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Enzyme Nomenclature
Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase
for references in articles please use BRENDA:EC3.1.2.6
Word Map on EC 3.1.2.6
- 3.1.2.6
- methylglyoxal
- gsh
- s-d-lactoylglutathione
- d-lactate
- monodehydroascorbate
-
glutathione-dependent
- mdhar
- dehydroascorbate
-
d-lactic
- hemithioacetal
-
4.4.1.5
- trypanothione
- metallo-beta-lactamase
- lactoylglutathione
- 2-oxoaldehydes
-
thiolester
- medicine
- pharmacology
- biotechnology
- agriculture
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.1.2.6
-
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RECOMMENDED NAME
GeneOntology No.
hydroxyacylglutathione hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
mechanism
-
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
-
-
-
-
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
active site residue Tyr175 contributes to the binding of glutathione derivatives by its hydroxyl group which forms hydrogen binds to the glycine in the glutathione moiety
-
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
reaction mechanism
-
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
active site and reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
9025-90-5
-
9025-92-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytoslic isozyme; overexpresssion in minmal media containing either Zn, Fe, or Mn
-
-
-
134161, 134162, 134169, 134172, 134173, 134178, 134180, 134183, 37413, 650317, 679014, 708728, 80981, 80984
-
-
cytosolic and mitochondrial isozyme, both encoded by gene HAGH for hydroxyacylglutathione hydrolase
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ectopic expression of OsGLYII-2 in Escherichia coli and tobacco provides improved tolerance against salinity and dicarbonyl stress indicating towards its role in abiotic stress tolerance; OsGLYII-2 is able to functionally complement a yeast GLY II mutant
metabolism
-
drought stress slightly decreases activity, selenium-pretreated seedlings maintain higher activity at either level of drought
physiological function
physiological function
-
assembly of a specific metal-enriched form of GLX2 may be a mechanism to regulate the enzyme activity in vivo
physiological function
-
a DELTAgloB mutant is as tolerant of methylglyoxal as the parent, despite having the same degree of inhibition of MG detoxification as a DELTAgloA strain. The DgloB mutant grows at a similar rate to the parent in K0.2 minimal medium and exhibits no obvious growth phenotype. Addition of 0.7 mM MG to both parent andmutant strains, in early exponential phase, causes immediate growth inhibition without recovery over the course of the experiment. Mehtylglyoxal disappeares from the medium in a linear fashion and the rate is greatly reduced in DELTAgloB cultures. Increased expression of GlxII from a multicopyplasmid sensitizes Escherichia coli to methylglyoxal. S-lactoylglutathione pools, KefGB potassium efflux system activity and cytoplasmic pH are linked and very sensitive to changes in the activity of GlxI and GlxII
physiological function
-
assembly of a specific metal-enriched form of GLX2 may be a mechanism to regulate the enzyme activity in vivo
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bis-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
mono-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
N,S-bisfluorenylmethoxycarbonylglutathione + H2O
9-fluorenylmethoxycarboxylate + glutathione
-
-
-
-
?
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-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
-
-
-
?
S-D-lactoylglutathione
D-lactate + glutathione
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactic acid + glutathione
-
-
-
?
S-D-lactoyltrypanothione + H2O
D-lactate + trypanothione
-
additionally S-D-lactoylglutathione used by mutant Y291R/C294K
-
-
?
S-glycolylglutathione + H2O
? + glutathione
hydrolysis at about half the rate of S-lactoylglutathione
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
-
-
-
?
S-lactonylglutathione + H2O
? + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-m-nitrobenzyloxycarbonylglutathione + H2O
m-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelic acid + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-o-nitrobenzyloxycarbonylglutathione + H2O
o-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-p-nitrobenzyloxycarbonylglutathione + H2O
p-nitrobenzyloxycarboxylate + glutathione
-
-
-
-
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
S-D-lactoylglutathione
-
-
?
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
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
lactoylglutathione + H2O
D-lactate + glutathione
enzyme does not show saturation kinetics up to 5 mM
-
-
?
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
-
-
-
?
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
Q940L0
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
hydrolysis at about half the rate of S-lactoylglutathione
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
55.6% of the activity with S-lactoylglutathione
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
8.6% of the activity with S-lactoylglutathione
-
-
?
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
-
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
-
used by mutant Y291R/C294K
-
-
?
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
-
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
-
-
?
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
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
-
-
?
S-formylglutathione + H2O
formate + glutathione
-
37.7% of the activity with S-lactoylglutathione
-
-
?
S-glycerylglutathione + H2O
glycerate + glutathione
-
61.6% of the activity with S-lactoylglutathione
-
-
?
S-glycoloylglutathione + H2O
glycolate + glutathione
-
38.6% of the activity with S-lactoylglutathione
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
preferred substrae
-
-
?
S-lactoylglutathione + H2O
D-lactate + 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
-
13.5% of the activity with S-lactoylglutathione
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
29.2% of the activity with S-lactoylglutathione
-
-
?
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
?
-
-
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
?
-
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.
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
Q581U6
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
Q581U6
-
-
-
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
Q581U6
-
-
-
?
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
-
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
-
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.
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe3+
Iron
Mn2+
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
Zinc
Zn2+
additional information
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+
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
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+
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
-
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
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+
-
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+
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
-
the cytosolic and mitochondrial glxII from Arabidopsis thaliana contain varying ratios of Zn2+, Fe2+ and Mn2+ and exhibit broad metal activation
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
cardiolipin
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
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
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
N-(9-fluorenylmethoxycarbonyl)-S-phenylmethoxycarbonylglutathione
-
N-phenylmethoxycarbonyl-S-(9-fluorenylmethoxycarbonyl)glutathione
-
phosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
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
2,4,6-Trinitrobenzenesulfonate
-
N-acetyl-S-(p-bromobenzyl)glutathione protects
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
-
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
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
50% inhibition at 0.0016 mM; 50% inhibition at 0.02 mM
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the Fe(III)Zn(II) complex [(2-{[bis(2-pyridylmethyl)amino]methyl}-6-[{[2-hydroxyphenyl)methyl]-(2-pyridylmethyl)amino}methyl]-4-methylphenolFe(III)Zn(II)(micro-O2C2H3)2]ClO4 promotes thioester hydrolysis
-
additional information
-
coldnesse enhances gly II transcript expression; drought enhances gly II transcript expression; salt enhances gly II transcript expression; zinc stress enhances gly II transcript expression
-
additional information
-
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
-
additional information
-
rosmarinic acid administration to fructose-fed mice brings the activity of glyoxalase II to near normal. Normalization of the glyoxalase system can be attributed to reduction in the formation of oxoaldehydes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
bis-(lactoyl)trypanothione
pH 7.2, 25°C; recombinant enzyme, pH 7.2, 25°C
0.32
S-D-lactoylgutathione
-
pH 6.5, 30°C, substrate concentration 1.5-3 mM
0.108
mono-(lactoyl)trypanothione
pH 7.2, 25°C; 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
0.162
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
0.255
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
0.05
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
0.703
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
0.0722
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
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
0.14
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C
0.151
S-D-lactoylglutathione
recombinant mutant L9A, pH 7.2, 25°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
0.275
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+
0.318
S-D-lactoylglutathione
recombinant mutant W57N, pH 7.2, 25°C
0.408
S-D-lactoylglutathione
enzyme otained from LB medium
0.439
S-D-lactoylglutathione
-
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
0.463
S-D-lactoylglutathione
enzyme obtained from minimal medium supplemented with Fe2+
0.6
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, medium with Fe added, pH 7.2, 25°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
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
0.0365
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
0.139
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without in presence of zinc
0.209
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium without added metal ion
0.254
S-Lactoylglutathione
-
pH and temperature not specified in the publication, Vmax: 1 mmol/min/mg
0.6
S-Lactoylglutathione
-
pH 7.2, 25°C, growth on minimal medium in presence of iron
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of the enzyme in situ, cells being permeabilized by digitonin
-
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numver is pH-independent in the range pH 6-9.3
-
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
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
285
S-D-lactoylglutathione
-
mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
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
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
470
S-D-lactoylglutathione
-
recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C
723
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
918
S-D-lactoylglutathione
-
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
979
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
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
pH not specified in the publication, temperature not specified in the publication
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
S-D-lactoylglutathione
-
mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
26
S-D-lactoylglutathione
-
mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
30
S-D-lactoylglutathione
-
mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4
41
S-D-lactoylglutathione
-
mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
810
S-D-lactoylglutathione
-
mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
2090
S-D-lactoylglutathione
-
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
2400
S-D-lactoylglutathione
-
mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
3300
S-D-lactoylglutathione
-
wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8
8700
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
10000
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
180
S-D-lactoyltrypanothione
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
1600
S-D-lactoyltrypanothione
-
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
710
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
2200
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000031
D-lactate
-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
0.0023
N,S-bis-(phenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
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
0.014
S-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.0049
S-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
glutathione
Salmonella enterica subsp. enterica serovar Typhimurium
-
Mn-GloB, in 10 mM MOPS buffer, 0.2 M NaCl, pH 7.2, at 30 °C
additional information
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
-
Fe- and Zn-GloB is inhibited at submillimolar concentrations of glutathione, in 10 mM MOPS buffer, 0.2 M NaCl, pH 7.2, at 30 °C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
clone B2 (pHD678/GLXII) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.05
clone B4 (p2T7/GLXII) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.21
wild-type minus tetracycine, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.22
clone B4 (p2T7/GLXII) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference; clone K3 (pHD678) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.23
clone K3 (pHD678) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.27
clone B2 (pHD678/GLXII) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
63
S-hydroxyglutaryltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
73
S-glycolyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
92
S-bis-lactoyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
96
S-propionyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
115
S-lactoylglutathionylspermidine as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
117
S-acetyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
additional information
additional information
activity of wild-type and mutants in crude extracts
additional information
-
activity is determined spectrophotometrically at 240 nm, the hepatic glyoxalase II activity of the 3'-methyl-4-dimethylaminoazobenzene group (10 weeks fed) is almost the same as that of the control group; determined spectrophotometrically at 240 nm, glyoxalase II activities of 2-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.3 times higher than that of the control rats; determined spectrophotometrically at 240 nm, glyoxalase II activities of 4'-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.4 times higher than that of the control rats
additional information
after the onset of interfering RNAi, GLX II activity in extracts of bloodstream cells is decreased to about 20% when compared to the respective non-induced cells; overexpression of GLX II has no apparent effect on Trypanosoma brucei
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
saturation kinetic behavior for the phosphate diester hydrolysis reaction
7 - 8
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 7.7
Q940L0
pH 6.3: aout 65% of maximal activity, pH 7.7: about 80% of maximal activity
7 - 9
-
saturation kinetic behavior for the thioester hydrolysis reaction. At pH 9.0 ligand exchange at the zinc center via deprotonation of the alpha-hydroxy group of the thioester to give an equilibrium amount of a zinc alkoxide species
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
-
25°C: about 60% of maximal activity, 55°C: about 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
culture-adapted bloodstream and procyclic Trypanosoma brucei of cell line 449, descendants of the strain Lister 427, stably transfected with pHD449 encoding the tetracycline repressor
for RNA interference experiments a cell line (427 1313 514) is employed that encodes a second tetracycline repressor and constitutively expresses a T7-polymerase
-
activity decreases after a two-week exposure to a sublethal concentration (1.6 mM) of Cu2+ compared to untreated control specimens in marine water
-
activity is unchanged after a two-week exposure to a sublethal concentration (1.6 mM) of Cu2+ compared to untreated control specimens in marine water
-
transcription of glyoxalase II is about threefold increased in cancerous tissue comared to noncancerous tissue. Glyoxalase II activity is significantly lower in pathological tissues than in normal ones
in the lung of diabetic rats, the increase in GLO I activity is not associated to a concomitant increase in GLO II activity. This finding could result in a defective methylglyoxal detoxification
-
increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
-
increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
-
differential expression of mitochondrial and cytosolic gly II