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acetoacetylglutathione hydrolase
Germ cell specific protein
hydrolase, acetoacetylglutathione
hydrolase, hydroxyacylglutathione
hydroxyacylglutathione hydrolase
Round spermatid protein RSP29
S-2-hydroxylacylglutathione hydrolase
acetoacetylglutathione hydrolase

-
-
-
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
acetoacetylglutathione hydrolase
-
-
acetoacetylglutathione hydrolase
-
Germ cell specific protein

-
-
-
-
Germ cell specific protein
-
-
Germ cell specific protein
-
Germ cell specific protein
-
-
Germ cell specific protein
-
-
Germ cell specific protein
-
Germ cell specific protein
-
-
Germ cell specific protein
-
-
Germ cell specific protein
-
Germ cell specific protein
-
-
Germ cell specific protein
-
GLO II

-
-
-
-
GloB

-
gene name
Glx II

-
-
GLX2

-
-
GLX2-2

-
-
GlxII

-
-
glyoxalase II

-
-
-
-
glyoxylase II

-
-
glyoxylase II
-
gene glo2
hydrolase, acetoacetylglutathione

-
-
-
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
hydrolase, acetoacetylglutathione
-
-
hydrolase, acetoacetylglutathione
-
hydrolase, hydroxyacylglutathione

-
-
-
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
hydrolase, hydroxyacylglutathione
-
-
hydrolase, hydroxyacylglutathione
-
hydroxyacylglutathione hydrolase

-
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
-
-
hydroxyacylglutathione hydrolase
-
-
hydroxyacylglutathione hydrolase
-
hydroxyacylglutathione hydrolase
-
-
Round spermatid protein RSP29

-
-
-
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
Round spermatid protein RSP29
-
-
Round spermatid protein RSP29
-
S-2-hydroxylacylglutathione hydrolase

-
-
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
S-2-hydroxylacylglutathione hydrolase
-
-
S-2-hydroxylacylglutathione hydrolase
-
additional information

-
the enzyme belongs to the metallo-beta-lactamase superfamily
additional information
enzyme belongs to the metallo-beta-lactamase superfamily
additional information
enzyme is a member of the zinc metallohydrolase family with a beta-lactamase fold
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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
-
-
-
?
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 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-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-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
?
-
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 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
-
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
-
second step in the glyoxalase system
-
-
?
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
-
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
-
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
-
second step in the glyoxalase system
-
-
?
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-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
Q84XQ5
-
-
-
?
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
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
4.8% of the activity with S-lactoylglutathione
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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 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 anion
S-acetyltrypanothione + H2O
acetate + trypanothione
Q581U6
-
-
-
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
Q581U6
-
-
-
?
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
Q581U6
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
Q581U6
-
-
-
?
S-lactoylglutathionylspermidine + H2O
?
Q581U6
-
-
-
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
Q581U6
-
-
-
?
additional information
?
-
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
Q940L0
-
-
?
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
O35952
-
-
-
?
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
Q16775
-
-
?
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
Q6KF36
enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis
-
?
additional information

?
-
O24496
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
?
-
-
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
?
-
Q940L0
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
?
-
Q581U6
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
?
-
Q581U6
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.
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+

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+
-
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+

0.1 mol per mol of protein, R248W mutant enzyme
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+
-
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 ironthiolate 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+

-
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+
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+
-
; 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+
-
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+
-
essential role in catalytic mechanism
Zn2+
-
contains a binuclear Zn/Fe centre in its active site
Zn2+
0.05 mol per mol of enzyme; 1.7 mol per mol of enzyme
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
-
metal binding structure, and metal content under different media conditions, overview, enzyme shows positive cooperative metal binding; 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
not: manganese
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
sequence contains the highly conserved metal binding motif THXHXDH; 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
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
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
-
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

-
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
-
-
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
-
benzyloxycarbonyl-S-derivatives are stronger inhibitors than the p-chlorophenacyl S-derivative
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.086
bis-(lactoyl)trypanothione
pH 7.2, 25°C; recombinant enzyme, pH 7.2, 25°C
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
0.009 - 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
-
0.039
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; recombinant enzyme, pH 7.2, 25°C
0.152
S-(2-hydroxyacyl)glutathione

-
mitochondrial isozyme, pH 7.2, 25°C
0.152
S-(2-hydroxyacyl)glutathione
-
cytosolic isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid
0.162
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
-
mitochondrial 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
0.201
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
-
-
0.15
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
0.177
S-D-lactoylglutathione
-
-
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+
0.251
S-D-lactoylglutathione
-
-
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
0.29
S-D-lactoylglutathione
-
-
0.295
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Zn2+
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
-
-
0.598
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
0.009
S-D-mandeloylglutathione

-
-
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
Q84XQ5
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
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
0.19
S-lactylglutathione

-
-
0.19
S-lactylglutathione
-
enzyme from liver
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
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics of the enzyme in situ, cells being permeabilized by digitonin
-
additional information
additional information
kinetics
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
82
S-Acetoacetylglutathione
-
-
10.6 - 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
-
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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0.006
cardiolipin
-
cytosolic isozyme, pH 7.2, 25°C
0.000031
D-lactate
-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
2.3
di-carbobenzoxyglutahione
-
-
-
0.0002
dioleoyl phosphatidic acid
-
cytosolic isozyme, pH 7.2, 25°C
0.0022
dipalmitoylphosphatidylserine
-
cytosolic isozyme, pH 7.2, 25°C
14 - 49
glutathione ethyl ester
0.00089 - 0.0028
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
0.0023
N,S-bis-(phenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.89
N,S-bis-FMOC-glutathione
-
-
0.0017
N-(9-fluorenylmethoxycarbonyl)-S-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.015
N-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.002
N-phenylmethoxycarbonyl-S-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.0056
N-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.055
phosphatidylserine
-
cytosolic isozyme, pH 7.2, 25°C
0.014
S-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.0005 - 0.035
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
0.0007 - 0.05
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
0.006
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
25°C
1.3
S-(p-azidophenacyl)glutathione
25°C
1.5
S-hexylglutathione
25°C
0.0049
S-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
1.9
S-propylglutathione
25°C
3.5
glutathione

-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
13
glutathione
-
inhibitor binding to the occupied enzyme, at 25°C, pH 6.8
14
glutathione ethyl ester

-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
49
glutathione ethyl ester
-
inhibitor binding to the occupied enzyme, at 25°C, pH 6.8
0.00089
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione

recombinant wild-type enzyme, pH 7.2, 25°C
0.0021
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
recombinant mutant W57D, pH 7.2, 25°C
0.0027
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
recombinant mutants W57N and K65A, pH 7.2, 25°C
0.0028
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
recombinant mutant L9A, pH 7.2, 25°C
0.0005
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione

25°C
0.0012
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
recombinant wild-type enzyme, pH 7.1, 37°C
0.03
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
25°C
0.035
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
recombinant mutant Y175F, pH 7.1, 37°C
0.0007
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione

25°C
0.05
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
25°C
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