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Information on EC 4.4.1.5 - lactoylglutathione lyase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
Also acts on 3-phosphoglycerol-glutathione.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glyoxalase i, glyoxalase 1, glo-1, glo-i, glo i, glyoxalase-i, glyoxalase-1, gly-i, lactoylglutathione lyase, glyoxylase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldoketomutase
-
-
-
-
GloA
-
-
Glx I
-
-
Glx-I
-
-
glyoxalase 1
-
-
glyoxalase I
glyoxalase-1
-
-
glyoxalase-I
-
-
glyoxylase I
-
-
-
-
ketone-aldehyde mutase
-
-
-
-
lyase, lactoylglutathione
-
-
-
-
methylglyoxalase
-
-
-
-
methylglyoxylase
-
-
-
-
rhGLO I
His-tagged GLO I protein
S-D-lactoylglutathione methylglyoxal lyase
-
-
-
-
S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-S-lactoylglutathione = glutathione + 2-oxopropanal
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing; glutathione-forming)
Also acts on 3-phosphoglycerol-glutathione.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-12-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
show the reaction diagram
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione ethyl ester + methylglyoxal
?
show the reaction diagram
-
-
-
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
show the reaction diagram
-
-
-
?
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
show the reaction diagram
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
determined monitoring the increase in absorbance at 240 nm for 5 min at 25°C, pH 7.0
-
?
methylglyoxal + glutathione
S-D-lactoylglutathione
show the reaction diagram
-
-
-
?
N1-glutathionylspermidine + methylglyoxal
?
show the reaction diagram
specificity constant of N1-glutathionylspermidine 50fold less than of glutathione
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + methylglyoxal
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
67% of activity with Zn2+
Ni2+
reactivation of apo gly I
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-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
-
-
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
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
-
-
baicalein
79% inhibition of rhGLO I at 0.1 mM
Baicalin
30% inhibition of rhGLO I at 0.1 mM
bisdemethoxycurcumin
buthionine sulfoximine
-
58% loss in Gly-I activity by 0.05 mM buthionine sulfoximine
Cbz-GSH
-
-
chrysin
-
-
Co2+
apo form reactivated
coumarin-10
-
-
coumarin-4
-
-
coumarin-5
-
-
coumarin-8
-
-
coumarin-9
-
-
curcumin
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
fisetin
-
-
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
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
indomethacin
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
Lapachol
-
-
Lawsone
-
-
luteolin
Mg2+
apo form reactivated
morin
-
-
myricetin
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
-
-
Ni2+
apo form reactivated
norlapachol
-
-
oroxylin A
140% inhibition of rhGLO I at 0.1 mM
phthicol
-
-
quercetin
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-(4-nitrobenzyloxycarbonyl)glutathione
-
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
IC50 0.06 microM
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.09 microM
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
-
IC50 2.5 microM
S-(N-p-iodophenyl-N-hydroxycarbamoyl)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
linear competitive inhibitor
S-benzylglutathione
-
-
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
-
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
S-p-bromobenzylglutathione
S-p-nitrobenzyloxycarbonylglutathione
-
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
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
-
-
Zn2+
apo form reactivated
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
glyoxalase I protein amounts are 1.5fold increased in early Alzheimer’s disease subjects
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
(R)-S-lactoylglutathione
-
30°C, pH 7.0
0.049
glutathione
-
0.042
glutathione ethyl ester
-
0.053
glutathione isopropyl ester
-
0.192
glutathione-methylglyoxal hemithioacetal
-
-
0.13 - 0.182
methylglyoxal
0.148
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
0.04
Phenylglyoxal
-
-
0.13
trypanothione
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1360
glutathione
-
164
glutathione ethyl ester
-
222
glutathione isopropyl ester
-
1820
glutathione-methylglyoxal hemithioacetal
-
-
1088 - 1130
methylglyoxal
83
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
1070
Phenylglyoxal
-
-
104
trypanothione
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
methylglyoxal
-
recombinant enzyme, pH 7.3, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036
(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
-
pH 7.1, 30°C
0.0046
(1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30°C
0.0026
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30°C
0.0032
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30°C
0.0128
(2S)-2-amino-3-[([(2R)-3-[(4-bromobenzyl)sulfanyl]-1-[(carboxymethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoic acid
-
0.05 M phosphate buffer pH 6.6, 30°C
0.00628
(S)-4-bromobenzyl glutathione
-
-
0.0036
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
-
pH 7.1, 30°C
0.0103
bisdemethoxycurcumin
-
0.0051 - 0.0182
curcumin
0.383
fenoprofen
-
pH 7.1, 30°C
0.0244
indomethacin
0.021
kaempferol
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°C
0.843
Ketoprofen
-
pH 7.1, 30°C
0.035
luteolin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°C
0.013
myricetin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°C
0.0000326
NH2-gamma-Gla[-Glu(CON(OH)-4-bromophenyl)Gly-OH]-OH
-
-
0.00000166
NH2-gamma-Glu[-D-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
0.000000123
NH2-gamma-Glu[-Dab(N-(4-bromobenzoyl)-N'-hydroxyl)-Gly-OH]-OH
-
-
0.00000617
NH2-gamma-Glu[-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
0.023
quercetin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°C
0.14
rutin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°C
0.00003
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
-
0.00005
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
-
0.000014
S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione
-
0.00001
S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
-
0.645
S-2,4-dinitrophenylglutathione
-
0.915
S-2,4-dinitrophenylglutathionylspermidine
-
0.000128
S-4-bromobenzylglutathione
-
0.0126
S-4-bromobenzylglutathionylspermidine
-
0.00028
S-benzylglutathione
-
-
0.00008
S-p-bromobenzylglutathione
-
0.00115
zinc (2S)-2-amino-3-([(3R)-3-([[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]methyl)-4-[(carboxylatomethyl)amino]-4-oxobutanoyl]amino)propanoate
-
0.05 M phosphate buffer pH 6.6, 30°C
0.00219
zinc (2S)-2-amino-3-[([(2R)-3-[[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]-1-[(carboxylatomethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoate
-
0.05 M phosphate buffer pH 6.6, 30°C
0.335
Zomepirac
-
pH 7.1, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
Homo sapiens
-
pH 7.0, 25°C
0.00828
1'-hydroxy-6'-phenyl-3,4'-bipyridin-2'(1'H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00119
1-hydroxy-4,6-diphenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
1-hydroxy-4-phenyl-6-(1H-pyrrolo[2,3-b]pyridin-5-yl)pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00051
1-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
1-hydroxy-6-(1H-indol-5-yl)-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00152
1-hydroxy-6-phenyl-4-(thiophen-3-yl)pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00813
1-hydroxy-6-phenyl-4-[4-(trifluoromethyl)phenyl]pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
1-hydroxy-6-[1-(2-methoxyethyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000014
1-hydroxy-6-[1-(2-methoxyethyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
1-hydroxy-6-[1-(3-methoxypropyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000011
1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0546
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
Homo sapiens
-
pH 7.0, 25°C
0.0932
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
Homo sapiens
-
pH 7.0, 25°C
0.00048
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-indol-1-yl]methyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-pyrrolo[2,3-b]pyridin-1-yl]methyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0084
4-(biphenyl-4-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01
4-(but-1-yn-1-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01
4-butyl-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
6-(1-butyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-1-hydroxy-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.011
baicalein
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.0206
kaempferol
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.007
luteolin
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.00056
myricetin
0.0032
quercetin
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.00006
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
Homo sapiens
-
IC50 0.06 microM
0.00009
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
Homo sapiens
-
IC50 0.09 microM
0.0025
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
Homo sapiens
-
IC50 2.5 microM
0.021
S-(p-bromobenzyl)glutathione
Homo sapiens
-
pH and temperature not specified in the publication
0.0332
S-4-bromobenzylglutathione
Homo sapiens
-
pH 7.0, 25°C
0.023
S-p-bromobenzylglutathione
Homo sapiens
calculated, effectively inhibits rhGLO I at 25°C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.4
-
breast cancer cell MDA-MD-231 cell, pH 7.0, 30°C
0.9
-
brain astrocytoma 1321N1 cell, pH 7.0, 30°C
1.17
-
breast cancer cell JIMT-1 cell, pH 7.0, 30°C
1.4
-
prostate cancer cell PC-3 cell, pH 7.0, 30°C
1019
-
-
110
-
30°C, pH 7.0
1150
-
-
1580
-
purified recombinant enzyme, pH 7.3, 25°C
1830
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
-
7
-
assay at
7.3 - 7.4
-
assay at
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is absent from the necrotic core of atherosclerotic plaques
Manually annotated by BRENDA team
-
MDA-MD-231 cell, JIMT-1 cell
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
human dermal microvascular endothelial cell
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
transcription level and glyoxalase I activity are higher in pathological tissues than in normal ones
Manually annotated by BRENDA team
-
GLOI is mainly localized in the anterior epithelium but the enzyme is diffusely present in outer cortical and nuclear regions of the human lens
Manually annotated by BRENDA team
-
Bcr-Abl+ leukemic stem cell
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
prostate cancer cell
Manually annotated by BRENDA team
-
carotid sample derived from thromboendarterectomy
Manually annotated by BRENDA team
-
medial, high expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
increased methylglyoxal levels, resulting from decreased enzyme activity, induce apoptosis in fully differentiated podocytes, as well as in endothelial cells and macrophages in hypoxic regions of atherosclerotic arteries
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LGUL_HUMAN
184
0
20778
Swiss-Prot
other Location (Reliability: 2)
X5DNM4_HUMAN
184
0
20778
TrEMBL
other Location (Reliability: 2)
V9HW62_HUMAN
184
0
20720
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20647
-
2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
20774
-
x * 20774, calculation from nucleotide sequence
21000
-
2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
23000
26000
-
2 * 26000
42000
-
reombinant enzyme, native PAGE
46000
-
-
51000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 20774, calculation from nucleotide sequence
dimer
homodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathionylation
glutathionylation strongly inhibits Glo1 activity in vitro
phosphoprotein
side-chain modification
-
posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity
additional information
-
NO-mediated modification can suppress NF-kappaB-dependent reporter gene expression, less powerful in suppression than phosphorylation of GLO1
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal sructure of glyoxalase I in complex with S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione and S-p-nitrobenzyloxycarbonylglutathione at 2.0 and 1.72 A, respectively
crystal structure of glyoxalase I complexed with S-benzylglutathione and S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
molecular docking of all inhibitors tested into crystal structure, PDB entry 1QIN. In the binding model of the three-ring curcumin derivatives, two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site. 6 ns molecular dynamics simulations of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione show two important hydrogen bonds: one is between hydroxyl oxygen atom of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione and the nitrogen atom in residue Arg37, and one between the hydroxyl oxygen of the compound inside the hydrophobic pocket and the carbonyl oxygen of residue Met179. The original hydrogen bond disappears but a new and stable one is formed. The average distance from Zn2+ to outer carbonyl oxygen of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione is about 2.095 A during 6 ns simulation. Pi-pi stacking interaction is observed between a phenyl ring of the ligand and residue Phe67
-
recombinant enzyme in complex with S-benzyl-glutathione
-
X-ray structure of the homodimeric humanGlo1 in the presence of the bound inhibitor S-benzylglutathione
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A111E
-
the mutation is associated with an increased risk of this neoplasia in breast cancer
E111A
-
the mutation is associated with estrogen-negative breast cancer
E172Q
-
100000fold lower activity than wild-type
E99Q
-
10000fold lower activity than wild-type
E99Q/Q33E
-
100fold lower activity than wild-type
S44A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S68A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S93A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T101A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T106A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, phosphorylation of GLO1 is completely abolished
T97A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from erythrocytes, purity above 90%
-
Ni-NTA resin column chromatography
-
purification of endogenous and His-tagged enzyme, wild-type and mutants (T106A, S44A, S68A, S93A, T97A, T101A). The amount of purified enzyme is higher, when GLO1 (wild-type and mutants) is co-expressed with calcium,calmodulin-dependent protein kinase II, suggesting that the kinase induces the stabilization of GLO1
-
recombinant enzyme from Escherichia coli strain JM103 by S-hexylglutathione affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Rattus norvegicus
-
expression in Escherichia coli
-
GST-GLOI fusion protein is expressed in Escherichia coli BL21 (DE3)pLysS cells
-
into vector pCMS-EGFP, overexpression in HRP cells
-
overexpression of Glo1 in endothelial cells to investigate the effect on hyperglycemia-induced impairment of angiogenesis in vitro. The overexpression results in an increased protection against dicarbonyl glycation of endothelial cell protein protecting against hyperglycemia-induced angiogenesis deficit. The formation of tube structures through hyperglycemia decreases by 32%
-
recombinant expression in Escherichia coli strain JM103
-
the gene for glyxalase I is located on chromosome 6, locus 6p21,3-6p21,2. Study of A419C (E111A) single nucleotide polymorphism of the glyoxalase I gene
-
wild-type and mutants (T106A, S44A, S68A, S93A, T97A, T101A) expressed and co-expressed in HEK-293 cells, co-expression of His-tagged GLO1 with the catalytic subunit of calcium, calmodulin-dependent protein kinase II and protein kinase A. GLO1 is only phosphorylated when it is co-expressed with the catalytic subunit of calcium, calmodulin-dependent protein kinase II but no phosphorylation is observed when GLO1 is co-expressed with protein kinase A. Overexpression of wild-type GLO1 suppresses tumor-necrosis factor-induced NF-kappaB-dependent reporter gene expression. Supression of the basal and tumor-necrosis factor-induced NF-kappaB activity is significantly stronger upon expression of a GLO1 mutant that is either deficient for the NO-mediated modification or phosphorylation on Thr106
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of receptor for advanced glycation endproducts by S100A12 protein decreases the expression of glyoxalase 1
-
compared with the respective parental cells, hypoxia adapted-Bcr-Abl+ cells have higher levels of protein and higher enzyme activity of glyoxalase-I. High Glo-I expression is sustained in hypoxia adapted-chronic myeloid leukemia cells after 6 months in normoxia
-
Gly-I activity in N-acetylcysteine-exposed cells is 40% higher than that in control cells
-
glyoxylase I expression is upregulated up to 10fold at the mRNA and protein level in metastatic melanoma tissue
-
in the human lens, GLOI activity and immunoreactivity both decrease with age
-
the promoter of Glo1 harbours an nuclear factor kappaB-responsive element, indicating a link between inflammation and reduced Glo1 expression
-
troglitazone downregulates GLO-1 expression
-
troglitazone treatment (0.025-0.1 mM) reduces glyoxalase I protein expression in glioma
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
flow cytometry method for GLO-1 detection in human leukocytes isolated from peripheral blood samples to investigate GLO-1 expression in leukocyte subsets from type 1 and 2 diabetes mellitus patients. Expression index of GLO-1-positive cells is slightly increased in mononuclear leukocytes from diabetic patients. This result correlates with the increase in GLO-1 activity in the whole blood samples of type 2 diabetes patients
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
vander Jagt, D.L.
The glyoxalase system
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
597-641
1989
Saccharomyces cerevisiae, Oryctolagus cuniculus, Escherichia coli, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum, Sus scrofa
-
Manually annotated by BRENDA team
Mannervik, B.; Aronsson, A.C.; Tibbelin, G.
Glyoxalase I from human erythrocytes
Methods Enzymol.
90
535-541
1982
Homo sapiens
Manually annotated by BRENDA team
Marmstal, E.; Aronsson, A.C.; Mannervik, B.
Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources
Biochem. J.
183
23-30
1979
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Aronsson, A.C.; Tibbelin, G.; Mannervik, B.
Purification of glyoxalase I from human erythrocytes by the use of affinity chromatography and separation of the three isoenzymes
Anal. Biochem.
92
390-393
1979
Homo sapiens
Manually annotated by BRENDA team
Cameron, A.D.; Olin, B.; Ridderstrom, M.; Mannervik, B.; Jones, T.A.
Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping
EMBO J.
16
3395-3395
1997
Homo sapiens
-
Manually annotated by BRENDA team
Ranganathan, S.; Walsh, E.S.; Godwin, A.K.; Tew, K.D.
Cloning and characterization of human colon glyoxalase-I
J. Biol. Chem.
268
5661-5667
1993
Homo sapiens
Manually annotated by BRENDA team
Kim, N.S.; Sekine, S.; Kiuchi, N.; Kato, S.
cDNA cloning and characterization of human glyoxalase I isoforms from HT-1080 cells
J. Biochem.
117
359-361
1995
Homo sapiens
Manually annotated by BRENDA team
Allen, R.E.; Lo, T.W.C.; Thornalley, P.J.
Inhibitors of glyoxalase I: design, synthesis, inhibitory characteristics and biological evaluation
Biochem. Soc. Trans.
21
535-540
1993
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Allen, R.E.; Lo, T.W.C.; Thornalley, P.J.
A simplified method for the purification of human red blood cell glyoxalase. I. Characteristics, immunoblotting, and inhibitor studies
J. Protein Chem.
12
111-119
1993
Homo sapiens
Manually annotated by BRENDA team
Shinohara, M.; Thornalley, P.J.; Giardino, I.; Beisswenger, P.; Thorpe, S.R.; Onorato, J.; Brownlee, M.
Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
J. Clin. Invest.
101
1142-1147
1998
Homo sapiens
Manually annotated by BRENDA team
Creighton, D.J.; Hamilton, D.S.
Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations
Arch. Biochem. Biophys.
387
1-10
2001
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Mitsumoto, A.; Kim, K.R.; Oshima, G.; Kunimoto, M.; Okawa, K.; Iwamatsu, A.; Nakagawa, Y.
Glyoxalase I is a novel nitric-oxide-responsive protein
Biochem. J.
344
837-844
1999
Homo sapiens
Manually annotated by BRENDA team
Cameron, A.D.; Ridderstrom, M.; Olin, B.; Kavarana, M.J.; Creighton, D.J.; Mannervik, B.
Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue
Biochemistry
38
13480-13490
1999
Homo sapiens (Q04760), Homo sapiens
Manually annotated by BRENDA team
Sakamoto, H.; Mashima, T.; Kizaki, A.; Dan, S.; Hashimoto, Y.; Naito, M.; Tsuruo, T.
Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis
Blood
95
3214-3218
2000
Homo sapiens
Manually annotated by BRENDA team
Himo, F.; Siegbahn, P.E.
Catalytic mechanism of glyoxalase I: a theoretical study
J. Am. Chem. Soc.
123
10280-10289
2001
Homo sapiens
Manually annotated by BRENDA team
ichter, U.; Krauss, M.
Active site structure and mechanism of human glyoxalase I-an ab initio theoretical study
J. Am. Chem. Soc.
123
6973-6982
2001
Homo sapiens
Manually annotated by BRENDA team
Lupidi, G.; Bollettini, M.; Venardi, G.; Marmocchi, F.; Rotilio, G.
Functional residues on the enzyme active site of glyoxalase I from bovine brain
Prep. Biochem. Biotechnol.
31
317-329
2001
Bos taurus, Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Davidson, S.D.; Milanesa, D.M.; Mallouh, C.; Choudhury, M.S.; Tazaki, H.; Konno, S.
A possible regulatory role of glyoxalase I in cell viability of human prostate cancer
Urol. Res.
30
116-121
2002
Homo sapiens
Manually annotated by BRENDA team
Akoachere, M.; Iozef, R.; Rahlfs, S.; Deponte, M.; Mannervik, B.; Creighton, D.J.; Schirmer, H.; Becker, K.
Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts
Biol. Chem.
386
41-52
2005
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Antognelli, C.; Baldracchini, F.; Talesa, V.N.; Costantini, E.; Zucchi, A.; Mearini, E.
Overexpression of glyoxalase system enzymes in human kidney tumor
Cancer J.
12
222-228
2006
Homo sapiens, Homo sapiens (Q04760)
Manually annotated by BRENDA team
Miller, A.G.; Smith, D.G.; Bhat, M.; Nagaraj, R.H.
Glyoxalase I is critical for human retinal capillary pericyte survival under hyperglycemic conditions
J. Biol. Chem.
281
11864-11871
2006
Homo sapiens
Manually annotated by BRENDA team
Ariza, A.; Vickers, T.J.; Greig, N.; Armour, K.A.; Dixon, M.J.; Eggleston, I.M.; Fairlamb, A.H.; Bond, C.S.
Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme
Mol. Microbiol.
59
1239-1248
2006
Homo sapiens (Q04760), Homo sapiens, Leishmania major (Q68RJ8), Leishmania major
Manually annotated by BRENDA team
Kuhla, B.; Boeck, K.; Schmidt, A.; Ogunlade, V.; Arendt, T.; Muench, G.; Lueth, H.J.
Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimers disease brains
Neurobiol. Aging
28
29-41
2007
Homo sapiens
Manually annotated by BRENDA team
Korybalska, K.; Wisniewska-Elnur, J.; Trominska, J.; Joerres, A.; Breborowicz, A.; Witowski, J.
The role of the glyoxalase pathway in reducing mesothelial toxicity of glucose degradation products
Perit. Dial. Int.
26
259-265
2006
Homo sapiens
Manually annotated by BRENDA team
Ahmed, U.; Dobler, D.; Larkin, S.J.; Rabbani, N.; Thornalley, P.J.
Reversal of hyperglycemia-induced angiogenesis deficit of human endothelial cells by overexpression of glyoxalase 1 in vitro
Ann. N. Y. Acad. Sci.
1126
262-264
2008
Homo sapiens
Manually annotated by BRENDA team
Kalousova, M.; Germanova, A.; Jachymova, M.; Mestek, O.; Tesar, V.; Zima, T.
A419C (E111A) polymorphism of the glyoxalase I gene and vascular complications in chronic hemodialysis patients
Ann. N. Y. Acad. Sci.
1126
268-271
2008
Homo sapiens
Manually annotated by BRENDA team
Takasawa, R.; Takahashi, S.; Saeki, K.; Sunaga, S.; Yoshimori, A.; Tanuma, S.
Structure-activity relationship of human GLO I inhibitory natural flavonoids and their growth inhibitory effects
Bioorg. Med. Chem.
16
3969-3975
2008
Homo sapiens (Q04760), Homo sapiens
Manually annotated by BRENDA team
Sukdeo, N.; Honek, J.F.
Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal
Drug Metabol. Drug Interact.
23
29-50
2008
Escherichia coli, Escherichia coli (P0AC81), Homo sapiens, Homo sapiens (Q04760), Leishmania braziliensis, Leishmania donovani, Leishmania major, Leishmania sp., Neisseria meningitidis, Neisseria meningitidis (P0A0T3), Plasmodium falciparum, Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HU72), Pseudomonas aeruginosa (Q9HY85), Pseudomonas aeruginosa (Q9I5L8), Pseudomonas putida, Pseudomonas putida (Q88GF8), Trypanosoma cruzi, Yersinia pestis
Manually annotated by BRENDA team
de Hemptinne, V.; Rondas, D.; Toepoel, M.; Vancompernolle, K.
Phosphorylation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kappaB
Mol. Cell. Biochem.
325
169-178
2009
Homo sapiens
Manually annotated by BRENDA team
Santel, T.; Pflug, G.; Hemdan, N.Y.; Schaefer, A.; Hollenbach, M.; Buchold, M.; Hintersdorf, A.; Lindner, I.; Otto, A.; Bigl, M.; Oerlecke, I.; Hutschenreuter, A.; Sack, U.; Huse, K.; Groth, M.; Birkemeyer, C.; Schellenberger, W.; Gebhardt, R.; Platzer, M.; Weiss, T.; Vijayalakshmi, M.A.; Krueger, M.
Curcumin inhibits glyoxalase 1: a possible link to its anti-inflammatory and anti-tumor activity
PLoS ONE
3
e3508
2008
Homo sapiens
Manually annotated by BRENDA team
Inagi, R.; Kumagai, T.; Fujita, T.; Nangaku, M.
The role of glyoxalase system in renal hypoxia
Adv. Exp. Med. Biol.
662
49-55
2010
Homo sapiens
Manually annotated by BRENDA team
Mailankot, M.; Padmanabha, S.; Pasupuleti, N.; Major, D.; Howell, S.; Nagaraj, R.H.
Glyoxalase I activity and immunoreactivity in the aging human lens
Biogerontology
10
711-720
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Yuan, M.; Luo, M.; Bu, X.; Luo, H.B.; Hu, X.
Binding of curcumin with glyoxalase I: Molecular docking, molecular dynamics simulations, and kinetics analysis
Biophys. Chem.
147
28-34
2010
Homo sapiens (Q04760)
Manually annotated by BRENDA team
Louie, B.; Rajamahanty, S.; Pyo, P.; Choudhury, M.; Konno, S.
Mode of cytotoxic action of nephrotoxic agents: oxidative stress and glutathione-dependent enzyme
BJU Int.
105
264-268
2010
Homo sapiens
Manually annotated by BRENDA team
Antognelli, C.; Del Buono, C.; Ludovini, V.; Gori, S.; Talesa, V.N.; Crino, L.; Barberini, F.; Rulli, A.
CYP17, GSTP1, PON1 and GLO1 gene polymorphisms as risk factors for breast cancer: an Italian case-control study
BMC Cancer
9
115
2009
Homo sapiens
Manually annotated by BRENDA team
Germanova, A.; Germanova, A.; Tesarova, P.; Jachymova, M.; Zvara, K.; Zima, T.; Kalousova, M.
Glyoxalase I Glu111Ala polymorphism in patients with breast cancer
Cancer Invest.
27
655-660
2009
Homo sapiens
Manually annotated by BRENDA team
Takeuchi, M.; Kimura, S.; Kuroda, J.; Ashihara, E.; Kawatani, M.; Osada, H.; Umezawa, K.; Yasui, E.; Imoto, M.; Tsuruo, T.; Yokota, A.; Tanaka, R.; Nagao, R.; Nakahata, T.; Fujiyama, Y.; Maekawa, T.
Glyoxalase-I is a novel target against Bcr-Abl+ leukemic cells acquiring stem-like characteristics in a hypoxic environment
Cell Death Differ.
17
1211-1220
2010
Homo sapiens
Manually annotated by BRENDA team
Davies, G.F.; Juurlink, B.H.; Harkness, T.A.
Troglitazone reverses the multiple drug resistance phenotype in cancer cells
Drug Des. Devel. Ther.
3
79-88
2009
Homo sapiens
Manually annotated by BRENDA team
Engelen, L.; Ferreira, I.; Brouwers, O.; Henry, R.M.; Dekker, J.M.; Nijpels, G.; Heine, R.J.; van Greevenbroek, M.M.; van der Kallen, C.J.; Blaak, E.E.; Feskens, E.J.; ten Cate, H.; Stehouwer, C.D.; Schalkwijk, C.G.
Polymorphisms in glyoxalase 1 gene are not associated with vascular complications: the Hoorn and CoDAM studies
J. Hypertens.
27
1399-1403
2009
Homo sapiens
Manually annotated by BRENDA team
More, S.S.; Vince, R.
Inhibition of glyoxalase I: the first low-nanomolar tight-binding inhibitors
J. Med. Chem.
52
4650-4656
2009
Homo sapiens
Manually annotated by BRENDA team
Helgager, J.; Li, J.; Lubensky, I.A.; Lonser, R.; Zhuang, Z.
Troglitazone reduces glyoxalase I protein expression in glioma and potentiates the effects of chemotherapeutic agents
J. Oncol.
2010
373491
2010
Homo sapiens
Manually annotated by BRENDA team
Bair, W.B.; Cabello, C.M.; Uchida, K.; Bause, A.S.; Wondrak, G.T.
GLO1 overexpression in human malignant melanoma
Melanoma Res.
20
85-96
2010
Homo sapiens
Manually annotated by BRENDA team
Karg, E.; Papp, F.; Tassi, N.; Janaky, T.; Wittmann, G.; Turi, S.
Enhanced methylglyoxal formation in the erythrocytes of hemodialyzed patients
Metab. Clin. Exp.
58
976-982
2009
Homo sapiens
Manually annotated by BRENDA team
Thornalley, P.J.; Waris, S.; Fleming, T.; Santarius, T.; Larkin, S.J.; Winklhofer-Roob, B.M.; Stratton, M.R.; Rabbani, N.
Imidazopurinones are markers of physiological genomic damage linked to DNA instability and glyoxalase 1-associated tumour multidrug resistance
Nucleic Acids Res.
38
5432-5442
2010
Homo sapiens
Manually annotated by BRENDA team
Birkenmeier, G.; Stegemann, C.; Hoffmann, R.; Guenther, R.; Huse, K.; Birkemeyer, C.
Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation
PLoS ONE
5
e10399
2010
Homo sapiens (Q04760), Homo sapiens
Manually annotated by BRENDA team
Thornalley, P.J.; Rabbani, N.
Highlights and hotspots of protein glycation in end-stage renal disease
Semin. Dial.
22
400-404
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Yuan, M.; Li, Z.; Cheng, Y.K.; Luo, H.B.; Hu, X.
Structural investigation into the inhibitory mechanisms of indomethacin and its analogues towards human glyoxalase I
Bioorg. Med. Chem. Lett.
21
4243-4247
2011
Homo sapiens
Manually annotated by BRENDA team
Takasawa, R.; Tao, A.; Saeki, K.; Shionozaki, N.; Tanaka, R.; Uchiro, H.; Takahashi, S.; Yoshimori, A.; Tanuma, S.
Discovery of a new type inhibitor of human glyoxalase I by myricetin-based 4-point pharmacophore
Bioorg. Med. Chem. Lett.
21
4337-4342
2011
Homo sapiens
Manually annotated by BRENDA team
Yuan, M.; Luo, M.; Song, Y.; Xu, Q.; Wang, X.; Cao, Y.; Bu, X.; Ren, Y.; Hu, X.
Identification of curcumin derivatives as human glyoxalase I inhibitors: A combination of biological evaluation, molecular docking, 3D-QSAR and molecular dynamics simulation studies
Bioorg. Med. Chem.
19
1189-1196
2011
Homo sapiens
Manually annotated by BRENDA team
Skapare, E.; Riekstina, U.; Liepinsh, E.; Konrade, I.; Makrecka, M.; Maurina, B.; Dambrova, M.
Flow cytometric analysis of glyoxalase-1 expression in human leukocytes
Cell Biochem. Funct.
29
171-174
2011
Homo sapiens
Manually annotated by BRENDA team
Hanssen, N.M.; Stehouwer, C.D.; Schalkwijk, C.G.
Methylglyoxal and glyoxalase I in atherosclerosis
Biochem. Soc. Trans.
42
443-449
2014
Homo sapiens
Manually annotated by BRENDA team
Deponte, M.
Glyoxalase diversity in parasitic protists
Biochem. Soc. Trans.
42
473-478
2014
Homo sapiens, Leishmania braziliensis, Leishmania donovani, Leishmania infantum, Leishmania major, no activity in Entamoeba histolytica, Plasmodium falciparum, Trypanosoma cruzi, no activity in Trypanosoma brucei, no activity in Giardia lamblia
Manually annotated by BRENDA team
Honek, J.F.
Bacterial glyoxalase I enzymes: structural and biochemical investigations
Biochem. Soc. Trans.
42
479-484
2014
Saccharomyces cerevisiae, Clostridium acetobutylicum, Escherichia coli, Homo sapiens, Leishmania donovani, Leishmania infantum, Leishmania major, Neisseria meningitidis, Yersinia pestis, Plasmodium falciparum, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas syringae, Trypanosoma cruzi
Manually annotated by BRENDA team
Wortmann, M.; Peters, A.S.; Hakimi, M.; Boeckler, D.; Dihlmann, S.
Glyoxalase I (Glo1) and its metabolites in vascular disease
Biochem. Soc. Trans.
42
528-533
2014
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chiba, T.; Ohwada, J.; Sakamoto, H.; Kobayashi, T.; Fukami, T.A.; Irie, M.; Miura, T.; Ohara, K.; Koyano, H.
Design and evaluation of azaindole-substituted N-hydroxypyridones as glyoxalase I inhibitors
Bioorg. Med. Chem. Lett.
22
7486-7489
2012
Homo sapiens
Manually annotated by BRENDA team
Holewinski, R.J.; Creighton, D.J.
Inhibition by active site directed covalent modification of human glyoxalase I
Bioorg. Med. Chem.
22
3301-3308
2014
Homo sapiens
Manually annotated by BRENDA team
Hikita, K.; Yamada, S.; Shibata, R.; Katoh, M.; Murata, T.; Kato, K.; Tanaka, H.; Kaneda, N.
Inhibitory effect of isoflavones from Erythrina poeppigiana on the growth of HL-60 human leukemia cells through inhibition of glyoxalase I
Nat. Prod. Commun.
10
1581-1584
2015
Homo sapiens (Q04760), Homo sapiens
Manually annotated by BRENDA team