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Information on EC 2.3.2.2 - gamma-glutamyltransferase
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2.3.2.2 gamma-glutamyltransferaseIUBMB Comments
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
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- 2.3.2.2
- aminotransferase
-
alt
- bilirubin
- cholesterol
- albumin
- triglyceride
- bile
- biliary
- women
- creatinine
- gsh
- transaminase
- hepatocytes
- cirrhosis
- fibrosis
- urinary
- cholestasis
- duct
-
uric
-
c-reactive
- steatosis
- aminopeptidase
- jaundice
-
drinkers
-
hepatotoxicity
-
non-alcoholic
-
intrahepatic
- nafld
-
nephrotoxicity
-
ursodeoxycholic
-
waist
-
ultrasonography
- diethylnitrosamine
-
circumference
-
corpuscular
-
hepatocarcinogenesis
-
abuse
-
hepatectomy
- hepatobiliary
- phenobarbital
-
preneoplastic
- alpha-fetoprotein
-
homa-ir
-
abstinence
- pruritus
- 2-acetylaminofluorene
-
n-acetyl-beta-d-glucosaminidase
- cholangitis
-
cholangiopancreatography
- pharmacology
-
elastography
- diagnostics
- nutrition
- food industry
- drug development
- analysis
- medicine
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a (5-L-glutamyl)-peptide
+
=
+
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
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
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
active site
-
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
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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
ping-pong bi bi mechanism
-
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
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
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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
mechanism
-
-
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
structure
-
-
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
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