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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

Reaction

(R)-S-lactoylglutathione
=
glutathione
+
2-oxopropanal

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

     4 Lyases
         4.4 Carbon-sulfur lyases
             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
                4.4.1.5 lactoylglutathione lyase

Inhibitors

Inhibitors on EC 4.4.1.5 - lactoylglutathione lyase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
-
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
-
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
-
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
-
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
-
-
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
-
inhibitor based on binding mode of myricetin, contributuion of the Zn2+-chelating group to inhibitory activity
(S)-4-bromobenzyl glutathione
-
potent Glx-I inhibitor
(S)-4-bromobenzylglutathione cyclopentyl diester
-
competitive inhibitor of GLOI
(Z)-1-[N-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate
-
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'-phenyl-3,4'-bipyridin-2'(1'H)-one
-
-
1,10-phenanthroline
1-chloro-2,4-dinitrobenzene
-
not reduced by dithiothreitol
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
10 mM, 65% inhibition
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
1-hydroxy-4,6-diphenylpyridin-2(1H)-one
-
-
1-hydroxy-4-phenyl-6-(1H-pyrrolo[2,3-b]pyridin-5-yl)pyridin-2(1H)-one
-
-
1-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-(1H-indol-5-yl)-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-phenyl-4-(thiophen-3-yl)pyridin-2(1H)-one
-
-
1-hydroxy-6-phenyl-4-[4-(trifluoromethyl)phenyl]pyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(2-methoxyethyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(2-methoxyethyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(3-methoxypropyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
-
-
1-Naphthaleneacetic acid
2,2'-dipyridyl
-
-
2,3-Butanedione
-
time and concentration dependent inactivation
2,3-Dihydroxybenzoic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-trinnitrobenzenesulphonic acid
-
2 mM, 60% inhibition
2,6-pyridindicarboxylic acid
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
-
inhibitor based on binding mode of myricetin
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
-
inhibitor based on binding mode of myricetin
2-aminopyridine
-
-
2-Hydroxy-5-nitrobenzyl bromide
-
-
3-hydroxyflavone
-
-
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-indol-1-yl]methyl]benzamide
-
-
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-pyrrolo[2,3-b]pyridin-1-yl]methyl]benzamide
-
-
4,6-diphenyl-N-hydroxypyridone
-
a lead compound for non-peptidic inhibitor screening against glyoxalase I
4-(biphenyl-4-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
4-(but-1-yn-1-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
4-bromoacetoxy-1-(S-glutathionyl)-acetoxy butane
-
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-butyl-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
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
-
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
-
-
adenine
-
-
adenosine
-
-
amino-group reagents
-
-
-
aniline
-
-
baicalein
Baicalin
30% inhibition of rhGLO I at 0.1 mM
benzimidazole
-
-
benzyladenine
bisdemethoxycurcumin
buthionine sulfoximine
-
58% loss in Gly-I activity by 0.05 mM buthionine sulfoximine
Caffeine
-
-
Cbz-GSH
-
-
Chelex-100
-
-
-
Chlorophyllin
-
-
chrysin
ClO2
-
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
Co2+
apo form reactivated
Colchicine
coproporphyrin
-
weak
coumarin-10
coumarin-4
coumarin-5
coumarin-8
coumarin-9
cromoglycate
-
0.1 mM, 50% inhibition
curcumin
cytidine
-
-
D-glucono-delta-lactone
-
weak
D-isoascorbate
-
-
Dansyl chloride
-
-
dichlorophen
-
0.048 mM, 50% inhibition
diethyl dicarbonate
-
-
diethyldicarbonate
-
2 mM, complete inhibition
dihydroxyfumaric acid
-
-
dipicolinic acid
greatest loss of GloA3 activity
dithiothreitol
-
slight
EGTA
-
-
fenoprofen
-
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
FeSO4
-
2.0 mM, 46.5% inhibition
fisetin
flavone
IC50 wild type 56 microM, IC50 enzyme overexpressor 69 microM
formaldehyde
-
-
formononetin 7-O-glucoside
-
0.074 mM, 50% inhibition
gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C
glutathione thioethers
-
competitive
glycerol
-
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
guanine
-
-
guanosine
-
-
H2O2
-
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
-
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
hyperin
below 5% inhibition of rhGLO I at 0.1 mM
I-
-
5 mM, complete inhibition
indomethacin
iodoacetamide
-
slight
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
kaempferol
Ketoprofen
-
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
-
tight-binding carboanalog of hydroxamate
L-gamma-glutamyl-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
hydroxamic acid-based transition state inhibitor, unstable toward gamma-glutamyltranspeptidase
Lapachol
Lawsone
luteolin
meso-tetrasubstituted porphyrines
-
-
-
methyl gerfelin
methylglutathione
-
methylglyoxal
morin
myricetin
N-Acetylimidazole
-
reversed by hydroxylamine
N-bromosuccinimide
-
-
N-bromsuccinimide
-
0.0032 mM, 35% inhibition
N-[(1S,4Z)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohept-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[(1S,4Z)-6-(4-bromophenyl)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohex-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
tight-binding competitive inhibitor, stable toward gamma-glutamyltranspeptidase
N2-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
tight-binding carboanalog of hydroxamate
naringenin
50% inhibition of rhGLO I at 0.1 mM
NH2-gamma-Gla[-Glu(CON(OH)-4-bromophenyl)Gly-OH]-OH
-
-
NH2-gamma-Glu[-D-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Dab(N-(4-bromobenzoyl)-N'-hydroxyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
NO3-
-
10 mM, 20% decrease of activity
norlapachol
octyl-S-glutathione
-
-
oroxylin A
140% inhibition of rhGLO I at 0.1 mM
oxibendazol
-
0.11 mM, 50% inhibition
p-hydroxymercuribenzene sulfonate
-
1 mM, 64% inhibition
para-substituted S-benzylglutathione
-
-
Phenylglyoxal
-
-
phosphate
-
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
phthicol
protoporphyrin
-
-
purpurogallin
pyridoxal
-
-
pyridoxal 5'-phosphate
-
-
pyridoxamine
-
-
quercetin
rhodizonic acid
-
-
rutin
-
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-(1-naphthylmethyl)-glutathione
-
-
S-(2-chlorobenzyl)-glutathione
-
-
S-(2-hydroxybenzyl)-glutathione
-
-
S-(4-bromophenyl)glutathione
-
glyoxalase I
S-(4-nitrobenzyloxycarbonyl)glutathione
-
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
S-(N-hydroxy-N-methylcarbamoyl)glutathione
-
S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione
-
S-(N-hydroxy-N-p-iodophenylcarbamoyl) glutathione
tight binding competitive inhibitor of human GLOI
S-(N-hydroxy-N-p-iodophenylcarbamoyl)glutathione
-
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
-
S-(omega-aminodecyl)glutathione
-
-
S-(p-bromobenzyl)glutathione
S-2,4-dinitrophenylglutathione
S-2,4-dinitrophenylglutathionylspermidine
S-4-bromobenzylglutathione
S-4-bromobenzylglutathione cyclopentyl diester
-
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-4-bromobenzylglutathionylspermidine
S-benzyl-glutathione
-
-
S-benzylglutathione
-
-
S-bromobenzylglutathione
S-hexylglutathione
S-nitroso-N-acetyl-D,L-penicillamine
-
released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosocysteine
-
released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosoglutathione
S-p-bromobenzyl glutathione
-
competitive inhibitor, unstable toward gamma-glutamyltranspeptidase
S-p-bromobenzylglutathione
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
S-p-nitrobenzylglutathione
S-p-nitrobenzyloxycarbonylglutathione
-
S-p-nitrosobenzylglutathione
-
squaric acid
-
-
Tetranitromethane
Theobromine
-
-
theophylline
-
-
thymine
-
-
Tolmetin
-
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
tryptophan
-
-
Uracil
-
-
uridine
-
-
vinblastine
xanthine
-
-
zinc (2S)-2-amino-3-([(3R)-3-([[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]methyl)-4-[(carboxylatomethyl)amino]-4-oxobutanoyl]amino)propanoate
-
-
zinc (2S)-2-amino-3-[([(2R)-3-[[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]-1-[(carboxylatomethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoate
-
-
Zomepirac
-
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
additional information
-