4.4.1.5: lactoylglutathione lyase
This is an abbreviated version!
For detailed information about lactoylglutathione lyase, go to the full flat file.
Word Map on EC 4.4.1.5
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4.4.1.5
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glycation
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detoxify
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gsh
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dicarbonyls
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erythrocyte
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d-lactate
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adduct
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dismutase
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endproducts
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rage
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s-transferase
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mellitus
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methylglyoxal-induced
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glyoxalases
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byproduct
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hyperglycemia
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glutathione-dependent
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phosphoglucomutase
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metalloenzyme
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hemithioacetal
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mg-induced
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hla-a
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aldose
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3-deoxyglucosone
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enediolate
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d-lactic
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pentosidine
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cyclopentyl
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mdhar
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haptoglobin
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aminoguanidine
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diesters
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monodehydroascorbate
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6-phosphogluconate
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anti-glycation
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dehydroascorbate
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anxiety-like
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gsh-dependent
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pyridoxamine
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analysis
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trypanothione
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medicine
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drug development
- 4.4.1.5
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glycation
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detoxify
- gsh
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dicarbonyls
- erythrocyte
- d-lactate
- adduct
- dismutase
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endproducts
- rage
- s-transferase
- mellitus
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methylglyoxal-induced
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glyoxalases
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byproduct
- hyperglycemia
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glutathione-dependent
- phosphoglucomutase
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metalloenzyme
- hemithioacetal
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mg-induced
- hla-a
- aldose
- 3-deoxyglucosone
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enediolate
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d-lactic
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pentosidine
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cyclopentyl
- mdhar
- haptoglobin
- aminoguanidine
- diesters
- monodehydroascorbate
- 6-phosphogluconate
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anti-glycation
- dehydroascorbate
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anxiety-like
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gsh-dependent
- pyridoxamine
- analysis
- trypanothione
- medicine
- drug development
Reaction
Synonyms
aldoketomutase, CLO GlxI, Glb33, GLI, GLO I, GLO-1, GLO-I, Glo1, GloA, GloA1, GloA2, GloA3, GloI, Glx I, Glx-I, Glx1, GLXI, Gly I, gly-I, GLY1, glyoxalase 1, glyoxalase I, glyoxalase-1, glyoxalase-I, glyoxylase I, GmGlyox I, ketone-aldehyde mutase, lactoylglutathione lyase, lactoylglutathione methylglyoxal lyase, LGL, lyase, lactoylglutathione, methylglyoxalase, methylglyoxylase, OsGLYI-11.2, PfGlx I, rhGLO I, S-D-lactoylglutathione methylglyoxal lyase, S-D-lactoylglutathione methylglyoxal lyase (isomerizing), S-D-lactoylglutathione:methylglyoxal lyase, SpGlo1, STM3117, YaiA
ECTree
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Inhibitors
Inhibitors on EC 4.4.1.5 - lactoylglutathione lyase
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(1E,4Z,6E)-4-(4-hydroxy-3-methoxybenzylidene)-1-(3-hydroxy-4-methoxyphenyl)-7-(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
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three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
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three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
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three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
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three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(2S)-2-amino-3-[([(2R)-3-[(4-bromobenzyl)sulfanyl]-1-[(carboxymethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoic acid
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(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
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inhibitor based on binding mode of myricetin, contributuion of the Zn2+-chelating group to inhibitory activity
(S)-4-bromobenzylglutathione cyclopentyl diester
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competitive inhibitor of GLOI
(Z)-1-[N-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate
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decreases glyoxalase I expression and activity relative to untreated control cells, cells undergo apoptosis, apoptosis increases further on co-incubation with high glucose
1-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
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1-hydroxy-6-[1-(2-methoxyethyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
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1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
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2,6-pyridindicarboxylic acid
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2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
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inhibitor based on binding mode of myricetin
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
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inhibitor based on binding mode of myricetin
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-indol-1-yl]methyl]benzamide
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3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-pyrrolo[2,3-b]pyridin-1-yl]methyl]benzamide
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4,6-diphenyl-N-hydroxypyridone
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a lead compound for non-peptidic inhibitor screening against glyoxalase I
4-bromoacetoxy-1-(S-glutathionyl)-acetoxy butane
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competitive inhibition of GLO1, the inhibitor is able to covalently bind to the free sulfhydryl group of Cys60 in the hydrophobic binding pocket adjacent to the enzyme active site and partially inactivate the enzyme, no complete inhibition, binding structure analysis, overview
4-[(4E)-5-(3,4-dimethoxyphenyl)-2-[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]-3-oxopenta-1,4-dien-1-yl]benzene-1,2-dicarbaldehyde
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three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
6-(1-butyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-1-hydroxy-4-phenylpyridin-2(1H)-one
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buthionine sulfoximine
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58% loss in Gly-I activity by 0.05 mM buthionine sulfoximine
ClO2
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study of the influence of chlorine dicloride during the disinfection process in 2 drinking water production plants at the river Po in North Italy. Measuring of the glyoxalase activity at two experimental times, 3 and 6 days. Plant 1-treated carp shows an increased glyoxalase I activity of about 140%, indicating an induced defense ability. Whereas the plant 2-treated specimens show the depletion of enzyme activity of 50%, indicating a compromised capacity to detoxify the peroxidative products formed during the oxidative process due to the inhibited glyoxalase activity
fenoprofen
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
flavone
IC50 wild type 56 microM, IC50 enzyme overexpressor 69 microM
gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C
glycerol
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64% loss in Gly-I activity by 2.5% (v/v) glycerol, Gly-I inactivation by glycerol is fully prevented or reversed by 0.5 mM N-acetylcysteine
H2O2
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2 mM, 2 h, significantly reduces enzyme activity from 0.2 U/single Caenorhabditis elegans (without addition of H2O2) to 0.065 U/single Caenorhabditis elegans
HgCl2
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67% loss in Gly-I activity by 0.03 mM HgCl2, Gly-I inactivation by HgCl2 is fully prevented or reversed by 0.5 mM N-acetylcysteine
isolupalbigenin
treatment of HL-60 cells leads to significant accumulation of substrate methylglyoxal and the caspase 3 activity of the cell lysate increases. Compound shows anti-proliferative activity against HL-60 cells
Ketoprofen
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
L-gamma-glutamyl-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
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tight-binding carboanalog of hydroxamate
L-gamma-glutamyl-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
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hydroxamic acid-based transition state inhibitor, unstable toward gamma-glutamyltranspeptidase
N-[(1S,4Z)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohept-4-en-1-yl]-L-glutamine
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beta-ketoester, competetive inhibitor
N-[(1S,4Z)-6-(4-bromophenyl)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohex-4-en-1-yl]-L-glutamine
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beta-ketoester, competetive inhibitor
N-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
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tight-binding competitive inhibitor, stable toward gamma-glutamyltranspeptidase
N2-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
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tight-binding carboanalog of hydroxamate
phosphate
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750 mM, strain BY4741, about 2fold decrease of glyoxalase I. In the YEpGLO1 strain, glyoxalase is higher than in BY4741, consistant with the overexpression of the glo1 gene. Enzyme inactivation is observed, cells subjected to 750 mM phosphate still show an increase of about 1.7fold relatively to BY4741 glyoxalase I activity
rutin
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competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
S-(N-hydroxy-N-p-iodophenylcarbamoyl) glutathione
tight binding competitive inhibitor of human GLOI
S-4-bromobenzylglutathione cyclopentyl diester
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detanonoate, NO donor, competitive inhibitor, concentration-dependent down-regulation of glyoxalase I, increases intracellular methylglyoxal and causes apoptosis, overexpression of glyoxalase I protects against S-4-bromobenzylglutathione cyclopentyl diester-induced apoptosis under high glucose conditions
S-nitroso-N-acetyl-D,L-penicillamine
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released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosocysteine
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released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-p-bromobenzyl glutathione
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competitive inhibitor, unstable toward gamma-glutamyltranspeptidase
S-p-bromobenzylglutathione cyclopentyl diester
GLO1 inhibitor, inhibiting osteoclastogenesis, inhibition kinetics from 0.03 to 3 microM, dose-dependently inhibited, strongest inhibition at 3 microM, pH 7.0, 30°C
Tolmetin
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Tolmetin coordinates with the zinc ion
zinc (2S)-2-amino-3-([(3R)-3-([[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]methyl)-4-[(carboxylatomethyl)amino]-4-oxobutanoyl]amino)propanoate
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zinc (2S)-2-amino-3-[([(2R)-3-[[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]-1-[(carboxylatomethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoate
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Zomepirac
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
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2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
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activity decreases by approximately 50% during differentiation in Brassica sp. gly I
1-Naphthaleneacetic acid
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activity decreases by approximately 50% during differentiation in Brassica sp. gly I
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activity decreases by approximately 50% during differentiation in Brassica sp. gly I
benzyladenine
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activity decreases by approximately 50% during differentiation in Brassica sp. gly I
bisdemethoxycurcumin
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Bisdemethoxycurcumin coordinates with the zinc ion
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competitve inhibition, structually related to glutathione, Dixon plot analysis, pH 7.0, 30°C, more efficient inhibition of GLO1 compared to quercetin, myricetin, kaempferol, luteolin, or rutin as inhibitor, results in a decrease of D-lactate release
curcumin
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Curcumin coordinates with the zinc ion
EDTA
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0.1 mM, approx. 50% inactivation after 50 min, approx. 80% inhibition after 250 min
indomethacin
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combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Indomethacin coordinates with the zinc ion and is able to occupy all four enzyme subsites, both subsites C and D may be occupied simultaneously
kaempferol
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competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
Lapachol
IC50 wild type 93 microM, IC50 enzyme overexpressor 96 microM
luteolin
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competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C
methylglyoxal
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200 mM, 8 h, significantly reduces enzyme activity from 0.2 U/single Caenorhabditis elegans (without addition of methylglyoxal) to 0.12 U/single Caenorhabditis elegans
methylglyoxal
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addition at pH 7.0 results in a modest 28% decrease in the glycolytic rate
MS-3
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inhibitor produced by a mushroom Stereum hirsutum; mechanism of inhibition
myricetin
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competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
myricetin
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substrate transition-state (Zn2+-bound methylglyoxal-glutathione hemithioacetal) mimetic inhibitor
IC50 wild type 70 microM, IC50 enzyme overexpressor 132 microM
quercetin
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competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
quercetin
IC50 wild type 26 microM, IC50 enzyme overexpressor 27 microM
S-4-bromobenzylglutathionylspermidine
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potent linear competitive inhibitor, selectively inhibits trypanosomatid GLO1 activity
S-hexylglutathione
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slows degradation of the wild-type enzyme and mutant E161Q/E345Q in comparison with uncomplexed protein
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glyoxal I activity in cells decreases rapidly within 30 min and reaches 10% of the control level within 2 h, activity returns to approx. 80% and 70% after removal of S-nitrosoglutathione or incubation with dithiothreitol, respectively, released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
Zn2+
inactivation of gly I, metal can bind to the enzyme gly I, but the resulting enzyme is inactive
Zn2+
inactivation of gloA1; inactivation of gly I
additional information
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substrate-analogue inhibitors and transition-state inhibitors
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additional information
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reducing glyoxalase I RNA levels with advancing stage of Alzheimers disease and with increasing age, continuously decrease in middle and late stages of Alzheimers disease, glyoxalase I activity neither significantly changes with age nor with the course of the disease
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additional information
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exposure of HPMC cells to heat-sterilized peritoneal dialysis fluids results in reduced GLO-I activity, GSH depletion, and a decrease in cell viability. Pretreatment of heat-sterilized peritoneal dialysis with either a combination of GLO-I and GSH markedly reduces inhibitory effects toward HPMC cells. Exposure of HPMC cells to L-2-oxothiazolidine-carboxylic acid increases cellular GSH and prevents loss of GLO-I activity in response to heat-sterilized peritoneal dialysis
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additional information
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posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity
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additional information
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design of 4-(7-azaindole)-substituted 6-phenyl-N-hydroxypyridones, thermodynamic binding parameters, binding modeling using the enzyme's crystal structure, overview. Inhibitory activity of 6-phenyl-N-hydroxypyridones with various substituents at 4-position
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additional information
not inhibitory: S-methyl-glutathione, S-propyl-glutathione, S-butyl-glutathione, S-hexyl-glutathione, S-octyl-glutathione at 1 mM, S-p-nitrobenzyl-glutathione and S-p-bromobenzyl-glutathione at 250 microM
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additional information
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not inhibitory: S-methyl-glutathione, S-propyl-glutathione, S-butyl-glutathione, S-hexyl-glutathione, S-octyl-glutathione at 1 mM, S-p-nitrobenzyl-glutathione and S-p-bromobenzyl-glutathione at 250 microM
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additional information
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tight-binding inhibitors are very potent against the recombinant enzyme
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additional information
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1.21 mg/kg crayfish, selenium-enriched diet, male crayfish, shows a lowered enzyme activity, 85% inhibited at day 30, 45% inhibited at day 50. A depletion of enzyme activity indicates a compromised detixificant ability against peroxidative metabolites. Since selenium affects only treated males, it seems that males are more susceptible than females
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additional information
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monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
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additional information
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no change in glyoxalase I activity in taurine-treated rats
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additional information
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substrate-analogue inhibitors and transition-state inhibitors
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additional information
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methylglyoxal toxicity is evaluated by viability assays using BY4741 and the null mutant DELTAglo1, lacking the glyoxalase I activity. The reference BY4741 strain shows no methylglyxoal toxicity up to 10 mM. In contrast, strains with deficiencies in the glyoxalase system, i.e. DELTAglo1 have decreased viability, progessively more severe with increasing methylglyoxal concentration
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additional information
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S-4-bromobenzylglutathione is inactive as inhibitor
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