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(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
(S)-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
-
?
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O
[[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoate
i.e. POM-HEX, substrate is a prodrug of the compound HEX, which inhibits the glycolytic enzyme enolase
-
-
?
bis-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
-
-
-
?
bis-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
D-lactoyltrypanothione + H2O
D-lactate + trypanothione
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O
fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O
fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(methoxyacetate) + H2O
fluorescein-3'-oxymethyl methoxyacetate + methoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(propoxyacetate) + H2O
fluorescein-3'-oxymethyl propoxyacetate + propoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis[(ethylsulfanyl)acetate] + H2O
fluorescein-3'-oxymethyl (ethylsulfanyl)acetate + (ethylsulfanyl)acetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis[(methylsulfanyl)acetate] + H2O
fluorescein-3'-oxymethyl (methylsulfanyl)acetate + (methylsulfanyl)acetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dibutanoate + H2O
fluorescein-3'-oxymethyl butanoate + butanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dihexanoate + H2O
fluorescein-3'-oxymethyl hexanoate + hexanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dipentanoate + H2O
fluorescein-3'-oxymethyl pentanoate + pentanoate
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
mono-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
N,S-bisfluorenylmethoxycarbonylglutathione + H2O
9-fluorenylmethoxycarboxylate + glutathione
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione + H2O
beta-ethoxy-alpha-D-hydroxybutyrate + glutathione
-
-
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
?
slow model substrate for computational study, the substrate does not coordinate to any of the zinc ions in the Michaelis complex. The hydroxyl group forms a hydrogen bond to the Asp58 residue.
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
N-hydroxy-N-bromophenylcarbamate + glutathione
-
weak substrate
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
S-acetylglutathione + H2O
acetate + glutathione
S-acetyltrypanothione + H2O
acetate + trypanothione
-
-
-
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
-
-
-
?
S-D-lactoylglutathione
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
S-D-lactoylglutathione + H2O
D-lactic acid + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
-
-
-
r
S-D-lactoyltrypanothione + H2O
D-lactate + trypanothione
additionally S-D-lactoylglutathione used by mutant Y291R/C294K
-
-
?
S-D-mandeloylglutathione + H2O
? + glutathione
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
S-formylglutathione + H2O
formate + glutathione
S-glyceroylglutathione + H2O
glycerate + glutathione
-
-
-
-
?
S-glycerylglutathione + H2O
glycerate + glutathione
S-glycoloylglutathione + H2O
glycolate + glutathione
S-glycolylglutathione + H2O
? + glutathione
hydrolysis at about half the rate of S-lactoylglutathione
-
-
?
S-glycolyltrypanothione + H2O
glycolate + trypanothione
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
-
-
-
?
S-L-glyceroylglutathione + H2O
glycerate + glutathione
-
-
-
-
?
S-lactonylglutathione + H2O
? + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
S-lactoylglutathione + H2O
GSH + D-lactate
-
-
-
-
?
S-lactoylglutathionylspermidine + H2O
?
-
-
-
?
S-m-nitrobenzyloxycarbonylglutathione + H2O
m-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
S-mandeloylglutathione + H2O
mandelic acid + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
S-o-nitrobenzyloxycarbonylglutathione + H2O
o-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-p-nitrobenzyloxycarbonylglutathione + H2O
p-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
trypanothione hemithioacetal + H2O
?
-
-
-
-
ir
additional information
?
-
(S)-D-lactoylglutathione + H2O

D-lactate + glutathione
-
-
-
-
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
lactoylglutathione + H2O

D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
S-D-lactoylglutathione
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
S-D-lactoylglutathione
-
?
lactoylglutathione + H2O
D-lactate + glutathione
little activity with this substrate
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
S-D-lactoylglutathione
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
enzyme does not show saturation kinetics up to 5 mM
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
mono-(lactoyl)trypanothione + H2O

D-lactate + trypanothione
-
-
-
?
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
-
-
-
-
ir
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O

glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O

glutathione + a 2-hydroxycarboxylate anion
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
second step in the glyoxalase system
regeneration of glutathione for the first step in the glyoxalase system
-
ir
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
the enzyme is involved in the detoxification process converting reactive dicarbonyl compounds such as methylglyoxal to less reactive hydroxyl acids
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
-
?
S-acetoacetylglutathione + H2O

acetoacetate + glutathione
hydrolysis at about half the rate of S-lactoylglutathione
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
55.6% of the activity with S-lactoylglutathione
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O

acetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
8.6% of the activity with S-lactoylglutathione
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O

D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system, detoxification of methylglyoxal
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system, detoxification of methylglyoxal
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
used by mutant Y291R/C294K
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
substrate is predominantly bound via ionic interactions with the conserved residues Arg257 and Lys260. Correct substrate binding is a pH- and salt-dependent rate-limiting step for catalysis. Bi Bi mechanism with the direct involvement of a hydroxide ion as a second substrate
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O

glutathione + D-lactate
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
enzyme is involved in the detoxification of methylglyoxal
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
enzyme is involved in the detoxification of methylglyoxal
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis
-
?
S-D-mandeloylglutathione + H2O

D-mandelate + glutathione
-
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
?
S-formylglutathione + H2O

formate + glutathione
-
-
-
-
?
S-formylglutathione + H2O
formate + glutathione
-
37.7% of the activity with S-lactoylglutathione
-
-
?
S-formylglutathione + H2O
formate + glutathione
-
-
-
-
?
S-glycerylglutathione + H2O

glycerate + glutathione
-
-
-
-
?
S-glycerylglutathione + H2O
glycerate + glutathione
-
61.6% of the activity with S-lactoylglutathione
-
-
?
S-glycoloylglutathione + H2O

glycolate + glutathione
-
-
-
-
?
S-glycoloylglutathione + H2O
glycolate + glutathione
-
38.6% of the activity with S-lactoylglutathione
-
-
?
S-lactoylglutathione + H2O

D-lactate + glutathione
-
-
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
preferred substrae
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-mandeloylglutathione + H2O

mandelate + glutathione
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
4.8% of the activity with S-lactoylglutathione
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
-
-
-
?
S-methyl hydroxy(phenyl)ethanethioate + H2O

methanethiol + hydroxy(phenyl)acetic acid
-
thioester hydrolysis is promoted by an Fe(III)Zn(II) complex
-
-
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
-
thioester hydrolysis promoted by a mononuclear zinc complex
-
-
?
S-propionylglutathione + H2O

propionate + glutathione
-
-
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
-
13.5% of the activity with S-lactoylglutathione
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O

succinate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
29.2% of the activity with S-lactoylglutathione
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
additional information

?
-
the enzyme participates in the detoxification of cytotoxic and mutagenic 2-oxoaldehydes
-
?
additional information
?
-
no substrate: S-formylglutathione
-
-
?
additional information
?
-
-
no substrate: S-formylglutathione
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate limiting step of the glyoxalase pathway
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
-
?
additional information
?
-
enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
-
?
additional information
?
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
-
-
?
additional information
?
-
the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins
-
-
?
additional information
?
-
The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction.
-
-
?
additional information
?
-
-
the enzyme does not promote S-glutathionylation of GAPDH
-
-
?
additional information
?
-
-
no substrate: S-lactoylglutathione
-
-
?
additional information
?
-
-
the glyoxalase system may play an important role in the regulation of cell division and differentiation
-
-
?
additional information
?
-
-
catalytic process involves a water molecule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron
-
-
?
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
-
-
?
additional information
?
-
OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
-
-
?
additional information
?
-
-
OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
no substrates: 4-nitrophenyl acetate, 4-nitrophenyl butanoate, 4-nitrophenyl trimethylacetate
-
-
-
additional information
?
-
recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
-
-
?
additional information
?
-
-
recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
-
-
?
additional information
?
-
The glyoxalase system, composed of glyoxalase I and II catalyzes the detoxification of reactive ketoaldehydes and thus protects cells from ketoaldehyde-mediated formation of advanced glycation end products. The main physiological substrate is the toxic and mutagenic methylglyoxal, which originates from triosephosphates during glycolysis as well as threonine catabolism.
-
-
?
additional information
?
-
-
The glyoxalase system, composed of glyoxalase I and II catalyzes the detoxification of reactive ketoaldehydes and thus protects cells from ketoaldehyde-mediated formation of advanced glycation end products. The main physiological substrate is the toxic and mutagenic methylglyoxal, which originates from triosephosphates during glycolysis as well as threonine catabolism.
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
S-acetyltrypanothione + H2O
acetate + trypanothione
-
-
-
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
S-D-lactoylglutathione + H2O
glutathione + D-lactate
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
-
-
-
r
S-glycolyltrypanothione + H2O
glycolate + trypanothione
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
-
-
-
?
S-lactoylglutathionylspermidine + H2O
?
-
-
-
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
-
-
-
?
additional information
?
-
S-(2-hydroxyacyl)glutathione + H2O

glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O

glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
second step in the glyoxalase system
regeneration of glutathione for the first step in the glyoxalase system
-
ir
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
the enzyme is involved in the detoxification process converting reactive dicarbonyl compounds such as methylglyoxal to less reactive hydroxyl acids
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
-
?
S-D-lactoylglutathione + H2O

D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system, detoxification of methylglyoxal
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system, detoxification of methylglyoxal
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
second step in the glyoxalase system
-
-
?
S-D-lactoylglutathione + H2O

glutathione + D-lactate
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
enzyme is involved in the detoxification of methylglyoxal
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
enzyme is involved in the detoxification of methylglyoxal
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis
-
?
additional information

?
-
the enzyme participates in the detoxification of cytotoxic and mutagenic 2-oxoaldehydes
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate limiting step of the glyoxalase pathway
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
-
the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. Accordingly, a specific responsive element is found in intron 1 of the GLX2 gene, which can be activated and bound by p63 and p73. Upon overexpression, the cytosolic, but not the mitochondrial, GLX2 inhibits the apoptotic response of a cell to methylglyoxal, a by-product of glycolysis. Cells deficient in GLX2 are hypersensitive to methylglyoxal-induced apoptosis. A deficiency in GLX2 enhances the susceptibility of a cell to DNA damage-induced apoptosis in a p53-dependent manner
-
-
?
additional information
?
-
GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
-
-
?
additional information
?
-
the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins
-
-
?
additional information
?
-
The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction.
-
-
?
additional information
?
-
-
the glyoxalase system may play an important role in the regulation of cell division and differentiation
-
-
?
additional information
?
-
-
catalytic process involves a water molecule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron
-
-
?
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
-
-
?
additional information
?
-
OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
-
-
?
additional information
?
-
-
OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
-
-
?
additional information
?
-
-
recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
-
-
?
additional information
?
-
The glyoxalase system, composed of glyoxalase I and II catalyzes the detoxification of reactive ketoaldehydes and thus protects cells from ketoaldehyde-mediated formation of advanced glycation end products. The main physiological substrate is the toxic and mutagenic methylglyoxal, which originates from triosephosphates during glycolysis as well as threonine catabolism.
-
-
?
additional information
?
-
-
The glyoxalase system, composed of glyoxalase I and II catalyzes the detoxification of reactive ketoaldehydes and thus protects cells from ketoaldehyde-mediated formation of advanced glycation end products. The main physiological substrate is the toxic and mutagenic methylglyoxal, which originates from triosephosphates during glycolysis as well as threonine catabolism.
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
-
the enzyme activity is increased by 23% and 53% at 0.25 and 0.5 mM Cd2+, respectively
Co2+
-
glxII apoenzyme activity is regained
Cobalt
0.6 mol per mol of protein
Ni2+
-
no activity of glxII, re-addition of Zn2+ results in a further inhibition of the residual enzyme activity of the incompletely demetalled apo-GlxII
Fe2+

-
-
Fe2+
0.8 mol per mol of protein, wild-type enzyme, 0.4 mol per mol of protein, R248W mutant enzyme
Fe2+
cytosolic isozyme, enzyme contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis, content of wild-type and mutant enzymes, overview
Fe2+
-
catalytic process of glyoxalase II involves a water moleule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron
Fe2+
the enzyme contains a binuclear Zn/Fe centre
Fe2+
-
contains a binuclear Zn/Fe centre in its active site
Fe2+
0.26 mol per mol of enzyme
Fe2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
Fe2+
-
behavior of Fe-GloB resembles that of Zn-GloB. Thiol-Fe bond is formed between the Cys moiety of glutathione and the metal site, the dinuclear iron sites show an enhanced antiferromagnetic coupling in the GloB-glutathione adduct. GloB-glutathione complex displays S-thiol-FeIII and S-thiol-FeII: charge transfer bands
Fe2+
-
stimulates activity (0.1 mM: 9-fold)
Fe3+

-
Arabidopsis thaliana mitochondrial and cytosolic gly II can accomodate a number of different metal centers, enzyme contains an iron-zinc binuclear metal center that os essential for activity
Fe3+
-
thioester hydrolysis is promoted by an Fe(III)Zn(II) complex. Thioester does not initially interact with the Fe(III) center, changes occur at this site over the course of the reaction. Formation of a Fe(III)-S-methyl ester moiety, which likely results from redox activity involving an iron(III) thiolate species. Thioester hydrolysis may involve initial coordination of the deprotonated alpha-hydroxy thioester to the zinc center followed by nucleophilic attack by a terminal Fe(III)-OH moiety and thiolate leaving group stabilization by the Fe(III) center
Fe3+
-
GloB-glutathione complex displays S-thiol-FeIII and S-thiol-FeII: charge transfer bands
Iron

-
0.55 mol per mol of protein in minimal medium, located in the dinuclear site, metalloenzyme, enzyme binds a mixture of zinc, iron, and manganese when produced in cells grown in rich medium
Iron
1.04 mol per mol of enzyme, contains a predominant Fe(III)Zn(II) center and an anti-ferromagnetically coupled Fe(III)Fe(II) center
Iron
0.42 mol per mol of protein
Mn2+

-
-
Mn2+
-
0.05 mol per mol of protein in minimal medium, metalloenzyme, enzyme binds a mixture of zinc, iron, and manganese when produced in cells grown in rich medium
Mn2+
0.1 mol per mol of protein, R248W mutant enzyme
Mn2+
-
no binding to Arabidopsis thaliana mitochondrial enzyme, but binding to cytosolic gly II
Mn2+
-
glxII apoenzyme activity is regained
Mn2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
Mn2+
-
MnII-thiolate bonds are less covalent and weaker than ironâthiolate bonds
Mn2+
-
stimulates activity (0.1 mM: 5-fold, 1mM: 7-fold)
Zinc

1.31 mol per mol of enzmye
Zinc
-
the mononuclear zinc complex [(bpta)Zn](ClO4)2 x 0.5 H2O promotes the hydrolysis of thioester when dissolved in CH3CN:H2O (50:50 buffered at pH 9.0). This reaction results in the formation of a mixture of CD3SH and a zinc thiolate complex, the latter of which can be protonated to generate additional CD3SH
Zinc
-
recombinant GloII is zinc-dependent
Zinc
0.45 mol per mol of protein
Zn2+

-
-
Zn2+
-
enzyme binds 2.1 mol of Zn(II) per monomer. The binding of Zn(II) is essential for enzyme viability and activity
Zn2+
0.4 mol per mol of protein, wild-type enzyme, 2.1 mol per mol of protein, R248W mutant enzyme
Zn2+
-
0.5 mol per mol of protein in minimal medium, located in the dinuclear site, metalloenzyme, enzyme binds a mixture of zinc, iron, and manganese when produced in cells grown in rich medium
Zn2+
cytosolic isozyme, enzyme contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis, content of wild-type and mutant enzymes, overview
Zn2+
-
glxII is a binuclear metalloenzyme with Zn2+ as the probable active site metal ion
Zn2+
-
thioester hydrolysis is promoted by an Fe(III)Zn(II) complex. Thioester hydrolysis may involve initial coordination of the deprotonated alpha-hydroxy thioester to the zinc center followed by nucleophilic attack by a terminal Fe(III)-OH moiety and thiolate leaving group stabilization by the Fe(III) center
Zn2+
binuclear zinc-dependent metalloenzyme
Zn2+
-
glxII is a binuclear metalloenzyme with Zn2+ as the probable active site metal ion, glxII is isolated with approximately two mol of Zn2+ bound per mole of glxII
Zn2+
-
essential for maintainance of native structure of the enzyme. Binding to the apoenzyme occurs during an essential step of refolding
Zn2+
glyoxalase I is a binuclear zinc-enzyme, Zn2+ stabilizes the charge of tetrahedral intermediate thereby lowering the barrier for the nucleophilic attack, while Zn1 stabilizes the charge of the thiolate product, thereby facilitating the C-S bond cleavage
Zn2+
-
contains two zinc atoms
Zn2+
-
essential role in catalytic mechanism
Zn2+
the enzyme contains a binuclear Zn/Fe centre
Zn2+
-
contains a binuclear Zn/Fe centre in its active site
Zn2+
1.7 mol per mol of enzyme
Zn2+
0.05 mol per mol of enzyme
Zn2+
-
stimulates activity
Zn2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
Zn2+
-
behavior of Zn-GloB resembles that of Fe-GloB
Zn2+
-
bound, molar ratio 0.65 Zn2+:1
additional information

enzyme possesses a binuclear active site, metal ion binding structure and kinetics, overview
additional information
-
enzyme possesses a binuclear active site, metal ion binding structure and kinetics, overview
additional information
-
metal binding structure, and metal content under different media conditions, overview, enzyme shows positive cooperative metal binding
additional information
not: manganese
additional information
-
not: manganese
additional information
-
overexpresssion of enzyme in minmal media containing either Zn, Fe, or Mn results in enzyme binding an average of 1 equivalent of metal ion, and presence of antiferomagnetically and ferromagnetically coupled dinuclear metal centers. Enzyme does not exist as a mononuclear metal ion containing enzyme, and shows positive cooperativity in metal binding
additional information
-
the cytosolic and mitochondrial glxII from Arabidopsis thaliana contain varying ratios of Zn2+, Fe2+ and Mn2+ and exhibit broad metal activation
additional information
metalloprotein
additional information
-
metalloprotein
additional information
-
the enzyme is almost unaffected by Mn2+, Mg2+, Ni2+, Fe2+ or Fe3+
additional information
the enzyme contains the highly conserved metal binding motif THXHXDH, total metal ions per mol of enzyme: 1.5 for the His-tagged enzyme, 0.7-0.9 for the free enzyme
additional information
-
the enzyme contains the highly conserved metal binding motif THXHXDH, total metal ions per mol of enzyme: 1.5 for the His-tagged enzyme, 0.7-0.9 for the free enzyme
additional information
sequence contains the highly conserved metal binding motif THXHXDH
additional information
-
sequence contains the highly conserved metal binding motif THXHXDH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
12-O-tetradecanoylphorbol-13-acetate
-
-
2,4,6-Trinitrobenzenesulfonate
acidic phospholipids
-
noncompetitive inhibition, lower thermal stability of the enzyme, inhibit protein intermolecular interactions/aggregation by thermal denaturation, small changes in the secondary structure are caused
-
anionic phospholipids
-
noncompetitive inhibition, cytosolic isozyme
-
cardiolipin
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
Cd2+
-
the enzyme activity decreases by 20% and 32% at 0.5 and 1.0 mM Cd2+, respectively
copper acetate
-
above 15 mM
dioleoyl phosphatidic acid
-
i.e. DOPA, negatively charged phospholipid, strongly inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
dipalmitoylphosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
diphosphate
-
25 mM, 50% inhibition
DTT
-
1.25 mM, 60% inhibition
Fe2+
addition to the medium slightly reduces the activity in vivo
fructose
-
inactivation of the glyoxalase system (glyoxalase I and II) in fructose fed mice
glutathione ethyl ester
-
carboxylate group of the glycine-moiety is modified, non-competitive inhibition
Guanidine-HCl
-
below 1 M, inactivation occurs without loss of the secondary structure
methylene blue
-
photoinactivation
methylglyoxal-glutathione hemimercaptal
Mn2+
addition to the medium reduces the activity in vivo
N,S-(dicarbobenzoxy)glutathione
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
-
N,S-bis-(phenylmethoxycarbonyl)glutathione
-
N,S-bis-carbobenzoxy-glutathione
-
-
N,S-bis-FMOC-glutathione
-
-
N,S-bisfluorenylmethoxycarbonylglutathione
-
-
N-(9-fluorenylmethoxycarbonyl)-S-phenylmethoxycarbonylglutathione
-
N-(9-fluorenylmethoxycarbonyl)glutathione
-
N-acetyl-S-(p-bromobenzyl)glutathione
N-benzoyl-S-(p-bromobenzyl)glutathione
-
-
N-benzyloxycarbonyl-S-(p-bromobenzyl)glutathione
-
-
N-phenylmethoxycarbonyl-S-(9-fluorenylmethoxycarbonyl)glutathione
-
N-phenylmethoxycarbonylglutathione
-
Na2HAsO4
-
0.5 mM arsenic decreases the enzyme activity by 29%
oxalate
-
20 mM, 38% inhibition
p-hydroxymercuribenzoate
-
-
p-nitrobenzyl-S-glutathione
-
very weak
phosphate
-
67 mM, 35% inhibition
phosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
S,N-blocked glutathiones
-
-
-
S-(9-fluorenylmethoxycarbonyl)glutathione
-
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
50% inhibition at 0.002 mM; 50% inhibition at 0.03 mM
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
50% inhibition at 0.006 mM; 50% inhibition at 0.185 mM
S-(p-Azidophenacyl)-glutathione
S-(p-azidophenacyl)glutathione
-
S-(p-bromobenzyl)glutathione
-
-
S-(p-chlorophenacyl)glutathione
S-benzyloxycarbonylglutathione
S-blocked glutathiones
-
-
-
S-fluorenylmethyloxycarbonylglutathione
S-m-nitrobenzyloxycarbonylglutathione
S-o-nitrobenzyloxycarbonylglutathione
S-p-nitrobenzyloxycarbonylglutathione
S-phenylmethoxycarbonylglutathione
-
transcription factor p63
-
upregulation of glyoxalase II
-
transcription factor p73
-
upregulation of glyoxalase II
-
Trinitrobenzenesulfonate
-
-
2,4,6-Trinitrobenzenesulfonate

-
-
2,4,6-Trinitrobenzenesulfonate
-
N-acetyl-S-(p-bromobenzyl)glutathione protects
2,4,6-Trinitrobenzenesulfonate
-
-
2,4,6-Trinitrobenzenesulfonate
-
N-acetyl-S-(p-bromobenzyl)glutathione protects
2,4,6-Trinitrobenzenesulfonate
-
-
Cu2+

-
-
D-lactate

-
-
D-lactate
-
competitive inhibition
diethyldicarbonate

-
pH 6
glutathione

-
-
glutathione
-
weak competitive
glutathione
-
a combination of methylglyoxal and glutathione has a greater than additive inhibitory activity
glutathione
-
non-competitive inhibition. Is a stronger inhibitor than the ethyl ester of glutathione. Theorell-Chance Bi Bi mechanism with glutathione as the second product
glutathione
-
8.0 mM, 43% loss of activity
glutathione
-
metal-selective end product inhibition. Thiol-Fe bond is formed between the Cys moiety of glutathione and the metal site, the dinuclear iron sites show an enhanced antiferromagnetic coupling in the GloB-glutathione adduct
Hg2+

-
-
Hg2+
-
HgCl2, most potent inhibitor
Hg2+
-
HgCl2, 0.5 mM, complete inhibition
iodoacetate

-
-
methylglyoxal

-
-
methylglyoxal-glutathione hemimercaptal

-
-
methylglyoxal-glutathione hemimercaptal
-
-
methylglyoxal-glutathione hemimercaptal
-
-
methylglyoxal-glutathione hemimercaptal
-
-
N,S-(dicarbobenzoxy)glutathione

-
-
N,S-(dicarbobenzoxy)glutathione
-
-
N-acetyl-S-(p-bromobenzyl)glutathione

-
-
N-acetyl-S-(p-bromobenzyl)glutathione
-
competitive
N-acetyl-S-(p-bromobenzyl)glutathione
-
-
N-acetyl-S-(p-bromobenzyl)glutathione
-
competitive
N-acetyl-S-(p-bromobenzyl)glutathione
-
-
NEM

-
-
PCMB

-
-
PCMB
-
0.3 mM, complete inhibition
Phenylglyoxal

-
10 mM, 1 h, 60% loss of activity
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione

-
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
competitive inhibition
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
50% inhibition at 0.0016 mM; 50% inhibition at 0.02 mM
S-(p-Azidophenacyl)-glutathione

-
linear competitive
S-(p-Azidophenacyl)-glutathione
-
-
S-(p-chlorophenacyl)glutathione

-
-
S-(p-chlorophenacyl)glutathione
-
-
S-benzyloxycarbonylglutathione

-
-
S-benzyloxycarbonylglutathione
-
-
S-benzyloxycarbonylglutathione
-
-
S-benzyloxycarbonylglutathione
-
-
S-benzyloxycarbonylglutathione
-
-
S-fluorenylmethyloxycarbonylglutathione

-
-
S-fluorenylmethyloxycarbonylglutathione
-
-
S-m-nitrobenzyloxycarbonylglutathione

-
-
S-m-nitrobenzyloxycarbonylglutathione
-
-
S-o-nitrobenzyloxycarbonylglutathione

-
-
S-o-nitrobenzyloxycarbonylglutathione
-
-
S-p-nitrobenzyloxycarbonylglutathione

-
-
S-p-nitrobenzyloxycarbonylglutathione
-
potent competitive
S-p-nitrobenzyloxycarbonylglutathione
-
-
S-p-nitrobenzyloxycarbonylglutathione
-
-
S-p-nitrobenzyloxycarbonylglutathione
-
-
additional information

-
inhibitory effect of methanol-extracts of some edible plants and some medicinal herbs against the glyoxalase II
-
additional information
-
negatively charged phospholipids, like dioleoyl phosphatidic acid, cardiolipin, and phosphatidylserine, specifically interact with the enzyme, but do not inhibit the mitochondrial isozyme, no effect by neutral phospholipids
-
additional information
-
no effect by neutral phospholipids, phospholipid binding studies
-
additional information
the enzyme is not sensitive against ionic strength
-
additional information
-
the enzyme is not sensitive against ionic strength
-
additional information
-
benzyloxycarbonyl-S-derivatives are stronger inhibitors than the p-chlorophenacyl S-derivative
-
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Adenocarcinoma
Overexpression of glyoxalase system enzymes in human kidney tumor.
Breast Neoplasms
A possible regulatory role of 17beta-estradiol and tamoxifen on glyoxalase I and glyoxalase II genes expression in MCF7 and BT20 human breast cancer cells.
Breast Neoplasms
Expression of glyoxalase I and II in normal and breast cancer tissues.
Carcinogenesis
Changes in concentrations of methylglyoxal, D-lactate and glyoxalase activities in liver and plasma of rats fed a 3'-methyl-4-dimethylaminoazobenzene-rich diet.
Carcinogenesis
Glyoxalase 2 drives tumorigenesis in human prostate cells in a mechanism involving androgen receptor and p53-p21 axis.
Carcinoma
Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas.
Carcinoma, Ovarian Epithelial
Germ cell specific protein VASA is over-expressed in epithelial ovarian cancer and disrupts DNA damage-induced G2 checkpoint.
Carcinoma, Renal Cell
Overexpression of glyoxalase system enzymes in human kidney tumor.
Diabetes Complications
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Diabetes Complications
Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
Diabetes Mellitus
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Diabetes Mellitus
The Relationship Between Alanerv(®) Consumption and Erythrocytes' Glyoxalases I and II Activities and The Level of Some Serum Markers of Carbonyl Stress in Post-Acute Stroke Patients Undergoing Rehabilitation.
Diabetes Mellitus, Type 1
Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
Diabetes Mellitus, Type 2
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Diabetic Retinopathy
Gene Expression of Glyoxalase II in Diabetic Retinopathy.
Elliptocytosis, Hereditary
Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis.
hydroxyacylglutathione hydrolase deficiency
Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis.
hydroxyacylglutathione hydrolase deficiency
Glyoxalase 2 deficiency in the erythrocytes of a horse: 1H NMR studies of enzyme kinetics and transport of S-lactoylglutathione.
hydroxyacylglutathione hydrolase deficiency
Studies of erythrocyte glyoxalase II in various domestic species: discovery of glyoxalase II deficiency in the horse.
Infections
Carbonyl stress phenomena during chronic infection with Opisthorchis felineus.
Infections
Definitive host influences the proteomic profile of excretory/secretory products of the trematode Echinostoma caproni.
Leishmaniasis, Visceral
Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs.
Leukemia
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Malaria
Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis.
Melanoma
[Activity of glyoxalase and glyoxalase II under the effect of toxohormone from melanoma]
Muscular Atrophy, Spinal
Glyoxalase enzyme system in human muscular dystrophy.
Muscular Dystrophies
Glyoxalase enzyme system in human muscular dystrophy.
Myeloproliferative Disorders
Platelet glyoxalases in thrombocytosis.
Neoplasms
Glyoxalase 2 drives tumorigenesis in human prostate cells in a mechanism involving androgen receptor and p53-p21 axis.
Neoplasms
Glyoxalase activities in human tumour cell lines in vitro.
Neoplasms
Glyoxalase activities in tumor and non-tumor human urogenital tissues.
Neoplasms
Glyoxalase II activity in tumours.
Neoplasms
Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy.
Neoplasms
S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II.
Neoplasms
The tumor promoting phorbol diester, 12-O-tetradecanoylphorbol-13-acetate (TPA) increases glyoxalase I and decreases glyoxalase II activity in human polymorphonuclear leukocytes.
Obesity
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Prostatic Hyperplasia
Glyoxalase activities in tumor and non-tumor human urogenital tissues.
Prostatic Neoplasms
Glyoxalase 2 Is Involved in Human Prostate Cancer Progression as Part of a Mechanism Driven By PTEN/PI3K/AKT/mTOR Signaling With Involvement of PKM2 and ER?.
Sarcoma
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Sarcoma 180
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Stroke
The Relationship Between Alanerv(®) Consumption and Erythrocytes' Glyoxalases I and II Activities and The Level of Some Serum Markers of Carbonyl Stress in Post-Acute Stroke Patients Undergoing Rehabilitation.
Thrombocytosis
Platelet glyoxalases in thrombocytosis.
Trypanosomiasis, African
Glyoxalase II of African trypanosomes is trypanothione-dependent.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.15 - 0.29
(S)-D-lactoylglutathione
0.009
(S)-D-mandeloylglutathione
-
-
0.086
bis-(lactoyl)trypanothione
3
lactoylglutathione
or above, pH 7.2, 25°C
0.039 - 0.108
mono-(lactoyl)trypanothione
0.152 - 0.283
S-(2-hydroxyacyl)glutathione
0.044 - 0.703
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
0.054 - 0.841
S-Acetoacetylglutathione
0.034 - 0.83
S-acetylglutathione
0.144
S-acetyltrypanothione
-
0.164
S-bis-lactoyltrypanothione
-
0.06 - 5.782
S-D-lactoylglutathione
0.32
S-D-lactoylgutathione
-
pH 6.5, 30°C, substrate concentration 1.5-3 mM
0.092 - 0.15
S-D-lactoyltrypanothione
0.0166 - 0.0365
S-D-mandeloylglutathione
0.153 - 0.213
S-formylglutathione
0.109
S-glyceroylglutathione
0.07 - 1.16
S-glycolylglutathione
0.265
S-glycolyltrypanothione
-
0.133
S-hydroxyglutaryltrypanothione
-
0.0966
S-L-glyceroylglutathione
-
-
0.0007 - 0.6
S-Lactoylglutathione
0.195
S-lactoylglutathionylspermidine
-
0.014 - 0.0164
S-mandeloylglutathione
0.213 - 1.2
S-propionylglutathione
0.109
S-propionyltrypanothione
-
0.134 - 0.535
S-succinylglutathione
additional information
additional information
-
0.15
(S)-D-lactoylglutathione

-
-
0.177
(S)-D-lactoylglutathione
-
-
0.251
(S)-D-lactoylglutathione
-
-
0.29
(S)-D-lactoylglutathione
-
-
0.086
bis-(lactoyl)trypanothione

pH 7.2, 25°C
0.086
bis-(lactoyl)trypanothione
recombinant enzyme, pH 7.2, 25°C
0.039
mono-(lactoyl)trypanothione

pH 7.2, 25°C
0.098
mono-(lactoyl)trypanothione
-
pH 6.8, 30°C
0.108
mono-(lactoyl)trypanothione
pH 7.2, 25°C
0.108
mono-(lactoyl)trypanothione
recombinant enzyme, pH 7.2, 25°C
0.152
S-(2-hydroxyacyl)glutathione

-
cytosolic isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid
0.152
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C
0.162
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid
0.169
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of cardiolipin
0.191
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of dipalmitoylphosphatidylserine
0.191
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C, in presence of cardiolipin
0.201
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C
0.255
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C, in presence of phosphatidylserine
0.283
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C, in presence of dipalmitoylphosphatidylserine
0.044
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione

-
cytosolic enzyme
0.05
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
0.703
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
0.054
S-Acetoacetylglutathione

-
-
0.116
S-Acetoacetylglutathione
-
-
0.13
S-Acetoacetylglutathione
-
-
0.295
S-Acetoacetylglutathione
-
enzyme from liver
0.296
S-Acetoacetylglutathione
-
-
0.413
S-Acetoacetylglutathione
-
enzyme from intermembrane space
0.634
S-Acetoacetylglutathione
-
matrix enzyme
0.841
S-Acetoacetylglutathione
-
cytosolic enzyme
0.034
S-acetylglutathione

-
-
0.2
S-acetylglutathione
-
-
0.266
S-acetylglutathione
-
-
0.266
S-acetylglutathione
-
enzyme from liver
0.568
S-acetylglutathione
-
cytosolic enzyme
0.6
S-acetylglutathione
-
matrix enzyme
0.603
S-acetylglutathione
-
enzyme from intermembrane space
0.662
S-acetylglutathione
-
mitochondrial enzyme
0.83
S-acetylglutathione
-
-
0.06
S-D-lactoylglutathione

mutant R225A, pH 7.2, 25°C
0.061
S-D-lactoylglutathione
-
0.062
S-D-lactoylglutathione
mutant C140A, pH 7.2, 25°C
0.063
S-D-lactoylglutathione
wild-type enzyme, pH 7.2, 25°C
0.0722
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
0.076
S-D-lactoylglutathione
mutant D58C, pH 7.2, 25°C
0.098
S-D-lactoylglutathione
-
-
0.098
S-D-lactoylglutathione
mutant N178A, pH 7.2, 25°C
0.112
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
0.114
S-D-lactoylglutathione
-
wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
0.116
S-D-lactoylglutathione
-
mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
0.12
S-D-lactoylglutathione
recombinant enzyme grown in medium supplemented with Mn2+, pH 7.2, 25°C
0.13
S-D-lactoylglutathione
mutant H54N, pH 7.2, 25°C
0.137
S-D-lactoylglutathione
-
-
0.14
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C
0.146
S-D-lactoylglutathione
-
-
0.151
S-D-lactoylglutathione
recombinant mutant L9A, pH 7.2, 25°C
0.17
S-D-lactoylglutathione
mutant K142A, pH 7.2, 25°C
0.187
S-D-lactoylglutathione
recombinant enzyme
0.2
S-D-lactoylglutathione
-
recombinant wild-type enzyme, pH 7.1, 37°C
0.21
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C
0.22
S-D-lactoylglutathione
recombinant enzyme grown in medium not supplemented with metal ions or supplemented with Fe2+, pH 7.2, 25°C
0.241
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Mn2+
0.256
S-D-lactoylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.268
S-D-lactoylglutathione
recombinant mutant W57D, pH 7.2, 25°C
0.27
S-D-lactoylglutathione
-
-
0.27
S-D-lactoylglutathione
-
enzyme from liver
0.275
S-D-lactoylglutathione
-
mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
0.288
S-D-lactoylglutathione
recombinant mutant K65A, pH 7.2, 25°C
0.295
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Zn2+
0.2982
S-D-lactoylglutathione
at pH 7.5 and 25°C
0.318
S-D-lactoylglutathione
recombinant mutant W57N, pH 7.2, 25°C
0.384
S-D-lactoylglutathione
-
matrix enzyme
0.408
S-D-lactoylglutathione
enzyme otained from LB medium
0.433
S-D-lactoylglutathione
-
cytosolic enzyme
0.439
S-D-lactoylglutathione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
0.44
S-D-lactoylglutathione
-
mitochondrial enzyme
0.463
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Fe2+
0.484
S-D-lactoylglutathione
-
-
0.5
S-D-lactoylglutathione
-
at pH 7.5 and 30°C
0.598
S-D-lactoylglutathione
-
enzyme from intermembrane space
0.6
S-D-lactoylglutathione
mutant R248W, pH 7.2, 25°C
0.6
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Fe added, pH 7.2, 25°C
1.6
S-D-lactoylglutathione
-
recombinant mutant Y175F, pH 7.1, 37°C
2.551
S-D-lactoylglutathione
-
mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4
2.867
S-D-lactoylglutathione
-
mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
3
S-D-lactoylglutathione
above, recombinant enzyme, pH 7.2, 25°C
4.308
S-D-lactoylglutathione
-
mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
5.782
S-D-lactoylglutathione
-
mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
0.092
S-D-lactoyltrypanothione

wild type protein, pH not specified in the publication, temperature not specified in the publication
0.15
S-D-lactoyltrypanothione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
0.0166
S-D-mandeloylglutathione

pH not specified in the publication, temperature not specified in the publication
0.0218
S-D-mandeloylglutathione
-
-
0.026
S-D-mandeloylglutathione
enzyme from erythrocytes
0.029
S-D-mandeloylglutathione
recombinant enzyme
0.0365
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
0.153
S-formylglutathione

-
-
0.153
S-formylglutathione
-
enzyme from liver
0.213
S-formylglutathione
-
cytosolic enzyme
0.109
S-glyceroylglutathione

-
-
0.109
S-glyceroylglutathione
-
enzyme from liver
0.07
S-glycolylglutathione

-
-
0.07
S-glycolylglutathione
-
enzyme from liver
0.237
S-glycolylglutathione
-
-
1.16
S-glycolylglutathione
-
brain
0.0007
S-Lactoylglutathione

-
-
0.086
S-Lactoylglutathione
-
-
0.1
S-Lactoylglutathione
25°C
0.12
S-Lactoylglutathione
pH 7.0
0.139
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without in presence of zinc
0.172
S-Lactoylglutathione
enzyme from erythrocytes
0.18
S-Lactoylglutathione
-
-
0.18
S-Lactoylglutathione
-
enzyme from erythrocytes
0.19
S-Lactoylglutathione
-
-
0.19
S-Lactoylglutathione
-
enzyme from liver
0.19
S-Lactoylglutathione
37°C
0.209
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without added metal ion
0.21
S-Lactoylglutathione
-
enzyme from liver
0.225
S-Lactoylglutathione
25°C
0.254
S-Lactoylglutathione
-
pH and temperature not specified in the publication, Vmax: 1 mmol/min/mg
0.304
S-Lactoylglutathione
-
enzyme from brain
0.325
S-Lactoylglutathione
-
enzyme from calf brain
0.391
S-Lactoylglutathione
25°C, pH 7.2
0.463
S-Lactoylglutathione
37°C, mutant Y185F
0.6
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium in presence of iron
0.014
S-mandeloylglutathione

-
-
0.014
S-mandeloylglutathione
-
enzyme from erythrocytes
0.015
S-mandeloylglutathione
-
enzyme from brain
0.016
S-mandeloylglutathione
-
enzyme from liver
0.0164
S-mandeloylglutathione
-
-
0.213
S-propionylglutathione

-
-
0.213
S-propionylglutathione
-
enzyme from liver
0.214
S-propionylglutathione
-
cytosolic enzyme
0.242
S-propionylglutathione
-
mitochondrial enzyme
0.378
S-propionylglutathione
-
mitochondrial enzyme
0.792
S-propionylglutathione
-
enzyme from intermembrane space
1.2
S-propionylglutathione
-
matrix enzyme
0.134
S-succinylglutathione

-
-
0.16
S-succinylglutathione
-
mitochondrial enzyme
0.186
S-succinylglutathione
-
enzyme from intermembrane space
0.2
S-succinylglutathione
-
-
0.2
S-succinylglutathione
-
enzyme from liver
0.25
S-succinylglutathione
-
-
0.25
S-succinylglutathione
-
-
0.325
S-succinylglutathione
-
cytosolic enzyme
0.535
S-succinylglutathione
-
matrix enzyme
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
kinetics
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics in presence of liposomes consisting of different phospholipids
-
additional information
additional information
-
kinetics in presence of liposomes consisting of different phospholipids
-
additional information
additional information
-
kinetics of the enzyme in situ, cells being permeabilized by digitonin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
82
S-Acetoacetylglutathione
-
-
0.9 - 6780
S-D-lactoylglutathione
16 - 241
S-D-lactoyltrypanothione
25.8 - 183
S-D-mandeloylglutathione
1740
S-glycoloylglutathione
-
-
1490
S-L-glyceroylglutathione
-
-
64.3 - 780
S-Lactoylglutathione
188 - 755
S-mandeloylglutathione
68
S-succinylglutathione
-
-
additional information
additional information
-
turnover-numver is pH-independent in the range pH 6-9.3
-
0.9
S-D-lactoylglutathione

-
at pH 7.5 and 30°C
10.6
S-D-lactoylglutathione
mutant D58C, pH 7.2, 25°C
10.9
S-D-lactoylglutathione
mutant H54N, pH 7.2, 25°C
16
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Fe2+
26.7
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Zn2+
60
S-D-lactoylglutathione
-
mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
67
S-D-lactoylglutathione
-
mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4
74
S-D-lactoylglutathione
-
mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
136
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Fe added, pH 7.2, 25°C
142
S-D-lactoylglutathione
-
-
149.9
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Fe2+
168
S-D-lactoylglutathione
recombinant enzyme grown in medium supplemented with Mn2+, pH 7.2, 25°C
168.8
S-D-lactoylglutathione
enzyme otained from LB medium
170
S-D-lactoylglutathione
-
in 10 mM MOPS buffer at pH 7.2, at 25 °C
171
S-D-lactoylglutathione
-
mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
209.9
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Zn2+
222
S-D-lactoylglutathione
-
mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
240
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C
280
S-D-lactoylglutathione
-
285
S-D-lactoylglutathione
-
mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
301
S-D-lactoylglutathione
-
322
S-D-lactoylglutathione
recombinant mutant L9A, pH 7.2, 25°C
359
S-D-lactoylglutathione
recombinant enzyme grown in medium supplemented with Fe2+, pH 7.2, 25°C
370
S-D-lactoylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
375
S-D-lactoylglutathione
-
wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
386
S-D-lactoylglutathione
recombinant mutant K65A, pH 7.2, 25°C
394.9
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Mn2+
408
S-D-lactoylglutathione
recombinant enzyme grown in medium not supplemented with metal ions, pH 7.2, 25°C
421
S-D-lactoylglutathione
recombinant mutant W57N, pH 7.2, 25°C
426
S-D-lactoylglutathione
recombinant mutant W57D, pH 7.2, 25°C
450
S-D-lactoylglutathione
-
-
466
S-D-lactoylglutathione
-
-
470
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C
484
S-D-lactoylglutathione
-
-
484
S-D-lactoylglutathione
mutant R248W, pH 7.2, 25°C
510
S-D-lactoylglutathione
-
recombinant mutant Y175F, pH 7.1, 37°C
600
S-D-lactoylglutathione
mutant R225A, pH 7.2, 25°C
605
S-D-lactoylglutathione
-
wild-type enzyme from mitochondria
723
S-D-lactoylglutathione
-
recombinat enzyme from mitochondria
723
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
727
S-D-lactoylglutathione
-
-
780
S-D-lactoylglutathione
-
recombinant wild-type enzyme, pH 7.1, 37°C
918
S-D-lactoylglutathione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
979
S-D-lactoylglutathione
-
recombinat enzyme from cytosol
979
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
1190
S-D-lactoylglutathione
mutant N178A, pH 7.2, 25°C
1760
S-D-lactoylglutathione
mutant K142A, pH 7.2, 25°C
3930
S-D-lactoylglutathione
wild-type enzyme, pH 7.2, 25°C
6780
S-D-lactoylglutathione
mutant C140A, pH 7.2, 25°C
16
S-D-lactoyltrypanothione

wild type protein, no activity observed with S-D-lactoylglutathione, pH not specified in the publication, temperature not specified in the publication
241
S-D-lactoyltrypanothione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
25.8
S-D-mandeloylglutathione

-
recombinant enzyme from mitochondria
25.8
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
35.1
S-D-mandeloylglutathione
-
recombinant enzyme from cytosol
35.1
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
38.1
S-D-mandeloylglutathione
-
wild-type enzyme from mitochondria
74
S-D-mandeloylglutathione
-
-
183
S-D-mandeloylglutathione
-
-
64.3
S-Lactoylglutathione

25°C
70
S-Lactoylglutathione
25°C
119.6
S-Lactoylglutathione
25°C
129
S-Lactoylglutathione
-
136
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium in presence of iron
240
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without in presence of zinc
470
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without added metal ion
508
S-Lactoylglutathione
-
pH and temperature not specified in the publication
780
S-Lactoylglutathione
recombinant enzyme
188
S-mandeloylglutathione

enzyme from erythrocytes
201
S-mandeloylglutathione
recombinant enzyme
755
S-mandeloylglutathione
enzyme from erythrocytes
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