Any feedback?
No. of entries
Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase
for references in articles please use BRENDA:EC3.1.2.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.2 Thioester hydrolases
3.1.2.6 hydroxyacylglutathione hydrolase
IUBMB Comments
Also hydrolyses S-acetoacetylglutathione, but more slowly.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.1.2.6
- methylglyoxal
- gsh
- s-d-lactoylglutathione
-
glyoxalases
- d-lactate
-
glycation
-
glutathione-dependent
- dehydroascorbate
- monodehydroascorbate
- hemithioacetal
-
d-lactic
- mdhar
-
dicarbonyls
- trypanothione
- 2-oxoaldehydes
-
4.4.1.5
- lactoylglutathione
- metallo-beta-lactamase
- drug development
- biotechnology
- pharmacology
- medicine
- agriculture
showSynonyms
glyoxalase ii, glyoxalase 2, gly ii, glyii, glxii, glx2-2, gloii, hydroxyacylglutathione hydrolase, cgloii, glo ii, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoacetylglutathione hydrolase
EC 3.1.2.8
-
-
formerly
-
Germ cell specific protein
GLO II
Glo2
GloB
Glx II
GLX2
GLX2-2
GlxII
Gly II
GLYII
glyoxalase II
glyoxylase II
HAGH
hydrolase, acetoacetylglutathione
hydrolase, hydroxyacylglutathione
hydroxyacylglutathione hydrolase
Round spermatid protein RSP29
S-2-hydroxylacylglutathione hydrolase
additional information
acetoacetylglutathione hydrolase
-
-
-
-
Germ cell specific protein
-
-
-
-
GLO II
-
-
-
-
glyoxalase II
-
-
-
-
hydrolase, acetoacetylglutathione
-
-
-
-
hydrolase, hydroxyacylglutathione
-
-
-
-
hydroxyacylglutathione hydrolase
-
-
-
Round spermatid protein RSP29
-
-
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
active site and reaction mechanism
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
reaction mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
methylglyoxal degradation I, methylglyoxal degradation VIII
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9025-90-5
-
9025-92-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O
[[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoate
Substrates: i.e. POM-HEX, substrate is a prodrug of the compound HEX, which inhibits the glycolytic enzyme enolase
Products: -
Products: -
?
bis-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
bis-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
Substrates: preferred substrate
Products: trypathione is bis(glutathionyl)spermidine
Products: trypathione is bis(glutathionyl)spermidine
?
D-lactoyltrypanothione + H2O
D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O
fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O
fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis(methoxyacetate) + H2O
fluorescein-3'-oxymethyl methoxyacetate + methoxyacetate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis(propoxyacetate) + H2O
fluorescein-3'-oxymethyl propoxyacetate + propoxyacetate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis[(ethylsulfanyl)acetate] + H2O
fluorescein-3'-oxymethyl (ethylsulfanyl)acetate + (ethylsulfanyl)acetate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene bis[(methylsulfanyl)acetate] + H2O
fluorescein-3'-oxymethyl (methylsulfanyl)acetate + (methylsulfanyl)acetate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene dibutanoate + H2O
fluorescein-3'-oxymethyl butanoate + butanoate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene dihexanoate + H2O
fluorescein-3'-oxymethyl hexanoate + hexanoate
Substrates: -
Products: -
Products: -
?
fluorescein-3',6'-bis(oxy)methylene dipentanoate + H2O
fluorescein-3'-oxymethyl pentanoate + pentanoate
Substrates: -
Products: -
Products: -
?
mono-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
Substrates: preferred substrate
Products: trypathione is bis(glutathionyl)spermidine
Products: trypathione is bis(glutathionyl)spermidine
?
N,S-bisfluorenylmethoxycarbonylglutathione + H2O
9-fluorenylmethoxycarboxylate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione + H2O
beta-ethoxy-alpha-D-hydroxybutyrate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
?
Substrates: 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.
Products: -
Products: -
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
N-hydroxy-N-bromophenylcarbamate + glutathione
-
Substrates: weak substrate
Products: -
Products: -
?
S-acetyltrypanothione + H2O
acetate + trypanothione
Substrates: -
Products: -
Products: -
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactic acid + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
Substrates: -
Products: -
Products: -
r
S-D-lactoyltrypanothione + H2O
D-lactate + trypanothione
Substrates: additionally S-D-lactoylglutathione used by mutant Y291R/C294K
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
? + glutathione
Substrates: -
Products: -
Products: -
?
S-glyceroylglutathione + H2O
glycerate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-glycolylglutathione + H2O
? + glutathione
Substrates: hydrolysis at about half the rate of S-lactoylglutathione
Products: -
Products: -
?
S-glycolyltrypanothione + H2O
glycolate + trypanothione
Substrates: -
Products: -
Products: -
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
Substrates: -
Products: -
Products: -
?
S-L-glyceroylglutathione + H2O
glycerate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-lactonylglutathione + H2O
? + glutathione
Substrates: hydrolysis about 10fold lower than of S-lactoylglutathione
Products: -
Products: -
?
S-lactoylglutathionylspermidine + H2O
?
Substrates: -
Products: -
Products: -
?
S-m-nitrobenzyloxycarbonylglutathione + H2O
m-nitrobenzyloxycarboxylate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelic acid + glutathione
Substrates: hydrolysis about 10fold lower than of S-lactoylglutathione
Products: -
Products: -
?
S-o-nitrobenzyloxycarbonylglutathione + H2O
o-nitrobenzyloxycarboxylate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-p-nitrobenzyloxycarbonylglutathione + H2O
p-nitrobenzyloxycarboxylate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
Substrates: -
Products: -
Products: -
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: S-D-lactoylglutathione
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: S-D-lactoylglutathione
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
Substrates: little activity with this substrate
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: S-D-lactoylglutathione
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: reaction is rate-limiting, methylglyoxal bypass of glycolysis
Products: -
Products: -
r
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
lactoylglutathione + H2O
D-lactate + glutathione
Substrates: enzyme does not show saturation kinetics up to 5 mM
Products: -
Products: -
?
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
-
Substrates: -
Products: -
Products: -
ir
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: second step in the glyoxalase system
Products: regeneration of glutathione for the first step in the glyoxalase system
Products: regeneration of glutathione for the first step in the glyoxalase system
ir
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: the enzyme is involved in the detoxification process converting reactive dicarbonyl compounds such as methylglyoxal to less reactive hydroxyl acids
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
Substrates: hydrolysis at about half the rate of S-lactoylglutathione
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: 55.6% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
Substrates: hydrolysis about 10fold lower than of S-lactoylglutathione
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
-
Substrates: 8.6% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
Substrates: -
Products: -
Products: -
?
S-acetylglutathione + H2O
acetate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: used by mutant Y291R/C294K
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: 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
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: enzyme is involved in the detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: enzyme is involved in the detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-formylglutathione + H2O
formate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-formylglutathione + H2O
formate + glutathione
-
Substrates: 37.7% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-formylglutathione + H2O
formate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-glycerylglutathione + H2O
glycerate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-glycerylglutathione + H2O
glycerate + glutathione
-
Substrates: 61.6% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-glycoloylglutathione + H2O
glycolate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-glycoloylglutathione + H2O
glycolate + glutathione
-
Substrates: 38.6% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: preferred substrae
Products: -
Products: -
?
S-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: 4.8% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-mandeloylglutathione + H2O
mandelate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
-
Substrates: thioester hydrolysis is promoted by an Fe(III)Zn(II) complex
Products: -
Products: -
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
-
Substrates: thioester hydrolysis promoted by a mononuclear zinc complex
Products: -
Products: -
?
S-propionylglutathione + H2O
propionate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-propionylglutathione + H2O
propionate + glutathione
-
Substrates: 13.5% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-propionylglutathione + H2O
propionate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-succinylglutathione + H2O
succinate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-succinylglutathione + H2O
succinate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-succinylglutathione + H2O
succinate + glutathione
-
Substrates: 29.2% of the activity with S-lactoylglutathione
Products: -
Products: -
?
S-succinylglutathione + H2O
succinate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-succinylglutathione + H2O
succinate + glutathione
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme participates in the detoxification of cytotoxic and mutagenic 2-oxoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: S-formylglutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: S-formylglutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the rate limiting step of the glyoxalase pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows broad substrate specificity with a preference for 2-hydoxy thiol esters
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not promote S-glutathionylation of GAPDH
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: S-lactoylglutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system may play an important role in the regulation of cell division and differentiation
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: 4-nitrophenyl acetate, 4-nitrophenyl butanoate, 4-nitrophenyl trimethylacetate
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: reaction is rate-limiting, methylglyoxal bypass of glycolysis
Products: -
Products: -
r
S-acetyltrypanothione + H2O
acetate + trypanothione
Substrates: -
Products: -
Products: -
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
Substrates: -
Products: -
Products: -
r
S-glycolyltrypanothione + H2O
glycolate + trypanothione
Substrates: -
Products: -
Products: -
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
Substrates: -
Products: -
Products: -
?
S-lactoylglutathionylspermidine + H2O
?
Substrates: -
Products: -
Products: -
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate
-
Substrates: -
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: enzyme is part of the glyoxalase system and involved in detoxification of methylglyoxal
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: second step in the glyoxalase system
Products: regeneration of glutathione for the first step in the glyoxalase system
Products: regeneration of glutathione for the first step in the glyoxalase system
ir
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
-
Substrates: the enzyme is involved in the detoxification process converting reactive dicarbonyl compounds such as methylglyoxal to less reactive hydroxyl acids
Products: -
Products: -
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
-
Substrates: second step in the glyoxalase system
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: -
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: enzyme is involved in the detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
-
Substrates: enzyme is involved in the detoxification of methylglyoxal
Products: -
Products: -
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
Substrates: enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme participates in the detoxification of cytotoxic and mutagenic 2-oxoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the rate limiting step of the glyoxalase pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system may play an important role in the regulation of cell division and differentiation
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: OsglyII gene expression is stimulated within 15 min in response to various abiotic stresses as well as treatment with abscisic acid or salicylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant glyoxalase II hydrolyzes the trypanothione-thioesters of methylglyoxal, glyoxal and 4,5-dioxovalerate, substrates of the classical glyoxalase system, with high efficiency
Products: -
Products: -
?
additional information
?
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
the enzyme activity is increased by 23% and 53% at 0.25 and 0.5 mM Cd2+, respectively
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+
-
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)
Fe2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
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+
0.56 mol/mol of protein, presence of a binuclear Zn/Fe centre in the All0580 active site
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+
-
MnII-thiolate bonds are less covalent and weaker than ironthiolate bonds
Mn2+
-
stimulates activity (0.1 mM: 5-fold, 1mM: 7-fold)
Mn2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
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+
-
0.5 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+
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+
-
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+
0.6 mol/mol of protein, presence of a binuclear Zn/Fe centre in the All0580 active site
Zn2+
-
behavior of Zn-GloB resembles that of Fe-GloB
Zn2+
-
bound, molar ratio 0.65 Zn2+:1
Zn2+
proteins expressed in minimal medium supplemented with Zn2+, Mn2+ or Fe2+ show similar activities
Zn2+
two zink ions are found near the active site. Zn1 is coordinated by residues His-54, His-56, and His-131, while Zn2 is coordinated by Asp-58, His-59, and His-191
additional information
-
metal binding structure, and metal content under different media conditions, overview, enzyme shows positive cooperative metal binding
additional information
-
overexpresssion of enzyme in minmal media containing either Zn, Fe, or Mn results in enzyme binding an average of 1 equivalent of metal ion, and presence of antiferomagnetically and ferromagnetically coupled dinuclear metal centers. Enzyme does not exist as a mononuclear metal ion containing enzyme, and shows positive cooperativity in metal binding
additional information
-
the cytosolic and mitochondrial glxII from Arabidopsis thaliana contain varying ratios of Zn2+, Fe2+ and Mn2+ and exhibit broad metal activation
additional information
enzyme possesses a binuclear active site, metal ion binding structure and kinetics, overview
additional information
-
enzyme possesses a binuclear active site, metal ion binding structure and kinetics, overview
additional information
-
the enzyme is almost unaffected by Mn2+, Mg2+, Ni2+, Fe2+ or Fe3+
additional information
the enzyme contains the highly conserved metal binding motif THXHXDH, total metal ions per mol of enzyme: 1.5 for the His-tagged enzyme, 0.7-0.9 for the free enzyme
additional information
-
the enzyme contains the highly conserved metal binding motif THXHXDH, total metal ions per mol of enzyme: 1.5 for the His-tagged enzyme, 0.7-0.9 for the free enzyme
additional information
sequence contains the highly conserved metal binding motif THXHXDH
additional information
-
sequence contains the highly conserved metal binding motif THXHXDH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
Cd2+
-
the enzyme activity decreases by 20% and 32% at 0.5 and 1.0 mM Cd2+, respectively
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
-
additional information
-
the enzyme is not sensitive against ionic strength
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
A possible regulatory role of 17beta-estradiol and tamoxifen on glyoxalase I and glyoxalase II genes expression in MCF7 and BT20 human breast cancer cells.
Carcinogenesis
Changes in concentrations of methylglyoxal, D-lactate and glyoxalase activities in liver and plasma of rats fed a 3'-methyl-4-dimethylaminoazobenzene-rich diet.
Carcinogenesis
Glyoxalase 2 drives tumorigenesis in human prostate cells in a mechanism involving androgen receptor and p53-p21 axis.
Carcinoma
Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas.
Carcinoma, Ovarian Epithelial
Germ cell specific protein VASA is over-expressed in epithelial ovarian cancer and disrupts DNA damage-induced G2 checkpoint.
Diabetes Complications
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Diabetes Complications
Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
Diabetes Mellitus
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Diabetes Mellitus
The Relationship Between Alanerv(®) Consumption and Erythrocytes' Glyoxalases I and II Activities and The Level of Some Serum Markers of Carbonyl Stress in Post-Acute Stroke Patients Undergoing Rehabilitation.
Diabetes Mellitus, Type 1
Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
Diabetes Mellitus, Type 2
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Elliptocytosis, Hereditary
Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis.
hydroxyacylglutathione hydrolase deficiency
Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis.
hydroxyacylglutathione hydrolase deficiency
Glyoxalase 2 deficiency in the erythrocytes of a horse: 1H NMR studies of enzyme kinetics and transport of S-lactoylglutathione.
hydroxyacylglutathione hydrolase deficiency
Studies of erythrocyte glyoxalase II in various domestic species: discovery of glyoxalase II deficiency in the horse.
Leishmaniasis, Visceral
Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs.
Leukemia
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Malaria
Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis.
Melanoma
[Activity of glyoxalase and glyoxalase II under the effect of toxohormone from melanoma]
Neoplasms
Glyoxalase 2 drives tumorigenesis in human prostate cells in a mechanism involving androgen receptor and p53-p21 axis.
Neoplasms
Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy.
Neoplasms
S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II.
Neoplasms
The tumor promoting phorbol diester, 12-O-tetradecanoylphorbol-13-acetate (TPA) increases glyoxalase I and decreases glyoxalase II activity in human polymorphonuclear leukocytes.
Obesity
Glyoxalase 1 and glyoxalase 2 activities in blood and neuronal tissue samples from experimental animal models of obesity and type 2 diabetes mellitus.
Persistent Infection
Definitive host influences the proteomic profile of excretory/secretory products of the trematode Echinostoma caproni.
Prostatic Hyperplasia
Glyoxalase activities in tumor and non-tumor human urogenital tissues.
Prostatic Neoplasms
Glyoxalase 2 Is Involved in Human Prostate Cancer Progression as Part of a Mechanism Driven By PTEN/PI3K/AKT/mTOR Signaling With Involvement of PKM2 and ER?.
Sarcoma
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Sarcoma 180
Further studies on liver glyoxalase I and glyoxalase II. Activity in mice bearing sarcoma 180 and L1210 leukemia.
Stroke
The Relationship Between Alanerv(®) Consumption and Erythrocytes' Glyoxalases I and II Activities and The Level of Some Serum Markers of Carbonyl Stress in Post-Acute Stroke Patients Undergoing Rehabilitation.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
S-D-lactoylgutathione
-
pH 6.5, 30°C, substrate concentration 1.5-3 mM
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
-
cytosolic isozyme, pH 7.2, 25°C, in presence of dipalmitoylphosphatidylserine
0.191
S-(2-hydroxyacyl)glutathione
-
mitochondrial isozyme, pH 7.2, 25°C, in presence of cardiolipin
0.255
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 in presence of liposomes consisting of different phospholipids
-
additional information
additional information
-
kinetics in presence of liposomes consisting of different phospholipids
-
additional information
additional information
-
kinetics of the enzyme in situ, cells being permeabilized by digitonin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
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
additional information
0.22
clone K3 (pHD678) minus tetracycline, 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
additional information
activity of wild-type and mutants in crude extracts
additional information
-
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
-
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
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
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
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
additional information
overexpression of GLX II has no apparent effect on Trypanosoma brucei
additional information
-
overexpression of GLX II has no apparent effect on Trypanosoma brucei
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7 - 8
7.2
6.5
-
saturation kinetic behavior for the phosphate diester hydrolysis reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 7.7
pH 6.3: aout 65% of maximal activity, pH 7.7: about 80% of maximal activity
6.5 - 8
enhanced enzyme activity in the pH range of 6.5-8.0
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
-
25°C: about 60% of maximal activity, 55°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme possesses both metallo-beta-lactamase (cf. EC 3.5.2.6) and glyoxalase II activities with similar catalytic efficiencies
UniProt
brenda
overexpresssion in minmal media containing either Zn, Fe, or Mn
-
-
brenda
recombinant enzyme expressed in Escherichia coli
Swissprot
brenda
-
-
-
brenda
cytosolic and mitochondrial isozyme, both encoded by gene HAGH for hydroxyacylglutathione hydrolase
UniProt
brenda
HAGH gene encodes both cytosolic and mitochondrial forms of glyoxalase II
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
for RNA interference experiments a cell line (427 1313 514) is employed that encodes a second tetracycline repressor and constitutively expresses a T7-polymerase
brenda
-
activity decreases after a two-week exposure to a sublethal concentration (1.6 mM) of Cu2+ compared to untreated control specimens in marine water
brenda
-
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
brenda
-
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
brenda
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
brenda
-
increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
brenda
-
increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
brenda
-
testis samples of prepubertal, pubertal, postpubertal cats. Expression of GLO-II significantly increases after puberty
brenda
-
differential expression of mitochondrial and cytosolic gly II
brenda
-
differential expression of mitochondrial and cytosolic gly II
brenda
-
differential expression of mitochondrial and cytosolic gly II
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mitochondrial isozyme is targeted directly to the mitochondrial matrix due to a mitochondrial targeting sequence
brenda
-
at least 4 enzyme forms, contain 10% of the total glyoxalase II activity in the homogenate
brenda
-
10-15% of the total glyoxalase II activity in liver. 56% of the activity resides in the matrix, 19% in the intermembrane space. 3 isoforms are exclusively mitochondrial
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
BLEG-1 may have evolved from glyoxalase II and adopted metallo-beta-lactamase activity through insertion of an active-site loop
malfunction
metabolism
physiological function
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
malfunction
-
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
metabolism
the enzyme performs S-glutathionylation of actin and malate dehydrogenase
metabolism
the enzyme limits lysine N-acetylation and N-succinylation of mitochondrial proteins
metabolism
GloB activates the prodrug bis(pivaloyloxymethyl) (1-hydroxy-2-oxopiperidin-3-yl)phosphonate. Mutation of GloB renders Staphylococcus aureus sensitive to bis(pivaloyloxymethyl) (1-hydroxy-2-oxopiperidin-3-yl)phosphonate
metabolism
the mechanism for the GlxII reaction starts with a nucleophilic attack of the bridging OH- group on the substrate. The coordination of the substrate to the Zn ions places its electrophilic center close to the hydroxide group, allowing the reaction to proceed. Structures with O2- as the bridging group and Asp-58 or Asp-134 protonated are 10.6 and 16.5 kcal/mol less stable than structures with OH-, respectively
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
-
enzyme overexpression leads to tolerance of transgenic yeast to salt stress
physiological function
the enzyme confers tolerance to abiotic stresses (salinity, drought, arsenic, heat, and UV-B stresses)
physiological function
GloB is active toward oxygen ethers. GloB has the highest activity against short-chain ethers, with some tolerance for branching at the first carbon beyond the ester carbonyl group. GloB exhibits a strong preference for oxygen at the beta-position to the carbonyl over the gamma-position but is indifferent to the positioning of sulfur
physiological function
enzyme is able to complement an Escherichia coli GlyII mutant strain
physiological function
transgenic plants overexpressing glyoxalase II show higher constitutive activity of glyoxalase II that increases further upon salt stress, and show higher tolerance to toxic concentrations of methylglyoxal and NaCl
physiological function
-
assembly of a specific metal-enriched form of GLX2 may be a mechanism to regulate the enzyme activity in vivo
-
Show AA Sequence and Transmembrane Helices (13641 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
21900
23000
24000
25000
26000
29000
31153
-
x * 31153, recombinant enzyme from mitochondria, GLO2, MALDI-TOF
31800
32000
31800
x * 31800, calculated, N-terminally truncated active form
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 31800, calculated, N-terminally truncated active form
?
-
x * 31153, recombinant enzyme from mitochondria, GLO2, MALDI-TOF
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Computational study, the bond distances of the bridging hydroxide to the two zinc ions are calculated to be 1.99 and 1.95 A, to be compared to the crystallographic distances of 2.03 and 1.99 A. The computed Zn-Zn distance of 3.29 A is also in very good agreement with the crystallographic distance of 3.34 A.
glyoxalase II and its complex with S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
-
crystals belong to space group C222(1), and diffract beyond 2.15 A, unit-cell parameters a = 65.6, b = 88.3, c = 85.2 A. Hanging-drop vapour-diffusion method using the crystallization tools
two glyoxalase II structures are solved. One with a bound spermidine molecule (1.8 A) and the other with D-lactate at the active site (1.9 A). The second structure is obtained by crystal soaking with the enzyme substrate (S)-D-lactoyltrypanothione. Hanging drop method
hanging-drop vapor diffusion method at 4°C and 18°C, the crystal structure of GloB solved at 1.4 A
structure to 1.44 A resolution. BLEG-1 has an insertion of an active-site loop, forming a binding cavity at the N-terminal region
structure of SeMet-substituted protein, to 1.65 A resolution. Four monomers of GloB are observed in the asymmetric unit. GloB exhibits the classic alphabeta/betalpha-fold that defines the metallo-beta-lactamases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C140A
site-directed mutagenesis, increased kcat, unaltered Km compared to the wild-type enzyme
D58C
site-directed mutagenesis, highly reduced kcat, unaltered Km compared to the wild-type enzyme
H172R
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
H54N
site-directed mutagenesis, highly reduced kcat, 2fold increased Km compared to the wild-type enzyme
H59C
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K142A
site-directed mutagenesis, 50% reduced kcat, 2fold increased Km compared to the wild-type enzyme
K65A
site-directed mutagenesis, reduced sensitivity to 9-fluoromethoxycarbonyl- or phenylmethoxycarbonyl-protected glutathione derivative inhibitors
L9A
site-directed mutagenesis, reduced sensitivity to 9-fluoromethoxycarbonyl- or phenylmethoxycarbonyl-protected glutathione derivative inhibitors
N178A
site-directed mutagenesis, reduced kcat, slightly increased Km compared to the wild-type enzyme
R225A
site-directed mutagenesis, increased activity compared to the wild-type enzyme
R248W
W57D
site-directed mutagenesis, reduced sensitivity to 9-fluoromethoxycarbonyl- or phenylmethoxycarbonyl-protected glutathione derivative inhibitors
W57N
site-directed mutagenesis, reduced sensitivity to 9-fluoromethoxycarbonyl- or phenylmethoxycarbonyl-protected glutathione derivative inhibitors
W199F
-
mid-point of unfolding transition curve is not very different from that of wild-type. Stability of the active site is slightly affected
W57F
-
mid-point of unfolding transition curve is not very different from that of wild-type enzyme. Stability of the active site is slightly affected
Y175F
-
site-directed mutagenesis, mutation has a marginal effect on kcat, but leads to a 8fold increased Km for S-(2-hydroxyacyl)glutathione compared to the wild-type, mutant shows a 30fold increased sensitivity to inhibition by S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione compared to the wild-type enzyme
K260D
-
unaltered metal binding sites and is correctly folded, but reduced activity. Has a much lower catalytic efficiency, but the spectrum is very similar to the wild-type enzyme. Has a highly simplified bell-shaped pH-activity profile with a maximum at pH 6.7 in contrast to the broad asymmetric profiles of the other enzymes
K260Q
-
unaltered metal binding sites and is correctly folded, but reduced activity
R154K
-
unaltered metal binding sites and is correctly folded, but reduced activity
R154M
-
unaltered metal binding sites and is correctly folded, but reduced activity
R257D
-
unaltered metal binding sites and is correctly folded, but reduced activity
R257Q
-
unaltered metal binding sites and is correctly folded, but reduced activity
additional information
R248W
mutant shows enhanced zinc content and reduced iron content compared to the wild-type enzyme
R248W
site-directed mutagenesis, about 8fold reduced kcat, about 10fold increased Km compared to the wild-type enzyme
additional information
introduction of beta-lactamase activity into the alphabeta/betaalpha metallohydrolase scaffold of glyoxalase II. The resulting enzyme, evMBL8 (evolved metallo beta-lactamase 8), completely loses its original activity and, instead, catalyzes the hydrolysis of, thus increasing resistance to Escherichia coli growth on cefotaxime by a factor of about 100
additional information
-
enhanced glyoxalase I and II enzyme levels, not only of one of the enzymes, by transgenic overexpression of a Oryza sativa enzyme lead to enhanced salinity stress tolerance, but no further modification of the phenotype
additional information
transgenic cotransfer of the gene in addition to the glyoxalase I gene to Nicotiana tabacum by Agrobacterium tumefaciens infection leads to overexpression of the enzymes and enhanced salt tolerance in the transgenic tobacco plants, no further modification of the tobacco phenotype
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partially proteolyzed by trypsin, under nondenaturing conditions, only at the level of the C-terminal region. Inactivation of the enzyme without loss of the secondary structure
-
protein stability increased in the presence of 10 mM MnCl2 and 5% PEG (PEG4000, PEG400, PEG8000)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, 1 mM S-octylglutathione, no significant loss of activity for at least 6 months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Co2+), gel filtration
ion exchange chromatography, ammonium sulfate precipitation, gel filtration, hydroxyapatite chromatography (not retained on the column)
-
iron-enriched GloB, manganese-enriched GloB and zinc-enriched GloB
-
partial, multiple forms
recombinant His-tagged and non-tagged enzyme expressed in Escherichia coli
wild-type and glutathione-binding site mutants, by sonication, centrifugation and on Ni-NTA column
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli BL21 Codon Plus cells. The protein is expressed with an N-terminal His-tag fusion
cloning of RNA interference constructs for targeting GLX II in bloodstream and procyclic Trypanosoma brucei, cloning of the constructs for the deletion of the GLX II alleles in procyclic cells and cloning of the pHD1701/GLXIImyc2 plasmid for the overexpression of GLX II
cytoplasmic gene GLO2 and mitochondrial gene GLO4, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, overexpression as N-terminally His-tagged and as free enzyme in Escherichia coli
DNA sequence determination and analysis of the single HAGH gene encoding both the cytosolic and mitochondrial isozymes, in vitro transcription, 2 splicing forms of mRNA
DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3)
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
-
glyoxalase II is cloned in pCAMBIA1304 and transformed into rice (Oryza sativa cv PB1) via Agrobacterium. The transgenic plants show higher constitutive activity of glyoxalase II that increases further upon salt stress, reflecting the upregulation of endogenous glyoxalase II. The transgenic rice shows higher tolerance to toxic concentrations of methylglyoxal and NaCl. Compared with non-transgenics, transgenic plants at the T1 generation exhibit sustained growth and more favorable ion balance under salt stress conditions
His-tagged version of mutant protein expressed in Escherichia coli BL21-Codon plus
into pQE30 vector. N-terminally MRGS(H)6GS-tagged GloII wild-type and mutant enzymes transformed into Escherichia coli competent XL1-Blue cells or EZ cells
-
overexpression of wild-type and mutants in Escherichia coli BL21(DE3)
pET32-gloB vector overexpressed in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity decreases upon the imposition of salt stress, especially at 300 mM NaCl
-
enzyme activity increases with increasing arsenic concentration, compared with the control seedlings. Supplementation with calcium to the arsenic-exposed seedlings further increases enzyme activity by 23 and 31%, respectively, compared with the seedlings treated with arsenic alone
-
expression is maximally upregulated in salinity followed by drought, arsenic, heat, and UV-B stresses
increased salinity (10 and 20% (w/v) PEG-6000 for 48 h) decreases the enzyme activity
-
increased salinity (25% (w/v) PEG-6000 for 24 or 48 h), 1.5 mM CdCl2 stress for 48 h or heat treatment at 40°C for 2 days decrease the enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
-
overexpression of glyoxalase II, plants are able to grow, flower, and set normal viable seeds in presence of 5 mM ZnCl2, without any penalty. Enzyme overexpression may also confer tolerance to cadmium or lead. Major sink for metal accumulation are roots. Double transgenics expressing both glyoxalase I and II perform better than single-gene transformants. Under high zinc conditions, transgenic plants show restricted methylglyoxal accumulation and less lipid peroxidation
drug development
-
cancer therapy, inhibitors of the glyoxalase system would be expected to suppress the growth of cancer cells and could find clinical use as anticancer drug
medicine
pharmacology
enzyme is a potential anti-cancer and/or anti-protozoal target, rational design of inhibitors
agriculture
the multistress response of OsglyII gene documents its future utility in developing tolerance to various stresses in crop plants
agriculture
transgenic plants overexpressing glyoxalase II show higher constitutive activity of glyoxalase II that increases further upon salt stress, and show higher tolerance to toxic concentrations of methylglyoxal and NaCl
agriculture
-
Si application modulates ascorbate and glutathione levels, ASA-GSH cycle enzyme activities, glyoxalase I and glyoxalase II activities, superoxide dismutase, and catalase activities, and results in a considerable reduction in ROS, malondialdehyde, and methylglyoxal levels during Pd stress. The expression of ascorbate peroxidase, catalase, glutathione reductase, dehydroascorbate reductase, and monodehydroascorbate reductase genes is induced in the presence of Si to alleviate Pd stress
medicine
cultivation of estrogen receptor positive MCF7 and estrogen receptor neagtive BT20 human breast cancer cells in presence of tamoxifen and 17beta-estradiol. Estradiol causes up to 60% decrease in enzyme mRNA in MCF7 cells, while there are no significant changes in presence of tamoxifen. In BT20 cells, tamoxifen causes a reduction of enzyme expression up to 85%.
medicine
GLX2 serves as a pro-survival factor of the p53 family and plays a critical role in the normal development and in the pathogenesis of various human diseases, including cancer, diabetes, and neurodegenerative diseases
EXTERNAL LINKS (specific for EC-Number 3.1.2.6)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
