3.4.19.13: glutathione gamma-glutamate hydrolase
This is an abbreviated version!
For detailed information about glutathione gamma-glutamate hydrolase, go to the full flat file.
Word Map on EC 3.4.19.13
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3.4.19.13
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medicine
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hydroxyacyl
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halide
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alpha-globin
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formyl
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dihalomethanes
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methanes
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phosphoglycolate
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monoxide
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decomposes
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diverted
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halogenated
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formaldehyde
- 3.4.19.13
- medicine
-
hydroxyacyl
- halide
-
alpha-globin
-
formyl
-
dihalomethanes
- methanes
- phosphoglycolate
-
monoxide
-
decomposes
-
diverted
-
halogenated
- formaldehyde
Reaction
Synonyms
At4g29210, BaGGT42, BaGGT469, BlGGT13, BsGGT168, gamma-glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gamma-GT, GGT, GGT-1, GGT1, GGT3, GGT4, GGT5, hp1118, More
ECTree
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Inhibitors
Inhibitors on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase
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(2RS)-2-amino-4-((R)-1-[N-(carboxymethyl)carbamoyl]-2-chloroethyl(phenyl)-phosphono)butanoic acid
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potent and irreversible inhibitor of enzyme, second-order rate constant value 188 per M and s, and good mimic of the putative transition state
(2RS)-2-amino-4-((S)-1-[N-(carboxymethyl)carbamoyl]-2-phenylethyl(phenyl)-phosphono)butanoic acid
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potent and irreversible inhibitor of enzyme, second-order rate constant value 389 per M and s, and good mimic of the putative transition state
(2RS)-2-amino-4-((S)-1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)-phosphono)butanoic acid
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potent and irreversible inhibitor of human enzyme, second-order rate constant value 145 per M and s, and good mimic of the putative transition state
6-diazo-5-oxo-L-norleucine
pretreatment of cells completely abolishes the extracellular hydrolysis of lgutathione and glutamine
serine borate
competitive, 8fold less effective as an inhibitor of isoform GGT5 than of GGT1; competitive, 8fold less effective as an inhibitor of isoform GGT5 than of GGT1
additional information
neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates
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the mechanism-based inhibitor
2-amino-4-[[3-(carboxymethyl)phenoxy](methoxy)phosphoryl] butanoic acid
the mechanism-based inhibitor is a stable compound. It inactivates the human enzyme significantly faster than the other phosphonates, and does not inhibit a glutamine amidotransferase. The inhibitor shows no cytotoxicity toward human fibroblasts and hepatic stellate cells up to 1 mM. It serves as a non-toxic, selective and highly potent irreversible inhibitor that can be used for various in vivo as well as in vitro biochemical studies. Critical electrostatic interaction between the terminal carboxylate of the inhibitor and the active-site residue Lys562 of human enzyme for potent inhibition
in cells treated with the xenobiotic monochlorobimane, application of acivicin leads to accumulation of glutathione S-bimane conjugates
acivicin
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inhibition of gamma-glutamyltranspeptidase by acivicin causes extensive loss of intracellular glutathione from ARL-16T2 cells, which show a high level of gamma-glutamyl transpeptidase, but produces no effect on glutathione levels in ARL-15C1 cells, which show a low level of gamma-glutamyl transpeptidase. Acivicin treatment causes a transient increase in intracellular glutathione in the ARL-16T2 but not the ARL-15C1 cells