2.3.2.2: gamma-glutamyltransferase
This is an abbreviated version!
For detailed information about gamma-glutamyltransferase, go to the full flat file.
Word Map on EC 2.3.2.2
-
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
- 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
Synonyms
(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase, alpha-glutamyl transpeptidase, AngammaGT, AsGGT1, At1g69820, At4g29210, At4g39640, At4g39650, BaGGT, BaGGT42, BaGGT469, BlGGT, BlGGT13, BsGGT168, Cgl0954, eqGGT, gamma glutamyl transferase, gamma-glutamyl peptidyltransferase, gamma-glutamyl transferase, gamma-glutamyl transferase 1, gamma-glutamyl transferase 5, gamma-glutamyl transferase/transpeptidase, gamma-glutamyl transferases, gamma-glutamyl transpeptidase, gamma-glutamyl transpeptidase 1, gamma-glutamyl transpeptidase 4, gamma-glutamyl transpeptidase-1, gamma-glutamyl-transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-GPT, gamma-GT, gamma-GTase, gamma-GTP, gammaGT, GGT, GGT A, GGT I, GGT-1, GGT1, GGT2, GGT3, GGT4, GGT5, ggtB, GGTII protein, GGTLA1, glutamyl transpeptidase, glutamyltransferase, gamma-, HGGT, L-gamma-glutamyl transpeptidase, L-gamma-glutamyltransferase, L-glutamyltransferase, More, PnGGT, SBLGGT, VvGGT3
ECTree
2.3.2.2 gamma-glutamyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.3.2.2 - gamma-glutamyltransferase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-D/L-glutamyl-phenylhydrazine + acceptor
phenylhydrazine + 5-L-glutamyl-acceptor
-
-
product is cytotoxic
ir
glutathione + amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
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
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
L-Glu-4-nitroanilide is a suicide substrate
-
-
?
lentinic acid + amino acid
desglutamyl lentinic acid + 5-L-glutamylamino acid
-
function in aroma evolution from lentinic acid
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
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
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + 5-L-Glu-Xaa
-
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
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Bacillus amyloliquefaciens SMB469
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
Q62WE3
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
ir
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
initial step of glutathione degradation
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
involved in polyglutamic acid synthesis
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
ectoenzyme protects the epithelial cells against oxidants by replenishing intracellular glutathione
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
?
poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end
-
-
?
poly(gamma-glutamic acid) + H2O
D-Glu + L-Glu
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
GGT3 catalyzes the obligate initial step in GSH conjugate metabolism, and has an important role in protecting plants from some xenobiotic chemicals
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
O65652
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
contribution of GGT in the mechanisms of drug resistance
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
additional information
?
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-
the ggh gene is a pseudogene that is transcriptionally active but phenotypically silent
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-
?
additional information
?
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-
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
?
-
-
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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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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enzyme activates the yeast cadmium factor 1, responsible for glutathione import into the vacuole
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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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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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purified recombinant enzyme added to Porphyromonas gingivalis results in H2S, ammonia and pyruvate release in this bacterium
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L-Glu-4-nitroanilide competes with glutathione and inhibits production of H2S, ammonia and pyruvate
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