning as the activator. In the structure of T399A-BlGGT, the side-chain of Thr417 is located at a competent position to activate the catalytic threonine (Thr399) and the main chain atoms of this residue is held in position by the side chain of Arg571, which in turn interacts with the side chain of Glu398 through electrostatic interactions. Then, the side chains of Glu398 and Arg571 are held in their spatial positions by the hydrogen bond networks involving His401, Ser479, Gly481, Gly482, Thr484, Asn550, and two water molecules. In this respect, residues Gly481 and Gly482 may play a role in the autocatalytic processing of BlGGT
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 enzyme is synthetized as single-chain precursor, and then self-processes to form the mature enzyme. Analysis of autocatalytic processing of recombinant mutant enzymes expressed in Escherichia coli strain M15
-
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 enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
proteolytic modification
-
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
-
proteolytic modification
-
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
-
proteolytic modification
-
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
-
proteolytic modification
-
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
-
proteolytic modification
-
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
-
proteolytic modification
-
the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits
proteolytic modification
-
the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits
-
proteolytic modification
-
the 60000 Da proenzyme is kinetically competent to form the mature 40000 and 20000 Da subunits and exhibits maximal autoprocessing activity at neutral pH. Processing is required for enzymatic activity
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
-
rat gammaGT is synthesized as a propeptide of 568 amino acids and is cleaved to yield a stable heterodimer with a large amphipathic subunit (379 amino acids) and a smaller hydrophilic subunit (189 amino acids). gammaGT propeptide cleavage occurs within the endoplasmic reticulum
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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
ammonium sulfate precipitation from 20 mM Tris-HCl, pH 8.0, 14.2 mg/ml protein, refrigerator, 1 week
-
ammonium sulfate precipitation, hanging-drop vapor diffusion method, crystal structure of gamma-glutamyltransferase at 1.95 A resolution and structure of the gamma-glutamyl-enzyme intermediate trapped by flash cooling the GGT crystal soaked in glutathione solution and the structure of GGT in complex with L-glutamate
ammonium sulfate precipitation, hanging-drop vapor diffusion method, crystal structure of the T391A mutant gamma-glutamyltranspeptidase that lacks autocatalytic processing ability refined at 2.55 A resolution
in complex with azaserine and acivicin, at 1.65 A resolution. Both inhibitors bind to the substrate-binding pocketand form a covalent bond with the Ogamma atom of residue T391. The two amido nitrogen atoms of Gly483 and Gly484, which form the oxyanion hole, interact with the inhibitors directly or via a water molecule. In the azaserine complex the carbon atom that forms a covalent bond with Thr391 is sp3-hybridized
purified recombinant deglycosylated hGGT1 mutant V272A with bound inhibitor DON, mixing of 0.002 ml of 4.3 mg/ml protein in 50 mM HEPES, pH 8.0, 0.5 mM EDTA, 0.02% sodium azide, and 2 mM DON, with 0.0017 ml of H2O, and 0.002 ml of reservoir solution containing 20-25% PEG 3350, 0.1 M Na-cacodylate, pH 6.0, and 0.1 M ammonium chloride, microseeding with apo-hGGT1 crystals, room temperature, 1-2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, modeling using the apo-form crystals of hGGT1 (PDB ID 4Z9O) as template
purified recombinant wild-type PnGGT enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 3-5 mg/ml protein in 0.1 M HEPES, pH 7.0, with 0.001 ml reservoir solution containing 16% PEG 8000, 15% PEG 400, 0.1 M HEPES, pH 7.0, 50 mM glycylglycine, and equilibration against 0.5 ml of reservoir solution, 20°C, 1 week, method optimization, X-ray diffraction structure determination and analysis at 1.57-1.70 A resolution, molecular replacement method using the structure of Escherichia coli GGT (EcGGT, PDB ID 2DG5) as the template, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G481A
A0A415J2H1
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
G481E
A0A415J2H1
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
G481R
A0A415J2H1
site-directed mutagenesis, the mutant shows increased catalytic activity, but abolished processing
G482A
A0A415J2H1
site-directed mutagenesis, the mutant shows increased catalytic activity
G482E
A0A415J2H1
site-directed mutagenesis, the mutant shows increased catalytic activity
G482R
A0A415J2H1
site-directed mutagenesis, the mutation leads to a marked reduction in the autocatalytic processing and results in an unprocessed enzyme with insignificant catalytic activity, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity
N450A
Q62WE3
site-directed mutagenesis, the mutant shows about 4.7fold increased catalytic efficiency compared to wild-type
N450D
N450K
Q62WE3
site-directed mutagenesis, N450K exhibits 81% increase in KM and 44.3% decrease in kcat compared to wild-type, leading to a profound reduction in its catalytic efficiency
N450Q
A0A415J2H1
site-directed mutagenesis, the mutant's theanine biosynthetic activity is similar to wild-type
N450R
Q62WE3
site-directed mutagenesis, the mutant shows a significant reduction in the catalytic activity compared to wild-type
R109E
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
R109F
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
R109K
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
R109L
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
R109M
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
R109S
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
T399A
T399S
T417A
T417S
N450A
-
site-directed mutagenesis, the mutant shows about 4.7fold increased catalytic efficiency compared to wild-type
-
N450D
-
site-directed mutagenesis, the mutant shows about 8fold increased catalytic efficiency compared to wild-type
-
N450K
-
site-directed mutagenesis, N450K exhibits 81% increase in KM and 44.3% decrease in kcat compared to wild-type, leading to a profound reduction in its catalytic efficiency
-
N450R
-
site-directed mutagenesis, the mutant shows a significant reduction in the catalytic activity compared to wild-type
-
T399A
-
site-directed mutagenesis, mutant structure analysis and comparison
-
R109E
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109K
-
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
-
R109L
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
-
R109M
-
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
-
R109S
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109E
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
R109K
-
site-directed mutagenesis of the catalytic residue results in low enzyme consumption, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Lys mutant has increased transpeptidation activity and catalytic efficiency compared to the other R109 mutants. The Arg109Lys mutant shows high conversion rates for L-theanine synthesis as well
-
R109L
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln, highly reduced transpeptidase activity compared to wild-type
-
R109M
-
site-directed mutagenesis of the catalytic residue results in reduced activity and high salt stability of the mutant, the mutation reduces the enzyme's affinity for L-Gln. The Arg109Met mutant shows increased hydrolytic activity as it completely alters the binding of L-Gln at the active site. Also, the salt stability of the mutant enzyme is significantly improved. Highly reduced transpeptidase activity compared to wild-type
-
R109S
-
site-directed mutagenesis, the mutation reduces the enzyme's affinity for L-Gln
-
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
D433N
-
mutation enables gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocepha-losporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins
S463D
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
S463K
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
T391A
mutant protein without intramolecular autocatalytic processing activity
T353A
T380A
-
mutant enzyme can not process even after 30 days at 37 °C, no enzymatic activity
T380S
-
mutant enzyme is strongly impaired with respect to processing. Prolonged incubation (more than 30 days) at 37°C leads to complete maturation of the T380S mutant. Vmax for hydrolysis of 5-L-glutamyl-4-nitroanilide is 8.8fold lower than wild-type enzyme. Vmax for transpeptidation of 5-L-glutamyl-4-nitroanilide of Gly-Gly
H383A
-
site-directed mutagenesis of conserved His383 residue, 3fold reduced activity and 62% reduced Vmax, altered binding of acceptor
K562S
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type: the mutant's affinity towards Gly-Gly dramatically decreases to 2.0% of wild-type level, whereas it retains 45% of wild-type hydrolytic activity
K568S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N120Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N230Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N266Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N297Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a slightly decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N344Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N511Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N95Q
the mutation results in an 8fold decrease in the cleavage efficiency of the propeptide
N95Q/N120Q/N230Q/N266Q/N297Q/N344Q/N511Q
total N-glycosylation knock-out mutant
H369N
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
R346A
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
R346E
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
Y327E
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
Y327N
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate. The mutant enzyme retains more than 90% transpeptidase activity in the presence of Ba2+, Ca2+, Cu2+, Mg2+, Mn2+, and Zn2+ and is completely inhibited by Cd2+, Co2+, Fe2+, Hg2+, Ni2+ and Pb2+
Y349D
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
H369N
Picrophilus oshimae DSM 9790
-
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
R346A
Picrophilus oshimae DSM 9790
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
R346E
Picrophilus oshimae DSM 9790
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
Y327E
Picrophilus oshimae DSM 9790
-
mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate
-
Y327N
Picrophilus oshimae DSM 9790
-
mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate. The mutant enzyme retains more than 90% transpeptidase activity in the presence of Ba2+, Ca2+, Cu2+, Mg2+, Mn2+, and Zn2+ and is completely inhibited by Cd2+, Co2+, Fe2+, Hg2+, Ni2+ and Pb2+
-
F417Y
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
W385T
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
W525A
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
F417Y
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
W385T
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
W525A
-
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type
-
additional information
N450D
Q62WE3
site-directed mutagenesis, the mutant shows about 8fold increased catalytic efficiency compared to wild-type
N450D
A0A415J2H1
site-directed mutagenesis, the mutant shows increased theanine biosynthetic activity compared to wild-type
T399A
Q62WE3
site-directed mutagenesis, mutant structure analysis and comparison
T399A
A0A415J2H1
site-directed mutagenesis, like the wild-type protein, T399A-BlGGT has a stacked alphabetaalphabeta core structure comprising two central beta-sheets and surrounding alpha-helices
T399A
A0A415J2H1
site-directed mutagenesis, precursor mimic mutant, structure analysis
T399S
-
precursor is able to precede a time-dependent autocatalytic process to generate the 44.9 and 21.7 kDa subunits of mature enzyme
T417A
-
precursor is able to precede a time-dependent autocatalytic process to generate the 44.9 and 21.7 kDa subunits of mature enzyme, processed enzyme lacks activity
T417S
-
precursor is able to precede a time-dependent autocatalytic process to generate the 44.9 and 21.7 kDa subunits of mature enzyme
T353A
-
mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
T353A
-
mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
-
additional information
-
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
O65652
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
-
expression of full length gene and six truncations lacking 36, 129, 132, 135, 144, and 174 bp, respectively, at the 5' end in Escherichia coli. Mutant proteins derived from genes lacking 135 and 144 bp show no enzymatic activity. Mutants derived of truncations of 36. 129, 132 process autocatalytically their precursors into alpha- und beta-subunits at 4°C
additional information
deletion of up to nine amino acid residues from the C-terminal end of the enzyme definitely affects its autocatalytic activity
additional information
-
deletion of up to nine amino acid residues from the C-terminal end of the enzyme definitely affects its autocatalytic activity
additional information
Q62WE3
molecular modeling of mutant enzymes using the X-ray crystal structures of BlGGT (PDB ID 4OTT) and T399A-BlGGT (PDB ID 4Y23) as templates. GdnHCl-induced denaturation of BlGGT and its variants, overview
additional information
-
molecular modeling of mutant enzymes using the X-ray crystal structures of BlGGT (PDB ID 4OTT) and T399A-BlGGT (PDB ID 4Y23) as templates. GdnHCl-induced denaturation of BlGGT and its variants, overview
additional information
easy and efficient method for GGT enzyme immobilization, preparation of thermo- and salt-tolerant chitosan cross-linked gamma-glutamyl transpeptidase from Bacillus licheniformis strain ER15, overview. The purified native enzyme is covalently immobilized onto chitosan microspheres (CMS) standardized with respect to pH, enzyme load, and time. Immobilization efficiency of 11.9 U/mg dry weight of microsphere is obtained in Tris-HCl, pH 9.0, at 18°C in 4 h. Immobilized enzyme CMS-GGT exhibits improved thermal stability (t1/2 of 70.7 min at 60°C), activity in a broader pH range and improved salt stability in 18% (3 M) sodium chloride solution as compared to free enzyme. Both free and immobilized enzymes specifically convert glutamine to glutamic acid in a mixture of amino acids. CMS-GGT has a better shelf life and high recyclability retaining 90% catalytic efficiency up to 10 reaction cycles compared to free enzyme. For long-term storage, CMS-GGT can be disinfected using either sodium azide or sodium hypochlorite solution without affecting the enzyme activity
additional information
A0A415J2H1
the transpeptidase-specialized mutants (N450D and N450Q) of enzyme GGT are employed for the biocatalytic synthesis of L-theanine (gamma-glutamyl-L-ethylamide). Preparative biocatalytic synthesis of L-theanine from a reaction mixture of L-Gln, ethanolamine, and borate buffer, pH 10.5, 37°C. Use of L-theanine as one kind of gamma-glutamyl donor for the transpeptidation action by the enzyme. The L-theanine production by wild-type BlGGT, mutant N450D, and mutant N450Q at pH 10.5 results in the individual yields of 56, 88, and 61%, respectively. The product yield is proportionally increased with the L-Gln concentration and reaches a maximum at a donor substrate concentration of 250 mM
additional information
-
deletion of up to nine amino acid residues from the C-terminal end of the enzyme definitely affects its autocatalytic activity
-
additional information
-
easy and efficient method for GGT enzyme immobilization, preparation of thermo- and salt-tolerant chitosan cross-linked gamma-glutamyl transpeptidase from Bacillus licheniformis strain ER15, overview. The purified native enzyme is covalently immobilized onto chitosan microspheres (CMS) standardized with respect to pH, enzyme load, and time. Immobilization efficiency of 11.9 U/mg dry weight of microsphere is obtained in Tris-HCl, pH 9.0, at 18°C in 4 h. Immobilized enzyme CMS-GGT exhibits improved thermal stability (t1/2 of 70.7 min at 60°C), activity in a broader pH range and improved salt stability in 18% (3 M) sodium chloride solution as compared to free enzyme. Both free and immobilized enzymes specifically convert glutamine to glutamic acid in a mixture of amino acids. CMS-GGT has a better shelf life and high recyclability retaining 90% catalytic efficiency up to 10 reaction cycles compared to free enzyme. For long-term storage, CMS-GGT can be disinfected using either sodium azide or sodium hypochlorite solution without affecting the enzyme activity
-
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
additional information
GGT enzyme-defective Bacillus subtilis mutant strain 2288
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
-
additional information
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
-
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
-
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
-
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
-
additional information
-
deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032
-
additional information
construction of truncation mutants lacking 11, 17, 18, 20 and 26 amino acids at the N-terminus. Mutants lacking 11 and 17 amino acids show about 10% reduction in specific activity, mutants lacking 18 or more amino acids show a complete loss of activity
additional information
-
construction of truncation mutants lacking 11, 17, 18, 20 and 26 amino acids at the N-terminus. Mutants lacking 11 and 17 amino acids show about 10% reduction in specific activity, mutants lacking 18 or more amino acids show a complete loss of activity
additional information
immobilization of recombinant enzyme on 3% sodium alginates inpresence of 2% CaCl2, immobilized recombinant gamma-glutamyltranspeptidase cells exhibit favourable operational stability for enzymatic synthesis of gamma-glutamylmethylamide from L-glutamylhydrazine and methylamine, usage of L-glutamylhydrazine as an economical substrate, immobilized gamma-glutamyltranspeptidase cells are used for 10 reaction cycles, and the average conversion ratio from L-glutamylhydrazine to gamma-glutamylmethylamide reaches 93.2%. No inhibition by 200 mM L-glutamylhydrazine
additional information
-
cells overexpressing gamma-GT exhibit a low susceptibility to arsenic trioxide-induced apoptosis, associated with low reactive oxygen species induction and increased catalase activity
additional information
-
in transfected melanoma cells, higher levels of GGT activity are associated with higher levels of background DNA damage and oxidized bases. GGT-over-expressing cells also present with a markedly higher glucose uptake, potentially leading to higher metabolic rate and oxidative DNA damage. When GGT-over-expressing cells are incubated in the presence of GGT substrates and a source of catalytic iron, increased levels of DNA damage and oxidized bases are observed
additional information
the N-terminal anchor domain of enzyme GGT is truncated, human GGT protein without the anchor domain is expressed as a soluble enzyme, and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain. The wild-type human GGT is expressed as a mature protein by autocatalytic processing during the period of infection. The autocatalytic process of K562S mutant is somewhat slow and is not enough under the same conditions, but the successful processing is attained by giving additional processing period for the purification step
additional information
-
the N-terminal anchor domain of enzyme GGT is truncated, human GGT protein without the anchor domain is expressed as a soluble enzyme, and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain. The wild-type human GGT is expressed as a mature protein by autocatalytic processing during the period of infection. The autocatalytic process of K562S mutant is somewhat slow and is not enough under the same conditions, but the successful processing is attained by giving additional processing period for the purification step
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
25°C, 7 h, 80% activity or higher is retained at pH 7.0-10.0 and, in all cases, it is above 50% at pH 5.0-11.0
5 - 12
free and immobilized enzymes, stable at with 90-100% activity remaining
6 - 11
-
pH stabilities of free GGT, immobilized MTWs-GGT, and immobilized modified MTWs-GGT-Phar, overview
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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
37 - 77
in both the transpeptidation and hydrolysis reactions, wild type enzyme exhibits full activity up to 47°C. At temperatures greater than 62°C, the wild type enzyme is rendered completely inactive
40
40 - 50
-
there is hardly any activity loss of the purified recombinant enzyme after preincubation at 40 °C for 72 h, but the activity drops to 7.5% after preincubation for 8 h at 50°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
45
50
56
58
59.5 - 70
A0A415J2H1
the melting temperature of enzyme BlGGT is around 59.5°C, the irreversible denaturation of this enzyme occurs at 70°C
60
additional information
45
24 h, no loss of gamma-L-glutamyl-4-nitroanilide hydrolase activity
60
-
the monomeric 30-kDa enzyme has a half-life of 240 min and 120 min at 60°C in the absence and presence of subtilisin, respectively. The heterodimeric 67-kDa enzyme has a half-life of 20 min at 60°C in the absence of subtilisin
60
t1/2: 30 min, gamma-L-glutamyl-4-nitroanilide hydrolase activity
additional information
melting temperature of enzyme GGT1 is 53-58°C depending on the buffer system and pH used, while with bound inhibitor 6-diazo-5-oxo-L-norleucine, the mellting temperature is 69-72°C, overview. The unbound enzyme is most stable in Na-citrate, pH 6.7, the inhibitor-bound enzyme in HEPES, pH 7.0
additional information
-
melting temperature of enzyme GGT1 is 53-58°C depending on the buffer system and pH used, while with bound inhibitor 6-diazo-5-oxo-L-norleucine, the mellting temperature is 69-72°C, overview. The unbound enzyme is most stable in Na-citrate, pH 6.7, the inhibitor-bound enzyme in HEPES, pH 7.0
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
GdnHCl-induced denaturation of BlGGT and its variants, overview
Q62WE3
retains 88% of its activity over 15 h and 72% of the activity after 30 h, while where the free enzyme retains 73% of its activity over 15 h and almost half of the activity lost after 30 h at 37° and pH 10.0
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
-
the immobilized enzyme shows a higher stability as compared to soluble enzyme. The immobilized enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
40°C, purified recombinant extracellular enzyme, 72 h, 90% of initial activity remaining, and more than 50% of initial activity after being maintained at different pH values for 24 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-Sepharose anion exchange chromatography
from hyperplastic hepatic nodules, Yoshida ascites hepatoma, primary hepatoma, kidney
-
from normal and cirrhotic liver and 6 isoforms from serum of patients with cellular hepatic carcinoma
-
N-terminal His-tagged enzyme is purified by ammonium sulfate precipitation and Sephacryl S-200 gel filtration
native enzyme 40.7fold from leaves by ammonium sulfate fractionation, dialysis, and gel filtration
-
native enzyme from bulbs by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration
native extracellular enzyme 4.6fold from Bacillus licheniformis strain ER15 by ultrafiltration, gel filtration, ion exchange chromatography, and dialysis, with 50.11% yield
one-step purfication, Ni-NTA affinity chromatography utilizing C-terminal His6 tag
one-step purification, Ni-NTA affinity chromatography utilizing N-terminal His6 tag
-
partial
partial from mammary-tumour virus and from milk fat-globule membranes, in presence of Triton X-100
-
partial from pancreas and pancreatic carcinoma and pancreatic carcinoma cell line HPC-Y1
-
recombinant
recombinant enzyme
recombinant extracellular C-terminally His6-tagged enzyme 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
-
recombinant His-tagged GGT from Escherichia coli strain M15 by nickel affinity chromatography
A0A415J2H1
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography
Q62WE3
recombinant His-tagged wild-type and mutant GGT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged eextracellular enzyme from Bacillus subtilis strain 168 by nickel affinity chromatography
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain M15 to near homogeneity by nickel affinity chromatography
A0A415J2H1
recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography and ultrafiltration, to homogeneity
recombinat GgtB N-terminally tagged with chitin-binding domain and intein tag from Escherichia coli strain ER25669 by chitin affinity chromatography and ultrafiltration
Triton X-100 solubilized liver enzyme is hydrophobic, papain-solubilized liver enzyme is hydrophilic
-
two-step purification, ammonium sulfate precipitation and chromatofocusing
two-step purification, DEAE cellulofine and Butyl FF column chromatography
-
native enzyme from bulbs by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration
native enzyme from bulbs by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration
one-step purfication, Ni-NTA affinity chromatography utilizing C-terminal His6 tag
-
one-step purfication, Ni-NTA affinity chromatography utilizing C-terminal His6 tag
-
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
a truncated Escherichia coli Novablue gamma-glutamyltranspeptidase gene lacking the first 48-bp coding sequence for part of the signal sequence is amplified by polymerase chain reaction and cloned into expression vector pQE-30 to generate pQE-EcGGT. The maximum production of His6-tagged enzyme by Escherichia coli M15 is achieved with 0.1 mM IPTG induction for 12 h at 20°C
-
cloning of liver specific isoform III from fetal mRNA, screening of rat genetic library, single copy gene, DNA, including enhancer and promotor, sequence determination, plasmid construction and expression in Escherichia coli, transient enzyme expression in hepatoma cell lines, dependent on differentiation state of the cells
-
expression in Escherichia coli
expression in gamma-glutamyltransferase deficient Escherichia coli K-12
expression of recombinant wild-type and mutants in Spodoptera frugiperda Sf21 cells via baculovirus infection
-
expression of wild-type and mutant lacking the putative signal sequence/anchor domain, amino acid 1-27, in Spodoptera frugiperda Sf21 cells via baculovirus infection
-
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 blggt, recombinant overexpression of extracellular enzyme in Escherichia coli strain BL21(DE3) in bioreactor under batch and fed-batch condition, development and optimization of a cost-effective method for overexpression and preparation of bacterial GGT enzyme for its industrial applications, method optimization, overview. The native signal is used for extracellular expression of the enzyme in Escherichia coli. Enzyme activity of 24500 U/l in the extracellular medium after 24 h. Subcloning in Escherichia coli strain DH5alpha, expression studies in Escherichia coli strains M!5 and BL21(DE3)
gene BsGGT168, sequence comparisons, recombinant expression of extracellular C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ggt, recombinant expression of His-tagged enzyme GGT in Escherichia coli strain M15
A0A415J2H1
gene ggt, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-pET22b
-
gene ggt, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain M15, subcloning in Escherichia coli strain XL-1 Blue
A0A415J2H1
gene ggt, recombinant expression of His6-tagged enzyme in Bacillus subtilis strain 168 (pHT43-spAmyQ-ggtDELTAsp) under control of the Plac promoter, extracellular secretion, subcloning in Escherichia coli strain DH5alpha, method optimization. Dual-signal peptides promote more secretion than a single signal peptide
-
gene ggt, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain M15, the recombinant BlGGT confers the ability to catalyze the synthesis of gamma-L-glutamyl-S-allyl-L-cysteine, gamma-glutamyl-L-phenylalanine, and gamma-glutamyl-L-leucine
A0A415J2H1
gene ggt, recombinant expression of wild-type and K562S mutant enzymes in Spodoptera frugiperda Sf9 cells via baculovirus transfection method
gene ggt, recombinant overexpression of wild-type and mutant enzymes
gene ggt, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15
Q62WE3
gene ggt, sequence comparisons, recombinant expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene GGT1, recombinant expression of enzyme mutant V272A in Pichia pastoris strain X-33
gene GGT3, Vitis vinifera appears to contain only a single GGT gene, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, transient functional recombinant overexpression of GFP-tagged enzyme in Allium cepa cells and in Nicotiana benthamiana leaves via transformation with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR exxpression analysis
gene ggtB, recombinat expression of GgtB with an N-terminal fusion of the chitin-binding domain and intein tag to the target protein, subcloning in Escherichia coli strain DH5alphaMCR and subsequently transformation into and expression in Escherichia coli strain ER25669
generation of transgenic mice that overexpress gamma-glutamyltransferase in a tissue-specific manner utilizing the Cre-loxP recombination system. Systemic as well as local production of gamma-glutamyltransferase accelerates osteoclast development and bone resorption in vivo by increasing the sensitivity of bone marrow macrophages to receptor activator of nuclear factor-kappaB ligand, an essential cytokine for osteoclastogenesis. Mutated gamma-glutamyltransferase devoid of enzyme activity is as potent as the wild-type molecule in inducing osteoclast formation, suggesting that gamma-glutamyltransferase acts not as an enzyme but as a cytokine
-
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
-
overexpression as His-tagged protein in Escherichia coli JM109, DNA sequence analysis
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
the enzyme is overexpressed under the control of a constitutive Histoplasma capsulatum-native promoter
-
the structural gene encoding GGTII is amplified from the genomic DNA of the fission yeast and ligated into the shuttle vector pRS316 to generate the recombinant plasmid pPHJ02. The Schizosaccharomyces pombe cells harboring plasmid pPHJ02 show about 4fold higher GGT activity in the exponential phase than cells harboring the vector only
transfection of Me665/2/21 human melanoma cell, DU145 human prostatic carcinoma cell, and BEAS-2B human bronchial epithelial cell
-
transient overexpression in Nicotiana benthamiana leaf and in onion cells
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
at pH 4.0, the bacterium augments enzyme production in the presence of glutamine (about 10 mM) in the medium, which predominantly occurs after a 6-min time-lag
exposure to cadmium increases the activities of both gammaglutamyl transferase and glutathione transferase 2
-
GGT3 transcript in whole berries is upregulated upon Botrytis cinerea infection as well as mechanical damage to leaf tissue
isoform GGT2 expression is enhanced in ggt1 knockout mutants, suggesting a compensatory effect to restore enzyme activity in the root apoplast. Supplementation with 0.1 mM glutathione results in the 4fold up-regulation of isoform GGT2 gene expression
the VvGGT3 transcript in whole berries is upregulated upon Botrytis cinerea infection as well as mechanical damage to leaf tissue. In comparison to Botrytis infection, there is only a mild about 2.0fold increase in the relative transcript abundance of VvGGT3in mechanically wounded leaves compared to the unwounded control leaves at 6 h post wounding beacoming significantly different after 12 h
tumor necrosis factor TNFalpha induces GGT promoter transactivation, mRNA and protein synthesis, as well as enzymatic activity. Remicade, a clinically used anti-TNFalpha antibody, small interfering RNA against p50 and p65 nuclear factor NF-kB isoforms, curcumin, a well characterized natural NF-kB inhibitor, as well as a dominant negative inhibitor IkBa, prevent GGT activation at various levels. Over-expression of receptor of TNFalpha-1, TNFR-associated factor-2 TRAF2, TNFR-1 associated death domain TRADD, dominant negative IkBa or NF-kB p65 further confirm GGT promoter activation via NF-kB.Mutation of the NF-kB site located at 110 additionally inhibits TNFalpha-induced promoter induction
-
at pH 4.0, the bacterium augments enzyme production in the presence of glutamine (about 10 mM) in the medium, which predominantly occurs after a 6-min time-lag
-
at pH 4.0, the bacterium augments enzyme production in the presence of glutamine (about 10 mM) in the medium, which predominantly occurs after a 6-min time-lag
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation as catalytically active enzyme after inactivation with 6-diazo-5-oxo-L-norleucine, requires glutathione or S-methyl derivative as a substrate ligand, circular dichroic spectra
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
drug development
development of 5-thiohistidine derivatives as therapeutics for GGT-positive tumors
food industry
medicine
nutrition
pharmacology
synthesis
analysis
-
plasma layer stratification might occur in primary lithium-heparin tubes for a limited number of routine clinical chemistry tests, introducing a statistically significant bias in the measurement of gamma-glutamyltransferase, lactate dehydrogenase, triglycerides and C-reactive protein in the upper vs. the bottom section. When delayed testing is necessary for these parameters, plasma should be separated after centrifugation and appropriately mixed before delayed/repeated analysis or aliquoting
analysis
assays for gamma-glutamyl transferase (GGT1) activity in blood are widely used in a clinical setting to measure tissue damage
analysis
-
GGT level is a good predictor of low coronary flow reserve at the receiver-operating characteristic curve
analysis
-
gamma-glutamyltransferase can be used as a marker related with oxidative stress
analysis
-
analytical method for the selective determination and speciation of S-nitrosoglutathione and its metabolite S-nitrosocysteinylglycine, based on liquid chromatography separation coupled to on-line enzymatic hydrolysis of S-nitrosoglutathione by commercial GGT. The limit of quantitation for S-nitrosoglutathione and S-nitrosocysteinylglycine in plasma ultrafiltrate is 5 nM, with a precision of 1-6% within the 5-1500 nM dynamic linear range. The method is applied to evaluate the recovery of exogenous S-nitrosoglutathione after addition of aliquots to human plasma samples presenting with different total GGT activities. By inhibiting GGT activity in a time-dependent manner, the recovery of S-nitrosoglutathione is inversely correlated with plasmatic levels of endogenous GGT
analysis
-
simple, robust and highly sensitive assay based on an alpha-phenylthio-containing glutathione peptide mimic gamma-glutamyl-D,L-phenylthioglycylglycine that eliminates thiophenol upon GGT-catalyzed hydrolysis of the c-glutamyl peptide bond
diagnostics
the GGT enzyme is known as a diagnostic enzyme for liver and biliary related diseases
diagnostics
-
direct detection of GGT activity can provide critical information for the diagnosis of several pathologies. Elevated serum GGT levels are a general marker of diseases affecting the liver
diagnostics
-
serum gamma-glutamyltranspeptidase activity is typically elevated in biliary atresia. In approximately 12%-25% of cases, gamma-glutamyltranspeptidase is normal or low. Normal or low gamma-glutamyltranspeptidase in patients with biliary atresia is associated with a worse prognosis
diagnostics
-
the abnormal gamma-glutamyl transferase in biliary cholangitis and cholestasis drug-induced liver injury is associated with cholestasis. In alcoholic liver disease, it is associated with both oxidative stress and cholestasis, and in non-alcoholic fatty liver disease, it is associated with oxidative stress. gamma-Glutamyl transferase levels have different characteristics in different liver diseases, which are closely related to the pathogenesis of liver diseases
diagnostics
-
the GGT enzyme is known as a diagnostic enzyme for liver and biliary related diseases
-
food industry
GGT has gained importance as a biotechnologically important catalyst in food sector. In food sector, GGT enzyme finds application in soy sauce industry, debittering of amino acids, synthesis of flavor enhancer, and nutraceutical peptides such as L-theanine
food industry
-
development of an enzymatic method involving Bacillus licheniformis GGT (BlGGT) for the synthesis of gamma-glutamyl-L-leucine (gamma-Glu-Leu) from glutamine and leucine, since the mass production of Kokumi peptides from natural resources in high purity generally involves several tedious and inefficient operation processes. Parameter optimization of the BlGGT-catalyzed reaction for the biocatalytic synthesis of this Kokumi-imparting molecule
food industry
some essential amino acids like Phe, Leu, Val and His, taste bitter when consumed orally. The addition of gamma-glutamyl moiety to these amino acids using Escherichia coli K-12 gamma-glutamyltransferase has been reported to dramatically reduce their bitterness and improve their taste preference due to the introduction of a refreshing sour flavor, making them suitable for oral consumption as amino acid supplements
food industry
-
some essential amino acids like Phe, Leu, Val and His, taste bitter when consumed orally. The addition of gamma-glutamyl moiety to these amino acids using Escherichia coli K-12 gamma-glutamyltransferase has been reported to dramatically reduce their bitterness and improve their taste preference due to the introduction of a refreshing sour flavor, making them suitable for oral consumption as amino acid supplements
-
food industry
-
GGT has gained importance as a biotechnologically important catalyst in food sector. In food sector, GGT enzyme finds application in soy sauce industry, debittering of amino acids, synthesis of flavor enhancer, and nutraceutical peptides such as L-theanine
-
medicine
-
bioconversion of cytotoxic and mutagenic agents to inactive 5-L-glutamyl-derivatives
medicine
-
gamma-glutamyltransferase might be an additional marker of arterial stiffness, especially in men, though the relationship with arterial stiffness is very weak
medicine
-
gamma-glutamyltransferase is associated with mortality in both men and women, especially in patients younger than 30 years. Even high-normal gamma-glutamyltransferase is a risk factor for all-cause mortality
medicine
-
GSTM1- and GSTM1-/GSTT1- genotypes may be a genetic risk factor for the increase of GGT in Japanese epileptic patients treated with valproic acid patients. It is not possible to clarify whether the GGT increase is caused by valproic acid-induced hepatotoxicity or not
medicine
-
the use short, simple questionnaires, combined with that of low-cost biochemical markers, such as gamma-glutamyltransferase, can serve as an initial screening for alcohol-related problems, especially for employees in hazardous occupations
medicine
-
gamma-glutamyltransferase levels may be a surrogate marker of insulin resistance, inflammation and metabolic syndrome
medicine
-
GGT, a predictor of type 2 diabetes, is associated with a risk of incident metabolic syndrome
medicine
-
level of GGT may be a useful marker to determine appropriate amounts of drinking for individuals
medicine
-
serum GGT is specifically associated with the visceral fat area, but not with the subcutaneous fat area, suggests that the serum GGT may be useful as a convenient indicator of visceral fat area in the clinical treatment of obesity
medicine
-
gender-specific clusters including mean corpuscular erythrocyte volume, carbohydrate-deficient transferrin, gamma-glutamyltransferase, homocysteine and folate led to an increase in sensitivity compared to single laboratory markers. This is a reliable help to identify patients with regular heavy drinking in clinical practice which might prevent further complications
medicine
-
given the involvement of GGT in bone and joint diseases characterized by accelerated osteoclast development, GGT may be a novel target for the development of diagnostics and therapeutics
medicine
-
habitual coffee consumption is associated with lower incidence of type II diabetes particularly in those with higher baseline serum GGT levels
medicine
-
high serum gamma-glutamyltransferase is associated with an increased risk of liver cancer
medicine
-
high gamma-glutamyltransferase levels significantly increased cancer risk in women
medicine
-
retreatment with PegIFN-alpha-2b and ribavirin for a minimum of 48 weeks should be considered in all patients with chronic hepatitis C unresponsive to previous IFN-based therapies. Baseline gamma-glutamyltransferase values and rapid virological response are highly predictive for retreatment outcome
medicine
-
the early detection of alcohol consumption (EDAC) test shows better performance than gamma-glutamyltransferase to detect heavy drinking in a large population of males and females
medicine
-
gamma-glutamyltransferase is a strong predictor of metabolic syndrome. Lipid peroxide measured by tert-butyl hydroperoxide-initiated chemiluminescence and gamma-glutamyltransferase activity are reliable markers of oxidative stress in this syndrome
medicine
-
gamma-glutamyltransferase is positively associated with incident coronary heart disease and stroke in both women and men in European populations and among self-reported nondrinkers. Therefore, gamma-glutamyltransferase levels probably also reflect other biological processes or indeed lifestyle or dietary behaviors that are linked to cardiovascular disease
medicine
-
gamma-glutamyltransferase is a useful as an indirect marker of liver disease
medicine
-
a longitudinal increase in GGT, independently of baseline GGT and even within its normal range, significantly increases risk of fatal cardiovascular disease
medicine
-
the modest elevation of GGT in overweight children may be of pathophysiological importance in the long term
medicine
-
elevated GGT is significantly associated with increased cancer risk in men
medicine
-
serum GGT within its normal range can predict cardiovascular diseases mortality in those aged less than 70 years, but may have limited usefulness for risk assessment in older adults
medicine
-
elevated gamma-glutamyltransferase is associated with significantly increased risk of stroke, fatal coronary heart disease events and cardiovascular disease mortality independent of established cardiovascular disease risk factors and may be a useful additional marker for long-term cardiovascular disease
medicine
-
gamma-glutamyltransferase is confirmed as independent risk factor in patients with established coronary artery disease. gamma-Glutamyltransferase, C-reactive protein, fasting glucose show an additive prognostic value, whereas low values of these biomarkers identify a subset of patients with the lowest risk of cardiac death
medicine
-
study on the association between gamma-GT and disability pension in a cohort of construction workers. gamma-GT is a strong risk indicator of all-cause occupational disability even at levels of gamma-GT in the normal range and is in particular associated with disability pension due to diseases of the digestive system, musculoskeletal disorders, cardiovascular, and mental diseases
medicine
-
GGT levels are higher in patients with coronary artery disease than in control. GGT activity and c-reactive protein levels are higher, left ventricular ejection fraction is lower in patients with acute coronary syndrome compared with stable coronary artery disease group. The increased GGT activity is related to left ventricular function, clinical stability, and inflammatory activity rather than the severity of coronary artery disease. Measurement of GGT activity may be useful in predicting cardiovascular risk
medicine
-
direct detection of GGT activity can provide critical information for the diagnosis of several pathologies. GGT may serve as a tumor biomarker and its presence on the cell surface is particularly attractive for imaging applications
medicine
development of 5-thiohistidine derivatives as therapeutics for GGT-positive tumors
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
nutrition
-
the enzyme is suitable for food fermentation under high salt conditions, e.g. the fermentation of soy sauce and miso
-
pharmacology
-
the administration of a single intraperitoneal dose of potassium dichromate decreases the activity of gamma-glutamyl transpeptidase and alanine aminopeptidase. Utility of gamma-GT and AAP activities as biomarkers in the evaluation of the Cr-induced nephrotoxicity
pharmacology
-
cisplatin administration significantly elevates blood urea nitrogen and serum creatinine in male rats day 5 post-treatment. Inhibition of gamma glutamyltranspeptidase prevents cisplatin nephrotoxicity, but not cellular toxicity in rat proximal tubular cultures
pharmacology
-
cisplatin administration significantly elevates blood urea nitrogen and serum creatinine in mice day 4 post-treatment. Inhibition of gamma glutamyltranspeptidase prevents cisplatin nephrotoxicity
pharmacology
-
bile extracts from diclofenac-dosed rats at 200 mg/kg, show the presence of the gamma-GT-mediated diclofenac-S-acyl-glutathione degradation product diclofenac-N-acyl-cysteinylglycine, where a total of 8 microg is excreted 6 h postadministration. When diclofenac-S-acyl-glutathione is incubated with gamma-GT, the GSH adduct is degraded in a linear time-dependent fashion
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
synthesis
-
synthesis of theanine from 5-L-glutamyl-4-nitroanilide and ethylamine
synthesis
in pharmaceutical and medical sectors GGT enzyme can be exploited in the synthesis of pro-drugs and therapeutic compounds such as gamma-glutamyl DOPA, gamma-D-glutamyl-L-tryptophan, and gamma-glutamyl-taurine
synthesis
-
high potentiality of BlGGT-catalyzed reaction in the synthesis of gamma-glutamyl compounds in variety of biotechnological and pharmaceutical applications
synthesis
-
the recombinant extracellular enzyme is used for enzymatic synthesis of L-theanine, which is performed at optimal conditions: 20 mM L-Gln, 100 mM ethylamine-HCl, 0.5 U/ml BaGGT, incubated at 40°C for 6 h, 200 rpm
synthesis
A0A415J2H1
using recombinant Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) in a straightforward procedure for the biocatalytic synthesis of gamma-glutamyl-phenylalanine (gamma-Glu-Phe), qualitative analysis of reaction products, mass spectrometry/nuclear magnetic resonance analyses
synthesis
operational stability and economical use of gamma-glutamyltransferase in the L-theanine synthesis process is improved by immobilizing gamma-glutamyltransferase on a prepared oxidized cellulose nanofiber membrane. L-Theanine could be accumulated over 70 g/l within 18 h via a simple fed-batch conversion
synthesis
the enzyme is employed in enzymatic synthesis of L-theanine, gamma-glutamyl-taurine or gamma-D-glutamyl-L-tryptophan (an immunomodulatory dipeptide with broadspectrum stimulatory activities)
synthesis
-
operational stability and economical use of gamma-glutamyltransferase in the L-theanine synthesis process is improved by immobilizing gamma-glutamyltransferase on a prepared oxidized cellulose nanofiber membrane. L-Theanine could be accumulated over 70 g/l within 18 h via a simple fed-batch conversion
-
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
-
synthesis
-
synthesis of theanine from 5-L-glutamyl-4-nitroanilide and ethylamine
-
synthesis
-
the enzyme is employed in enzymatic synthesis of L-theanine, gamma-glutamyl-taurine or gamma-D-glutamyl-L-tryptophan (an immunomodulatory dipeptide with broadspectrum stimulatory activities)
-
synthesis
-
the recombinant extracellular enzyme is used for enzymatic synthesis of L-theanine, which is performed at optimal conditions: 20 mM L-Gln, 100 mM ethylamine-HCl, 0.5 U/ml BaGGT, incubated at 40°C for 6 h, 200 rpm
-
synthesis
-
in pharmaceutical and medical sectors GGT enzyme can be exploited in the synthesis of pro-drugs and therapeutic compounds such as gamma-glutamyl DOPA, gamma-D-glutamyl-L-tryptophan, and gamma-glutamyl-taurine
-
EXTERNAL LINKS (specific for EC-Number 2.3.2.2)
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Release 2026.1 (March 2026)
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