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Information on EC 1.1.1.21 - aldose reductase and Organism(s) Homo sapiens and UniProt Accession P42330

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.21 aldose reductase
IUBMB Comments
Has wide specificity.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P42330
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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
Reaction Schemes
Synonyms
aldose reductase, akr1b10, akr1b3, akr1b, aldose reductase-like, aldose reductase-like protein, aldo-keto reductase family 1 member b1, akr1b14, aldrxv4, aldose reductase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17betaHSD5
-
aldoketo reductase 1C3
-
20-alpha-HSD
-
-
-
-
20-alpha-hydroxysteroid dehydrogenase
-
-
-
-
AKR1B
-
-
AKR1B1
AKR1B10
aldehyde reductase
alditol/NADP+ oxidoreductase
alditol: NADP+ 1-oxidoreductase
-
-
alditol:NAD(P)+1oxidoreductase
-
-
alditol:NADP 1-oxidoreductase
-
-
-
-
alditol:NADP oxidoreductase
-
-
-
-
aldo-keto reductase family 1 member B1
-
aldo-keto reductase family 1 member B7
-
-
-
-
aldose reductase
aldose reductase-like
-
aldose reductase-like protein
-
aldose xylose reductase
-
-
-
-
ALR1
-
-
Fibroblast growth factor regulated protein
-
-
-
-
FR-1 protein
-
-
-
-
HRAR
-
-
MVDP
-
-
-
-
NADPH-aldopentose reductase
-
-
-
-
NADPH-aldose reductase
-
-
-
-
polyol dehydrogenase (NADP2)
-
-
-
-
small intestine reductase
-
TPN-polyol dehydrogenase
-
-
-
-
VAS deferens androgen-dependent protein
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alditol + NAD(P)+ = aldose + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alditol:NAD(P)+ 1-oxidoreductase
Has wide specificity.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-31-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-acetyl-2,3,5,6-tetrahydro-1H,4H-11-oxa-3a-aza-benzo[de]anthracen-10-one + NADPH + H+
? + NADP+
show the reaction diagram
fluorogenic synthetic substrate
-
-
?
1-butanal + NADPH + H+
butanol + NADP+
show the reaction diagram
-
-
-
?
1-decanol + NADP+
decanal + NADPH + H+
show the reaction diagram
-
-
-
?
1-dodecanal + NADPH + H+
dodecanol + NADP+
show the reaction diagram
-
-
-
?
1-heptanal + NADPH + H+
heptanol + NADP+
show the reaction diagram
-
-
-
?
1-hexanal + NADPH + H+
hexanol + NADP+
show the reaction diagram
-
-
-
?
1-hydroxynonen-4-one + NADPH
1,4-dihydroxynon-2-ene + NADP+
show the reaction diagram
-
-
-
?
1-nonanal + NADPH + H+
nonanol + NADP+
show the reaction diagram
-
-
-
?
1-nonanol + NADP+
nonanal + NADPH + H+
show the reaction diagram
-
-
-
?
1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine + NADPH
1-palmitoyl-2-(5-hydroxyvaleryl)sn-glycero-3-phosphocholine + NADP+
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine + NADPH + H+
? + NADP+
show the reaction diagram
ALR2
-
-
?
1-tetradecanol + NADP+
tetradecanal + NADPH + H+
show the reaction diagram
-
-
-
?
11-deoxyisocorticosterone + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
2,3-bornanedione + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
2,3-hexanedione + NADPH + H+
?
show the reaction diagram
-
-
-
?
2-D-deoxygalactose + NADPH
?
show the reaction diagram
-
-
-
-
?
20-isocortisol + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
20alpha-hydroxyprogesterone + NADPH + H+
?
show the reaction diagram
-
-
-
?
20alpha-isocorticosterone + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
21-dehydrocortisol + NADPH + H+
?
show the reaction diagram
-
-
-
?
3-deoxyglucosone + NADPH + H+
?
show the reaction diagram
-
-
-
?
4-bromobenzaldehyde + NADPH + H+
4-bromobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
r
4-carboxybenzaldehyde + NADPH + H+
4-carboxybenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
r
4-hydroxynonenal + NADPH + H+
4-hydroxynonanol + NADP+
show the reaction diagram
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD(P)H
4-hydroxyphenylethyl alcohol + NAD(P)+
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylglycolaldehyde + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
4-nitrobenzaldehyde + NAD(P)H
4-nitrobenzyl alcohol + NAD(P)+
show the reaction diagram
-
-
-
-
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
?
4-oxonon-2-enal + NADPH + H+
1-hydroxynonen-4-one + NADP+
show the reaction diagram
-
-
-
?
5-pregnene-3beta,20alpha-diol + NADPH
?
show the reaction diagram
-
-
-
?
5alpha-pregnan-20alpha-ol-3-one + NADPH + H+
?
show the reaction diagram
-
-
-
?
5alpha-pregnane-3beta,20alpha-diol + NADPH + H+
?
show the reaction diagram
-
-
-
?
alditol + NAD(P)+
aldose + NAD(P)H
show the reaction diagram
-
-
-
-
r
aldose + NAD(P)H
alditol + NAD(P)+
show the reaction diagram
aldose + NADPH + H+
alditol + NADP+
show the reaction diagram
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
show the reaction diagram
-
-
-
?
benzyl alcohol + oxidized 3-acetylpyridine adenine dinucleotide + H+
benzaldehyde + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
butyraldehyde + NAD(P)H
butanol + NAD(P)+
show the reaction diagram
-
-
-
-
?
D-erythrose + NAD(P)H
erythritol + NAD(P)+
show the reaction diagram
-
-
-
-
r
D-erythrose + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-galactose + NAD(P)H
dulcitol + NAD(P)+
show the reaction diagram
D-galactose + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-glucose + NAD(P)H
sorbitol + NAD(P)+
show the reaction diagram
D-glucose + NADPH + H+
D-sorbitol + NADP+
show the reaction diagram
D-glucose + NADPH + H+
sorbitol + NADP+
show the reaction diagram
D-glucuronate + NAD(P)H
?
show the reaction diagram
-
-
-
-
r
D-glucuronolactone + NADPH
?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
show the reaction diagram
-
-
-
-
?
D-lactaldehyde + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-lyxose + NADPH
arabitol + NADP+
show the reaction diagram
-
-
-
-
?
D-ribose + NAD(P)H
ribitol + NAD(P)+
show the reaction diagram
-
-
-
-
r
D-ribose + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-xylose + NAD(P)H
xylitol + NAD(P)+
show the reaction diagram
-
-
-
-
r
D-xylose + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
-
?
decanal + NAD(P)H
decanol + NAD(P)+
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
show the reaction diagram
DL-glyceraldehyde + NAD(P)H + H+
glycerol + NAD(P)+
show the reaction diagram
-
-
-
?
DL-glyceraldehyde + NADPH
glycerol + NAD(P)+
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
?
show the reaction diagram
-
-
-
?
DL-glyceraldehyde + NADPH + H+
DL-glycerol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
farnesal + NADPH + H+
trans,trans-farnesol + NADP+
show the reaction diagram
specific substrate
-
-
?
geraniol + NADP+
geranial + NADPH + H+
show the reaction diagram
-
-
-
?
geranylgeranial + NADPH + H+
geranylgeraniol + NADP+
show the reaction diagram
specific substrate
-
-
?
glucose + NADPH
sorbitol + NADP+
show the reaction diagram
-
-
-
-
?
glutathione-S-4-oxonon-2-enal + NADPH
S-(1-hydroxy-4-oxonona-3-yl)glutathione + NADP+
show the reaction diagram
-
-
-
?
glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
glycolaldehyde + NADPH + H+
?
show the reaction diagram
-
-
-
?
glyoxal + NADPH + H+
?
show the reaction diagram
-
-
-
?
indole-3-acetaldehyde + NAD(P)H
indole-3-ethanol + NAD(P)+
show the reaction diagram
-
-
-
-
?
isatin + NADPH + H+
3-hydroxyisatin + NADP+
show the reaction diagram
specific substrate
-
-
?
isocaproaldehyde + NADPH + H+
?
show the reaction diagram
-
-
-
?
L-arabinose + NAD(P)H
L-arabitol + NAD(P)+
show the reaction diagram
-
-
-
-
r
L-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
L-idose + NADPH + H+
alditol + NADP+
show the reaction diagram
L-threose + NADPH + H+
?
show the reaction diagram
-
-
-
?
L-xylose + NAD(P)H
L-xylitol + NAD(P)+
show the reaction diagram
nerol + NADPH + H+
?
show the reaction diagram
-
-
-
?
octanal + NADPH + H+
octanol + NADP+
show the reaction diagram
-
-
-
?
phenylglyoxal + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD(P)H
propanol + NAD(P)+
show the reaction diagram
-
-
-
-
?
pyridine-3-aldehyde + NADPH + H+
3-pyridinemethanol + NADP+
show the reaction diagram
pyridine-3-methanol + NADP+
?
show the reaction diagram
-
-
-
?
pyridinecarboxaldehyde + NAD(P)H
pyridylmethanol + NAD(P)+
show the reaction diagram
-
2-, 3- and 4-pyridinecarboxaldehyde
-
-
?
sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
aldehyde reductase, ALR1
-
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
?
trans-2-buten-1-al + NADPH + H+
?
show the reaction diagram
-
-
-
?
trans-2-decen-1-al + NADPH + H+
?
show the reaction diagram
-
-
-
?
trans-2-hexen-1-al + NADPH + H+
?
show the reaction diagram
-
-
-
?
trans-2-nonen-1-al + NADPH + H+
?
show the reaction diagram
-
-
-
?
xylitol + NAD(P)+
D-xylose + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
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
aldose + NAD(P)H
alditol + NAD(P)+
show the reaction diagram
-
-
-
-
r
aldose + NADPH + H+
alditol + NADP+
show the reaction diagram
D-glucose + NADPH + H+
D-sorbitol + NADP+
show the reaction diagram
D-glucose + NADPH + H+
sorbitol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
DL-glycerol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
?
glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
?
sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
aldehyde reductase, ALR1
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
-
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Li2SO4
Mg2+
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butyl-2-[[(4-oxo-3,4-dihydroquinazolin-2-yl)methyl]sulfanyl]-1H-benzimidazole-5-sulfonamide
classical competitive mechanism. No significant influence on 11beta-HSD activities
2-[(4-fluorobenzyl)[(2-fluorophenyl)sulfonyl]amino]-N-[2-(3-fluorophenyl)ethyl]acetamide
-
methyl 3-methyl-2-([2-nitro-4-(trifluoromethyl)phenyl]amino)butanoate
-
N-tert-butyl-2-(2-chloro-6-methoxy-4-([(3-methyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)amino]methyl)phenoxy)acetamide
-
((3aR,4R,6S,6aR)-6-((Z)-(((4-hydroperoxybenzyl)oxy)imino)methyl)-4-hydroxy-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl 3-chlorobenzoate
83% inhibition at 0.1 mM, oxyimino derivative, obtained by reaction of a 1,5-dicarbonyl substrate with O-(arylmethyl)hydroxylamine. Inhibitor reduces both cell death and the apoptotic process when tested in an in vitro model of diabetic retinopathy
(1H-indol-1-yl)acetic acid
-
(2,3-dihydrocyclopenta[b]indol-4(1H)-yl)acetic acid
-
(2-carbamoyl-5-fluorophenoxy)acetic acid
the carboxamide nitrogen can undergo a further H-bond to the additionally recruited water molecule W2 that in turn mediates H-bonded contacts involving the additional water molecule W3 to the amide bonds next to Leu300. Using water molecules W2 and W3 as mediating partners, the compound forms additional polar contacts to the protein
(2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
7fold selectivity for ALR2 over ALR1
(2-oxo-8-phenyl-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
-
(2-oxo-8-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
24fold selectivity for ALR2 over ALR1
(2-[(4-bromo-2-fluorobenzyl)carbamoyl]-5-chlorophenoxy)acetic acid
thermodynamic binding data for isoform ALR2 and mutants
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
-
(2R)-1-[(benzyloxy)carbonyl]-2,3-dihydro-1H-indole-2-carboxylic acid
CC-13401
(2S)-3beta,7,4'-trihydroxy-5-methoxy-8-(gamma,gamma-dimethylallyl)-flavanone
-
-
(2S)-7,4'-dihydroxy-5-methoxy-8-(gamma,gamma-dimethylallyl)-flavanone
-
potent inhibitor of recombinant human aldose reductase
(3-benzothiazol-2-yl-pyrrol-1-yl)acetic acid
-
50% inhibition at 49 nM
(3-methyl-1-oxo-5-phenylpyrimido[4,5-c]quinolin-2(1H)-yl)acetic acid
14fold selectivity for isoform AKR1B1 over AKR1B10
(3-sulfanyl-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
(3-sulfanyl[1,2,5]triazepino[4,3-b]indol-6(3H)-yl)acetic acid
-
(3-[(5-chloro-1,3-benzothiazol-2-yl)methyl]-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetic acid
thermodynamic binding data for isoform ALR2 and mutants
(3-[[(2-fluorophenyl)methyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
(3-[[2-oxo-2-(2,4,6-trimethylanilino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
(4-benzothiazol-2-yl-2-benzoylpyrrol-1-yl)acetic acid
-
50% inhibition at 45 nM
(4-hydroxy-3-methoxyphenyl)acetonitrile
-
IC50: 0.0244 mM
(4-hydroxy-3-methoxyphenyl)methamine
-
IC50: 0.0634 mM
(4-hydroxyphenyl)(6-hydroxypyrazin-2-yl)methanone
-
isolated from red ascidian Botryllus leachi, pyrazine derivative, IC50: 0.0414 mM
(4-hydroxyphenyl)[4-(4-hydroxyphenyl)-1H-imidazol-2-yl]methanone
-
isolated from red ascidian Botryllus leachi, imidazole derivative, IC50: 0.0214 mM
(4-oxo-3,4-dihydro-5H-pyridazino[4,5-b]indol-5-yl)acetic acid
-
(5-chloro-2-[(3-nitrobenzyl)carbamoyl]phenoxy)acetic acid
thermodynamic binding data for isoform ALR2 and mutants
(5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid
-
-
(5-methylIndoleDs)1-(3-(3,4,5-trimethoxyphenyl)-3-(5-methyl-1H-indol-3-yl)propanoyl)-4-(5-methyl-1H-indol-3-yl)piperidin-2-one
-
-
(5-methylIndoleMs)1-(3-(3,4,5-trimethoxyphenyl)-3-(5-methyl-1H-indol-3-yl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
(5Z)-3-chloro-4-(3,5-dibromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.019 mM
(5Z)-3-chloro-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-4-(4-hydroxyphenyl)furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.0008 mM
(5Z)-4-(3,5-dibromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.020 mM
(5Z)-4-(3-bromo-4-hydroxyphenyl)-3-chloro-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.013 mM
(5Z)-4-(3-bromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.048 mM
(5Z)-4-(3-bromo-4-hydroxyphenyl)-5-[(3-bromo-4-hydroxyphenyl)methylidene]-3-chlorofuran-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.017 mM
(5Z)-5-(3-aminobenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.69
(5Z)-5-(3-fluorobenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.04
(5Z)-5-(3-hydroxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.97
(5Z)-5-(3-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.88
(5Z)-5-(3-methylbenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.03
(5Z)-5-(3-phenoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.21
(5Z)-5-(3-{(E)-[(4-hydroxyphenyl)imino]methyl}benzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.73
(5Z)-5-(4-fluorobenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.09
(5Z)-5-(4-hydroxy-3-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.93
(5Z)-5-(4-hydroxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 5.05
(5Z)-5-(4-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.39
(5Z)-5-(4-{(E)-[(4-hydroxyphenyl)imino]methyl}benzylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.64
(5Z)-5-(naphthalen-1-ylmethylidene)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.97
(5Z)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-4-(4-hydroxyphenyl)furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.057 mM
(5Z)-5-[(3-bromo-4-hydroxyphenyl)methylidene]-3-chloro-4-(4-hydroxyphenyl)furan-2(5H)-one
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.046 mM
(5Z)-5-[3-(trifluoromethyl)benzylidene]-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.89
(5Z)-5-[4-(trifluoromethyl)benzylidene]-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.50
(6H-indolo[2,3-b]quinoxalin-6-yl)acetic acid
-
(7H-indolo[2',3':5,6][1,2,4]triazino[2,3-a]benzimidazol-7-yl)acetic acid
uncompetitive
(8-methyl-3-[[2-oxo-2-(propylamino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
(E)-1-(3-(1,3-diphenyl-1H-pyrazol-4-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(2,5-dimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)piperidin-2-one
-
-
(E)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)pyrrolidin-2-one
-
-
(E)-1-(3-(3-(trifluoromethyl)phenyl)acryloyl)-5,6-dihydropyridin-2(1)-one
-
-
(E)-1-(3-(3-methyl-1-phenyl-1H-pyrazol-4-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(3-phenoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(4-bromophenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(4-chlorophenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(benzo[d][1,3]dioxol-5-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(furan-2-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(naphthalen-2-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(pyridin-2-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-(thiophen-2-yl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(3-mesitylacryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-1-(4-benzylpiperazin-1-yl)-3-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(E)-1-(4-methylpiperazin-1-yl)-3-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(E)-1-(4-phenylpiperazin-1-yl)-3-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(E)-1-(piperidin-1-yl)-3-(3,4,5-trimethoxyphenyl) prop-2-en-1-one
-
-
(E)-1-(pyrrolidin-1-yl)-3-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(E)-2-(3-(3,4,5-trimethoxyphenyl)acryloyl)benzo[d]isothiazol-3(2H)-one
-
-
(E)-2-(3-(3,4,5-trimethoxyphenyl)acryloyl)isoindolin-1-one
-
-
(E)-3-((4-chlorophenyl)(hydroxy)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-((4-fluorophenyl)(hydroxy)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(3-(3,4,5-trimethoxyphenyl)acryloyl)benzo[d]oxazol-2(3H)-one
-
-
(E)-3-(5-(3-nitrophenyl)furan-2-yl)acrylic acid
-
(E)-3-(hydroxy(2-nitrophenyl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(4-nitrophenyl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(naphthalen-2-yl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(p-tolyl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(phenyl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(pyridin-2-yl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-3-(hydroxy(thiophen-2-yl)methyl)-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-5,6-dihydropyridin-2(1H)-one
-
-
(E)-4-(hydroxy(2-oxo-1-(3-(3,4,5-trimethoxyphenyl)acryloyl)-1,2,5,6-tetrahydropyridin-3-yl)methyl)benzonitrile
-
-
(E)-methyl 3-(3,4,5-trimethoxyphenyl)acrylate
-
-
(E)-N-ethanethioyl-3-(3,4,5-trimethoxyphenyl)acrylamide
-
-
(E,E)-5[2-methyl-3-phenyl-2-propenylidene-4-oxo-2-thioxo-3-thiazolidine]acetic acid
(NH4)2SO4
-
0.05 mM: slight inhibition, 400 mM: activation
(S)-6-fluorospiro[chroman-4,5'-imidazolidine]-2',4'-dione
(Z)-2-(5-biphenyl-4-ylmethylene-2,4-dioxothiazolidin-3-yl)-N-hydroxyacetamide
-
(Z)-2-(5-biphenyl-4-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
18% inhibition at 0.0125 mM
(Z)-2-(5-naphthalen-1-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
32% inhibition at 0.0125 mM
(Z)-2-(5-naphthalen-2-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
3% inhibition at 0.0125 mM
(Z)-2-[2,4-dioxo-5-(3-phenoxybenzylidene)thiazolidin-3-yl]acetamide
8% inhibition at 0.0125 mM
(Z)-2-[5-(3-hydroxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
16% inhibition at 0.0125 mM
(Z)-2-[5-(3-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
10% inhibition at 0.0125 mM
(Z)-2-[5-(4-benzyloxybenzylidene)-2,4-dioxothiazolidin-3-yl]-N-hydroxyacetamide
-
(Z)-2-[5-(4-hydroxy-3-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
-
(Z)-2-[5-(4-hydroxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
31% inhibition at 0.0125 mM
(Z)-N-hydroxy-2-(5-naphthalen-1-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
-
(Z)-N-hydroxy-2-(5-naphthalen-2-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
39% inhibition at 0.025 mM
(Z)-N-hydroxy-2-[2,4-dioxo-5-(3-phenoxybenzylidene)-thiazolidin-3-yl]acetamide
-
(Z)-N-hydroxy-2-[2,4-dioxo-5-(4-phenoxybenzylidene)-thiazolidin-3-yl]acetamide
-
(Z)-N-hydroxy-2-[5-(4-hydroxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
-
([2-[(4-methoxy-1-methyl-1H-indazol-3-yl)amino]-2-oxoethyl]sulfanyl)acetic acid
HTS-03834
([5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl)acetic acid
crystallization data
1'-(4-fluorobenzene-1-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
no selectivity for ALR2 over ALR1
1'-(5-chlorothiophene-2-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
3.4fold selectivity for ALR2 over ALR1
1-((2E,4E)-5-(benzo[d][1,3]dioxol-5-yl)penta-2,4-dienoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-((2E,4E,6E)-7-(3,4,5-trimethoxyphenyl)hepta-2,4,6-trienoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(2-chlorobenzoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(2-iodobenzoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(1-benzyl-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-4-(1-benzyl-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(1-benzyl-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-4-(1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(1-methyl-1H-indol-3-yl)propanoyl)-4-(1-methyl-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(1-methyl-1H-indol-3-yl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(2-methyl-1H-indol-3-yl)propanoyl)-4-(2-methyl-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(2-phenyl-1H-indol-3-yl)propanoyl)-4-(2-phenyl-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(5-methoxy-1H-indol-3-yl)propanoyl)-4-(5-methoxy-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(5-nitro-1H-indol-3-yl)propanoyl)-4-(5-nitro-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(3,4,5-trimethoxyphenyl)-3-(5-nitro-1H-indol-3-yl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(5-bromo-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-4-(5-bromo-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(5-bromo-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(5-fluoro-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-4-(5-fluoro-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(5-fluoro-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(5-iodo-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-4-(5-iodo-1H-indol-3-yl)piperidin-2-one
-
-
1-(3-(5-iodo-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(3-(5-methoxy-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(4-fluorobenzoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(4-fluorophenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
2.1fold selectivity for ALR2 over ALR1
1-(4-methoxyphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
8.5fold selectivity for ALR2 over ALR1
1-(4-methylphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
1.5fold selectivity for ALR2 over ALR1
1-(4-nitrobenzoyl)-5,6-dihydropyridin-2(1H)-one
-
-
1-(5-chlorothiophen-2-yl)-1,3-diazaspiro[4.5]decane-2,4-dione
1.9fold selectivity for ALR2 over ALR1
1-cinnamoyl-5,6-dihydropyridin-2(1H)-one
-
-
1-O-Galloyl-beta-D-glucose
i.e. beta-glucogallin or BGG, a major component of the Emblica officinalis medicinal plant, and a stable, potent, and specific inhibitor of aldose reductase, noncompetitive inhibition through binding the active site of AKR1B1, occupying both the anionic and the specificity pockets
1-[3-(2-phenyl-1H-indol-3-yl)-3-(3,4,5-trimethoxyphenyl)propanoyl]-5,6-dihydropyridin-2(1H)-one
-
-
17alpha-estradiol
-
17beta-estradiol
-
2,1,3-benzoxadiazol-5-yl 5-chlorothiophene-2-sulfonate
KM-07100
2,2'-[sulfonylbis(benzene-4,1-diyliminomethylylidene)]dipropanedinitrile
BTB-06667
2,2,2-trifluoro-1-[1-(1-hydroxy-1H-pyrazol-4-yl)-4-[4-(methylsulfanyl)benzoyl]-1H-pyrrol-2-yl]ethan-1-one
mixed-type inhibition
2,2,2-trifluoro-1-[4-(4-fluorobenzoyl)-1-(1-hydroxy-1H-pyrazol-4-yl)-1H-pyrrol-2-yl]ethan-1-one
mixed-type inhibition
2,5-dihydro-3H-[1,2,4]triazino[5,6-b]indole-3-thione
-
2,6-dichlorophenylacetic acid
-
competitive
2-(3,4-dimethoxyphenyl)-ethanoic acid
-
IC50: 0.0303 mM
2-(4-hydroxy-3-methoxyphenyl)ethanoic acid
-
derived from ginger rhizom, Zingiber officinale, IC50: 0.0185 mM, suppresses nt only sorbitol accumulation in human erythrocytes
2-(4-hydroxy-3-methoxyphenyl)ethanol
-
derived from ginger rhizom, Zingiber officinale, IC50: 0.0192 mM, suppresses sorbitol accumulation in human erythrocytes
2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide
crystallization data
2-amino-4-oxo-3,4-dihydropteridine-6-carboxylic acid
-
2-amino-4-oxo-3,4-dihydropteridine-7-carboxylic acid
-
2-bromophenylacetic acid
-
competitive
2-Chlorophenylacetic acid
-
competitive
2-hydroxyphenylacetic acid
-
competitive
2-naphthylacetic acid
-
competitive
2-oxo-3-(3,4,5-trihydroxyphenoxy)-1,8-naphthyridine-1(2H)-carboxylic acid
21.7fold selectivity for AKR1B1 over AKR1A1
2-oxo-3-(3,4,5-trimethoxyphenoxy)-1,8-naphthyridine-1(2H)-carboxylic acid
20.8fold selectivity for AKR1B1 over AKR1A1
2-oxo-3-phenoxy-1,8-naphthyridine-1(2H)-carboxylic acid
27fold selectivity for AKR1B1 over AKR1A1
2-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]-4-phenylbutanoic acid
-
2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide
crystallization data
3'-(4-fluorobenzene-1-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
10fold selectivity for ALR2 over ALR1
3'-(5-chlorothiophene-2-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
1.1fold selectivity for ALR2 over ALR1
3,3-Tetramethylene glutaric acid
-
-
3,4-dihydroxyphenylacetic acid
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
3,4-dinitro-2,5-bis(phenylsulfanyl)thiophene
SEW-05367
3,5-dichlorosalicylic acid
uncompetitive inhibition
3-(1H-indol-1-yl)propanoic acid
-
3-(2,4-dihydroxyphenyl)-5-hydroxy-7-methoxy-6-(3-methylbut-2-en-1-yl)-4H-chromen-4-one
-
a gamma,gamma-dimethylallyl type prenylated isoflavonoid
3-(2-phenylthiazole-4-yl)propanoic acid
-
3-(3,4,5-trimethoxyphenyl)-3-(2-methyl-1H-indol-3-yl)propanoic acid
-
-
3-(3,4-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
16.9fold selectivity for AKR1B1 over AKR1A1
3-(3,4-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
17.6fold selectivity for AKR1B1 over AKR1A1
3-(3,5-dihydroxy-4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
25.8fold selectivity for AKR1B1 over AKR1A1
3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
20.8fold selectivity for AKR1B1 over AKR1A1
3-(3,5-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
21.5fold selectivity for AKR1B1 over AKR1A1
3-(3-hydroxy-4,5-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
31.6fold selectivity for AKR1B1 over AKR1A1
3-(3-hydroxy-4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
19.3fold selectivity for AKR1B1 over AKR1A1
3-(3-hydroxy-5-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
15.1fold selectivity for AKR1B1 over AKR1A1
3-(4-fluorophenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
2.3fold selectivity for ALR2 over ALR1
3-(4-hydroxy-3-methoxyphenyl)propanol
-
IC50: 0.283 mM
3-(4-hydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
15.9fold selectivity for AKR1B1 over AKR1A1
3-(4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
20fold selectivity for AKR1B1 over AKR1A1
3-(4-methoxyphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
1.2fold selectivity for ALR2 over ALR1
3-(4-methylphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
11fold selectivity for ALR2 over ALR1
3-(4-nitrophenyl)-2-[(phenylsulfonyl)amino]propanoic acid
SPB-08302
3-(5-(3-(trifluormethyl)phenyl)thiophene-2-yl)propanoic acid
-
3-(5-(3-acetylphenyl)furan-2-yl)propanoic acid
-
3-(5-(3-aminophenyl)furan-2-yl)propanoic acid
-
3-(5-(3-methoxyphenyl)furan-2-yl)propanoic acid
-
3-(5-(3-methoxyphenyl)thiophene-2-yl)propanoic acid
-
3-(5-(3-methylphenyl)furan-2-yl)propanoic acid
-
3-(5-(3-methylphenyl)thiophene-2-yl)propanoic acid
-
3-(5-(3-methylsulfonyl)phenylfuran-2-yl)propanoic acid
-
3-(5-(3-nitrophenyl)furan-2-yl)propanoic acid
-
3-(5-(3-nitrophenyl)thiophene-2-yl)propanoic acid
-
3-(5-(3-trifluormethyl)phenylfuran-2-yl)propanoic acid
-
3-(5-chlorothiophen-2-yl)-1,3-diazaspiro[4.5]decane-2,4-dione
127fold selectivity for ALR2 over ALR1, 79% reduction in blood glucose level
3-(5-phenylfuran-2-yl)propanoic acid
-
3-(5-phenylthiophene-2-yl)propanoic acid
-
3-(5-pyridine-2-yl-furan-2-yl)propanoic acid
-
3-(5-pyridine-3-yl-furan-2-yl)propanoic acid
-
3-benzyl-1-methyl-2-oxo-1,2-dihydroquinolin-4-yl 4-methylbenzenesulfonate
NRB-05245
3-hydroxy-4-methoxymandelic acid
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
3-hydroxybutyrate
-
-
3-hydroxybutyric acid
-
-
3-nitro-L-tyrosine
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
3-[(4-bromo-2-fluorophenyl)methyl]-3,4-dihydro-4-oxo-1-phthalazineacetic acid
-
recombinant from baculovirus system in Spodoptera frugiperda cells
3-[2-(carboxymethoxy)-4-fluorobenzamido]benzoic acid
the ligand directs its acid group toward the surrounding solvent and accommodates the hydrophobic cleft adjacent to the sealed specificity pocket
3-[3,4-dihydroxy-5-(3-methylbut-2-en-1-yl)phenyl]-5,7-dihydroxy-6-(3-methylbut-2-en-1-yl)-4H-chromen-4-one
-
a gamma,gamma-dimethylallyl type prenylated isoflavonoid
3-[3-[(diethylamino)methyl]-1H-indol-1-yl]propanoic acid
-
4-(4-hydroxy-3-methoxyphenyl)-2-butanone
-
IC50: 0.197 mM
4-(4-hydroxy-3-methoxyphenyl)butanol
-
IC50: 0.642 mM
4-(5-(3-methylphenyl)thiophene-2-yl)butanoic acid
-
4-(5-phenylthiophene-2-yl)butanoic acid
-
4-androsten-17alpha-ol-3-one
i.e. epitestosterone
4-androsten-17beta-ol-3-one
i.e. testosterone
4-androstene-3,17-dione
-
4-hydroxy-3-methoxymandelic acid
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
4-hydroxy-3-methoxyphenol
-
IC50: 0.273 mM
4-hydroxy-3-methoxyphenyl methanol
-
IC50: 0.0244 mM
4-hydroxy-3-methoxyphenylacetic acid
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
4-hydroxy-3-methoxyphenyllactic acid
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
4-hydroxybenzoic acid
-
-
4-oxo-4-(5-(3-methylphenyl)thiophene-2-yl)butanoic acid
-
4-oxo-4-(5-phenylthiophen-2-yl)butanoic acid
-
4-pregenene-21-ol-3,20-dione
i.e. 11-deoxycorticosterone
4-pregnene-11beta,17alpha,21-triol-3,20-dione
i.e. cortisol
4-pregnene-11beta,21-diol-3,20-dione
i.e. corticosterone
4-pregnene-17alpha,21-diol-3,11,20-trione
i.e. cortisone
4-pregnene-18-al-11beta,21-diol-3,20-dione
i.e. aldosteron
4-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]butanoic acid
-
4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid
crystallization data
4-[3-(5-oxo-2,3-dihydro-5H-[1,3]thiazolo[3,2-a]pyrimidin-6-yl)-1,2,4-oxadiazol-5-yl]butanoic acid
4-[5,7-dimethoxy-6-(3-methylbut-2-en-1-yl)-2H-chromen-3-yl]benzene-1,3-diol
-
a gamma,gamma-dimethylallyl type prenylated isoflavonoid
4-[7-hydroxy-5-methoxy-6-(3-methylbut-2-en-1-yl)-2H-chromen-3-yl]benzene-1,3-diol
-
a gamma,gamma-dimethylallyl type prenylated isoflavonoid
5,5-diphenylhydantoin
-
-
5,6-dihydro-1-((E)-3-(3,4,5-trimethoxyphenyl)acryloyl)pyridin-2(1H)-one
-
-
5-(3-phenoxybenzyl)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.10
5-(4-phenoxybenzyl)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.39
5-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.18
5-androsten-3beta-ol-17-one
i.e. dehydroepiandrosterone
5-cholenic acid-3beta-ol
-
5-oxo-3-phenyl-5-(quinolin-2-ylamino)pentanoic acid
HTS-06058
5-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]pentanoic acid
-
5-[4-(benzyloxy)benzyl]-1,3-thiazolidine-2,4-dione
-
pIC50 is 4.50
5alpha-Androstan-17alpha-ol-3-one
-
5alpha-androstan-17beta-ol-3-one
i.e. 5alpha-dehydrotestosterone
5alpha-Androstan-3alpha-ol-17-one
-
5alpha-Androstan-3beta-ol-17-one
competitive inhibition with respect to geraniol
5alpha-androstane-3,17-dione
competitive inhibition with respect to geraniol
5alpha-androstane-3alpha,17beta-diol
-
5alpha-Androstane-3beta,17beta-diol
-
5alpha-cholanic acid-3beta-ol
-
5alpha-pregnan-3beta-ol-20-one
-
5alpha-pregnane-21-ol-3,20-dione
-
5alpha-pregnane-3,20-dione
competitive inhibition with respect to geraniol
5beta-androstan-17beta-ol-3-one
-
5beta-Androstan-3alpha-ol-17-one
-
5beta-androstan-3beta-ol-17-one
-
5beta-androstane-3,17-dione
-
5beta-androstane-3beta,17beta-diol
-
5beta-cholan-24-ol
-
5beta-cholanic acid
competitive inhibition with respect to geraniol
5beta-cholanic acid methyl ester
-
5beta-cholanic acid-3-one
-
5beta-cholanic acid-3alpha,12alpha-diol
i.e. chenodeoxycholic acid
5beta-cholanic acid-3alpha,6alpha-diol
i.e. hyodeoxycholic acid
5beta-cholanic acid-3alpha,7alpha,12alpha-triol
i.e. cholic acid
5beta-cholanic acid-3alpha,7alpha-diol
i.e. deoxycholic acid
5beta-cholanic acid-3alpha,7beta-diol
i.e. ursodeoxycholic acid
5beta-cholanic acid-3alpha-ol
i.e. lithocholic acid
5beta-cholanic acid-3beta-ol
i.e. isolithocholic acid
5beta-Pregnan-3alpha-ol-20-one
-
5beta-Pregnan-3beta-ol-20-one
-
5beta-pregnane-3,20-dione
-
6',6''-dinitrorosmarinic acid
docking structure with ALR2, overview
6'-nitrorosmarinic acid
docking structure with ALR2, overview
6-bromo-3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
19.8fold selectivity for AKR1B1 over AKR1A1
6-chloro-3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
18.4fold selectivity for AKR1B1 over AKR1A1
6-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]hexanoic acid
-
6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one
binding structure, inhibition mechanism, residues Trp111, His110, Thr113, Tyr48, Trp20, and Phe122, and the residues of the C-terminal loop Ala299, Leu300, Leu301, Ser302, Cys303 are involved, overview
6-[[(di(2,4-dimethoxyphenyl)methylidene)amino]oxy]hexanoic acid
-
-
6-[[(di(3,5-dimethoxyphenyl)methylidene)amino]oxy]hexanoic acid
-
-
6-[[(di(4-methoxy-3-methylphenyl)methylidene)amino]oxy]hexanoic acid
-
-
7-Hydroxy-4-oxo-4H-chromen-2-carboxylic acid
-
-
8-lavandulylkaempferol
-
potent inhibitor of recombinant human aldose reductase
8-methoxy-N-[(1S)-2-methyl-1-(5-phenyl-1H-imidazol-2-yl)propyl]-2H-1-benzopyran-3-carboxamide
-
8-methoxy-N-[(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
-
8-methoxy-N-[[5-(4-methoxyphenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
Alrestatin
Barbital
-
-
bezafibrate
-
noncompetitive, IC50: 0.003 mM, recombinant enzyme
butein
-
89.9% inhibition at 0.002 mM
Cibacron blue F3GA
competitive inhibition with respect to NADP+, noncompetitive inhibition with respect to geraniol
ciprofibrate
-
competitive, IC50: 0.00086 mM, recombinant enzyme
citrate
-
inhibition is pH-dependent
Clofibric acid
-
noncompetitive, IC50: 0.0012 mM, recombinant enzyme
coptisine
-
53.85-61.54% inhibition at 0.075 mg/ml
CuCl2
-
0.007 mM, 20% residual activity, addition of dithiothreitol recovers activity
curcumin
inhibits ALR2 in a non-competitive manner, also inhibits AKR1B10, docking analysis and kinetics, overview. Curcumin is able to suppress sorbitol accumulation in human erythrocytes under high glucose conditions
davallialactone
-
-
desmethylanhydroicaritin
-
potent inhibitor of recombinant human aldose reductase
dithiothreitol
-
increased inhibitory effect of sorbinil
DL-dihydrolipoic acid
-
binds very tight to the enzyme, best inhibitor of the investigated, competitive
DL-lipoamide
-
binds three-fold more weakly than D,L-lipoic acid, competitive
DL-lipoic acid
-
is effective in the treatment of diabetic complications, binds tightly to the enzyme, competitive
ellagic acid
-
-
epalrestat
epiberberine
-
69.23-76.92% inhibition at 0.075 mg/ml
estriol
i.e. 16alpha-hydroxyestradiol
Ethosuccinimide
-
-
ethyl 1-benzyl-3-hydroxy-2(5H)-oxopyrrole-4-carboxylate
-
an AR inhibitor, abolishes the accumulation of TPA-treated cells in S phase was almost completely
fenofibrate
-
competitive, IC50: 0.00056 mM, recombinant enzyme
ferulic acid
-
-
fidarestat
fisetin
-
31.1% inhibition at 0.002 mM
folic acid
-
fustin
-
20.1% inhibition at 0.002 mM
gallic acid
-
-
gemfibrozil
-
noncompetitive, IC50: 0.0065 mM, recombinant enzyme
glycochenodeoxycholic acid
-
glycolithocholic acid
groenlandicine
-
69.23-76.92% inhibition at 0.075 mg/ml
hexanoic acid
-
competitive
hypholomine B
-
-
IDD 594
IDD594
imirestat
-
-
indole-1-acetic acid
-
indomethacin
-
iodoacetate
-
-
isoliquiritigenin
-
-
isolithocholic acid
uncompetitive inhibition with respect to NADP+, competitive inhibition with respect to geraniol
kuraridin
kushenol E
-
potent inhibitor of recombinant human aldose reductase
L-tyrosine
able to prevent the formation of the tubulin/aldose reductase complex and the activation of aldose reductase by tubulin
Li2SO4
-
0.4 M: essential for full activity
lidorestat
liquiritigenin
-
-
lithocholic acid
competitive inhibition with respect to geraniol
lukianol B
-
IC50: 0.0006 mM
Mandelic acid
-
competitive
methyl [(5Z)-2,4-dioxo-5-(3-phenoxybenzylidene)-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 5.88
methyl [(5Z)-5-(3-aminobenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 4.41
methyl [(5Z)-5-(3-methoxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 5.05
methyl [(5Z)-5-(3-methylbenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 5.00
methyl [(5Z)-5-(4-fluorobenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 4.89
methyl [(5Z)-5-(4-hydroxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 5.21
methyl [5-(3-methoxybenzyl)-2,4-dioxo-1,3-thiazolidin-3-yl]acetate
-
pIC50 is 4.68
methyl {(5Z)-2,4-dioxo-5-[3-(trifluoromethyl)benzylidene]-1,3-thiazolidin-3-yl}acetate
-
pIC50 is 4.54
methyl {(5Z)-2,4-dioxo-5-[4-(trifluoromethyl)benzylidene]-1,3-thiazolidin-3-yl}acetate
-
pIC50 is 5.46
minalrestat
Morin hydrate
-
14.1% inhibition at 0.002 mM
Myricitrin
-
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-beta-alanine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-alanine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-isoleucine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-leucine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-phenylalanine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-serine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-tyrosine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-valine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)glycine
-
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)glycyl-L-phenylalanine
9% inhibition at 10.5 mM
N-(2-phenylethyl)-N-{[4-(trifluoromethyl)phenyl]sulfonyl}glycine
-
-
N-cyclopropyl-N-[cyclopropyl(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
-
N-cyclopropyl-N-[cyclopropyl(5-phenyl-1H-imidazol-2-yl)methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-cyclopropyl-N-[cyclopropyl[5-(pyridin-3-yl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
N-cyclopropyl-N-[cyclopropyl[5-(pyridin-3-yl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-ethylmaleimide
-
-
N-galloyl beta-D-glucopyranosylamine
-
N-[(1S)-1-[5-(4-bromophenyl)-1H-imidazol-2-yl]-2-methylpropyl]-2H-1-benzopyran-3-carboxamide
-
N-[(1S)-1-[5-(4-bromophenyl)-1H-imidazol-2-yl]-2-methylpropyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-[(1S)-2-methyl-1-(5-phenyl-1H-imidazol-2-yl)propyl]-2H-1-benzopyran-3-carboxamide
-
N-[(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-bromophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-bromophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl](cyclopropyl)methyl]-N-cyclopropyl-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl](cyclopropyl)methyl]-N-cyclopropyl-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
-
N-[[5-(4-methoxyphenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
-
N-[[6-methoxy-5(trifluoromethyl)-1-naphthalenyl]thioxomethyl]-N-methylglycine
N2-(2-methylaminobenzoyl)tetrahydro-1H-pyrido[3,4-b]indol-1-one
-
i.e. rhetsinine, from Evodia rutaecarpa hot water extract. Rhetsinine inhibits sorbitol accumulation by 79.3% at 0.1 mM in erythrocytes
NaCl
-
-
NADP+
-
-
naringenin
uncompetitive. The interaction is enthalpy driven and the microenvironment of aromatic residues is also altered. Naringenin inhibits fructosamine content by approximately 31.6% at 0.01 mM, and more than 93% inhibition of fluorescent advanced glycation end-products is achieved. Naringenin forms hydrogen bonds (Asn160 and Ile260), and two Pi-Pi interactions with Trp20 and one with His110
nitric oxide
-
from NO donors S-nitroso-N-acetylpenicillamine or S-nitrosoglutathione in vivo and in vitro, leads to increased S-glutathiolation of the enzyme
p-catechuic acid
-
-
p-coumaric acid
-
-
p-hydroxymercuribenzoate
-
-
pentagalloyl glucose
-
46.6% inhibition at 0.002 mM
Phenobarbital
-
-
Phenobarbitone
-
-
phenylacetic acid
-
competitive
piplartine
-
-
ponalrestat
protocatechuic acid
-
12.6% inhibition at 0.002 mM
pyrazolo[5,1-c][1,2,4]benzotriazin-8-yl dimethylcarbamate
EN-00263
quercetin
quercitrin
-
-
rosmarinic acid
docking structure with ALR2, overview
S-nitrosoglutathione
-
0.05 mM, up to 40% inhibition, possibly due to selctive formation of a single mixed disulfide between glutathione and Cys298
semilicoisoflavone B
-
contains a gamma,gamma-dimethylchromene ring on the aromatic ring
sorbinil
Statil
molecular modeling redicts an enhancement of net binding energy of the complex by 33% through replacement of the fluorine atom of statil by a carboxylate group
sulfuretin
-
69.8% inhibition at 0.002 mM
sulindac
exhibits both the highest inhibitory activity towards human aldose reductase among popular non-steroidal anti-inflammatory drugs and clear beneficial clinical effects on Type 2 diabetes, uncompetitive inhibition, enzyme binding structure, overview
sulindac sulfide
enzyme binding structure, overview
sulindac sulfone
enzyme binding structure, overview
syringic acid
-
-
Tolmetin
enzyme binding structure, overview
Tolrestat
trans-cinnamic acid
-
-
vanillic acid
Zenarestat
zopolrestat
[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino](phenyl)acetic acid
-
[(3-[[(3-nitrophenyl)methyl]carbamoyl][1,1'-biphenyl]-4-yl)oxy]acetic acid
-
[(5H-[1,2,4]triazino[5,6-b]indol-3-yl)sulfanyl]acetic acid
-
[(5Z)-2,4-dioxo-5-(3-phenoxybenzylidene)-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.89
[(5Z)-2,4-dioxo-5-(4-phenoxybenzylidene)-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.09
[(5Z)-5-(3-fluorobenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.13
[(5Z)-5-(3-hydroxy-4-methoxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.25
[(5Z)-5-(3-hydroxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.18
[(5Z)-5-(3-methoxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.32
[(5Z)-5-(3-methylbenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.19
[(5Z)-5-(3-nitrobenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.31
[(5Z)-5-(4-fluorobenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.94
[(5Z)-5-(4-hydroxy-3-methoxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.15
[(5Z)-5-(4-hydroxybenzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.82
[(5Z)-5-(biphenyl-4-ylmethylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.59
[(5Z)-5-(naphthalen-1-ylmethylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.77
[2,4-dioxo-5-(3-phenoxybenzyl)-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 6.00
[2,4-dioxo-5-(4-phenoxybenzyl)-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.55
[2-(ethynylcarbamoyl)-5-fluorophenoxy]acetic acid
the ligand exhibits a terminal pi-electron rich substituent at the amide function, which fills the cleft between Leu300 and Trp219 next to the sealed specificity pocket
[2-oxo-8-[(E)-2-phenylethenyl]-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
9fold selectivity for ALR2 over ALR1
[2-[(1,3-benzothiazol-2-yl)carbamoyl]-5-fluorophenoxy]acetic acid
an H-bond is formed between the backbone Leu300NH group and the nitrogen atom of the benzothiazolyl moiety
[3-(2,2-dimethylpropanoyl)-1H-indol-1-yl]acetic acid
-
[3-(2,4-dihydroxyphenyl)-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-(2,5-dihydroxyphenyl)-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
-
-
[3-[(diethylamino)methyl]-1H-indol-1-yl]acetic acid
-
[3-[(dimethylamino)methyl]-2-methyl-1H-indol-1-yl]acetic acid
-
[3-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
most potent activity
[3-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[(E)-2-(4-hydroxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[(E)-2-(4-hydroxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
most active inhibitor evaluated
[3-[(morpholin-4-yl)methyl]-1H-indol-1-yl]acetic acid
-
[3-[(propan-2-yl)sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl]acetic acid
-
[3-[(pyrrolidin-1-yl)methyl]-1H-indol-1-yl]acetic acid
-
[3-[2-(4-hydroxy-3-methoxyphenyl)ethyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[2-(4-hydroxy-3-methoxyphenyl)ethyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[3-[2-(4-hydroxyphenyl)ethyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
-
[5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
i.e. CMD, a potent inhibitor of ALR2, but not for ALR1, structure molecular modelling, overview. The non-conserved C-terminal residue Leu300 in ALR2, which is Pro301 in ALR1, contributes to inhibitor selectivity
[5-(3-hydroxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
i.e. HMD, modelling of inhibitor-enzyme active site complex
[5-(3-methoxybenzyl)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.53
[5-(4-bromophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
[5-(4-chlorophenyl)-1-oxo-3-propylpyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
18fold selectivity for isoform AKR1B1 over AKR1B10
[5-(4-chlorophenyl)-3-ethyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
39fold selectivity for isoform AKR1B1 over AKR1B10
[5-(4-chlorophenyl)-3-ethyl-9-fluoro-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
9fold selectivity for isoform AKR1B1 over AKR1B10
[5-(4-chlorophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
37fold selectivity for isoform AKR1B1 over AKR1B10
[5-(4-chlorophenyl)-9-fluoro-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
3fold selectivity for isoform AKR1B1 over AKR1B10
[5-(4-hydroxybenzyl)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.68
[5-(4-methoxybenzyl)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.97
[5-(biphenyl-4-ylmethyl)-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid
-
pIC50 is 5.77
[5-fluoro-2-(phenylcarbamoyl)phenoxy]acetic acid
ligand is among the weakest of the known ALR2 binders that open the specificity pocket
[5-fluoro-2-[(3-nitrophenyl)carbamoyl]phenoxy]acetic acid
the ligand opens the specificity pocket with its terminal benzyl moiety and places the meta attached nitro group deeply in the transient pocket
[5-fluoro-2-[(4,5,7-trifluoro-1,3-benzothiazol-2-yl)carbamoyl]phenoxy]acetic acid
-
[5-fluoro-2-[[[(4,5,7-trifluoro-2-benzothiazolyl)methyl]amino]carbonyl]phenoxy]acetic acid
-
[6-ethyl-3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
-
-
[6-hydroxy-3-(4-hydroxyphenoxy)pyrazin-2-yl](4-hydroxyphenyl)methanone
-
isolated from red ascidian Botryllus leachi, pyrazine derivative, IC50: 0.0194 mM
[6-methoxy-2-oxo-3-(2,4,6-trihydroxyphenyl)quinoxalin-1(2H)-yl]acetic acid
-
[6-methyl-3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
-
-
[7-methoxy-2-oxo-3-(2,4,6-trihydroxyphenyl)quinoxalin-1(2H)-yl]acetic acid
-
[7-methoxy-2-oxo-3-[(E)-2-phenylethenyl]quinoxalin-1(2H)-yl]acetic acid
-
[8-(4-formylphenyl)-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[8-(4-methoxyphenyl)-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[8-[(E)-2-(4-fluorophenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
25.7fold selectivity for ALR2 over ALR1
[8-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
24fold selectivity for ALR2 over ALR1
[8-[(E)-2-(4-hydroxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
60fold selectivity for ALR2 over ALR1
[8-[(E)-2-(4-methoxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[8-[(E)-2-(4-methylphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[8-[(E)-2-(4-nitrophenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[8-[(E)-2-(4-tert-butylphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
4fold selectivity for ALR2 over ALR1
[8-[(E)-2-([1,1'-biphenyl]-4-yl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
-
[9-fluoro-5-(4-methoxyphenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
9fold selectivity for isoform AKR1B1 over AKR1B10
[[(4-methylphenyl)sulfonyl](2-thiophen-2-ylethyl)amino]acetic acid
S-12728
{(5Z)-2,4-dioxo-5-[3-(trifluoromethyl)benzylidene]-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.33
{(5Z)-2,4-dioxo-5-[4-(trifluoromethyl)benzylidene]-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.34
{(5Z)-5-[3-(carboxymethoxy)-4-ethoxybenzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 5.85
{(5Z)-5-[3-(carboxymethoxy)benzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.64
{(5Z)-5-[4-(benzyloxy)benzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.55
{(5Z)-5-[4-(carboxymethoxy)-3-methoxybenzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.59
{(5Z)-5-[4-(carboxymethoxy)benzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid
-
pIC50 is 6.22
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
12-O-tetradecanoylphorbol-13-acetate
-
i.e. TPA, induces enzyme expression in A-549 cells and increases the enzyme activity, TPA is a potent tumor promoter, TPA-induced increase in mRNA level and promoter activity of the AR gene is significantly attenuated in the presence of inhibitors of protein kinase C, tyrosine kinase, or nuclear kinase and NF- kB, cycloheximide, actinomycin D, bisindolylmaleimide I, and genistein abolish enzyme induction by TPA
N-(beta-glucopyranosyl)-N2-acetyl-S-nitroso-N-acetylpenicillamine
-
2 mM, up to 7fold increase in activity, possibly due to nitrosation of Cys298
Na2SO4
NaCl
-
increased concentration
NADPH
in absence, loss of 60% of activity
peroxynitrite
-
peroxynitrite activates by oxidizing cysteine resiudes to sulfenic acid. C298 is the major site of sulfenic acid formation and oxidation of C298 is necessary and sufficient for enzyme activation by peroxynitrite
pyridoxal 5'-phosphate
-
2,5fold activity at 0,5 mM
SO42-
-
stimulation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.091
1-butanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0044
1-Decanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0026
1-Dodecanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0027
1-heptanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.112
1-hexanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.18
1-Hexanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0007
1-nonanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.011
1-nonanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0017
1-octanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0096
1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine
-
pH 6.0, 30°C
0.0006
1-Tetradecanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.051
2,3-Hexanedione
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0009
20alpha-hydroxyprogesterone
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.001
20alpha-Isocorticosterone
-
and 20alpha-isocortisol, values below
0.0032
21-Dehydrocortisol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.129
3-deoxyglucosone
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.02
4-bromobenzaldehyde
-
-
0.005
4-carboxybenzaldehyde
-
-
0.01
4-hydroxyphenylacetaldehyde
-
-
0.002 - 0.003
4-nitrobenzaldehyde
0.0002
5-Pregnene-3beta,20alpha-diol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0004
5alpha-pregnan-20alpha-ol-3-one
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0008
5alpha-pregnane-3beta,20alpha-diol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0097 - 0.025
benzaldehyde
0.3
benzyl alcohol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
40 - 49.3
D-galactose
57.3 - 205
D-glucose
0.152 - 6.4
D-glucuronate
0.035
D-glyceraldehyde
-
-
0.74
D-lactoaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
506 - 2740
D-Lyxose
5.04 - 1340
D-xylose
0.02 - 84
DL-glyceraldehyde
130.2 - 142
galactose
0.025
geraniol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0004 - 0.0009
geranylgeraniol
155
glucose
-
-
0.51
glyceraldehyde
-
-
21
glycolaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
11
Glyoxal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.016
Indole-3-acetaldehyde
-
-
0.0022
isatin
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.056
isocaproaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.018
L-glyceraldehyde
4
L-idose
pH 6.8, 37°C
100 - 1190
L-Xylose
0.25 - 0.62
NADH
0.0032 - 0.232
NADPH
0.02
nerol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.007
p-nitrobenzaldehyde
-
-
0.011
propionaldehyde
-
-
0.039 - 0.13
Pyridine-3-aldehyde
0.49
Pyridine-3-methanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
102
ribose
-
-
0.0023 - 0.0033
trans,trans-farnesol
0.25
trans-2-buten-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.004
trans-2-decen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.028
trans-2-hexen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0034
trans-2-nonen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
29.77
xylose
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
1-butanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.05
1-Decanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.25
1-Dodecanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
2
1-heptanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
2.37
1-hexanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.158
1-Hexanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.38
1-nonanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.065
1-nonanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.37
1-octanal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.61
1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine
-
pH 6.0, 30°C
0.017
1-Tetradecanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.32
2,3-Hexanedione
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.004
20alpha-hydroxyprogesterone
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.64
20alpha-Isocorticosterone
-
20alpha-isocortisol
0.48
21-Dehydrocortisol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.75
3-deoxyglucosone
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.006
5-Pregnene-3beta,20alpha-diol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.008
5alpha-pregnan-20alpha-ol-3-one
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.012
5alpha-pregnane-3beta,20alpha-diol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.73
benzaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.167
benzyl alcohol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.233 - 0.525
D-galactose
0.183 - 126
D-glucose
0.418 - 2.3
D-glucuronate
0.55
D-glyceraldehyde
-
-
1.87
D-lactoaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.635 - 1.7
D-xylose
0.09 - 4.6
DL-glyceraldehyde
0.567
geraniol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.078 - 0.165
geranylgeraniol
0.58
glycolaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.12
Glyoxal
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.12
isatin
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.43
isocaproaldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
143
L-idose
pH 6.8, 37°C
0.117
nerol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.76
Phenylglyoxal
-
-
2.5
Pyridine-3-aldehyde
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.042
Pyridine-3-methanol
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.155 - 0.5
trans,trans-farnesol
0.78
trans-2-buten-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.83
trans-2-decen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.82
trans-2-hexen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
1.34
trans-2-nonen-1-al
in 0.1 M potassium phosphate, pH 7.4, at 25°C
additional information
DL-glyceraldehyde
-
turnover number in mol per seconds for several mutants
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00044
(3-methyl-1-oxo-5-phenylpyrimido[4,5-c]quinolin-2(1H)-yl)acetic acid
pH 7.5, 25°C
0.00004 - 0.0078
(5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid
0.00297
6-[[(di(2,4-dimethoxyphenyl)methylidene)amino]oxy]hexanoic acid
-
pH 6.8, 37°C
0.00299
6-[[(di(3,5-dimethoxyphenyl)methylidene)amino]oxy]hexanoic acid
-
pH 6.8, 37°C
0.00292
6-[[(di(4-methoxy-3-methylphenyl)methylidene)amino]oxy]hexanoic acid
-
pH 6.8, 37°C
0.0011 - 0.0026
bezafibrate
-
pH 6.2, 25°C, recombinant enzyme
0.00088
ciprofibrate
-
pH 6.2, 25°C, recombinant enzyme
0.00124
Clofibric acid
-
pH 6.2, 25°C, recombinant enzyme
0.00056
davallialactone
-
pH 6.2, 37°C
0.00137
ellagic acid
-
pH 6.2, 37°C
0.00056
fenofibrat
-
pH 6.2, 25°C, recombinant enzyme
0.0012 - 0.0037
gemfibrozil
-
pH 6.2, 25°C, recombinant enzyme
0.00128
hypholomine B
-
pH 6.2, 37°C
0.00045
sorbinil
-
pH 6.2, 25°C, recombinant enzyme
0.000458
sulindac
pH 6.2, temperature not specified in the publication, ALR2
0.0003
sulindac sulfide
pH 6.2, temperature not specified in the publication, ALR2
0.000434
sulindac sulfone
pH 6.2, temperature not specified in the publication, ALR2
0.000043
zopolrestat
-
pH 6.2, 25°C, recombinant enzyme
0.00015
[5-(4-bromophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.00013
[5-(4-chlorophenyl)-1-oxo-3-propylpyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.000073
[5-(4-chlorophenyl)-3-ethyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.0005
[5-(4-chlorophenyl)-3-ethyl-9-fluoro-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.00013
[5-(4-chlorophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.00024
[5-(4-chlorophenyl)-9-fluoro-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
0.00024
[9-fluoro-5-(4-methoxyphenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
pH 7.5, 25°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00029
1-butyl-2-[[(4-oxo-3,4-dihydroquinazolin-2-yl)methyl]sulfanyl]-1H-benzimidazole-5-sulfonamide
Homo sapiens
pH 6.6, temperature not specified in the publication
0.0012
2-[(4-fluorobenzyl)[(2-fluorophenyl)sulfonyl]amino]-N-[2-(3-fluorophenyl)ethyl]acetamide
Homo sapiens
pH 6.6, temperature not specified in the publication
0.00126
methyl 3-methyl-2-([2-nitro-4-(trifluoromethyl)phenyl]amino)butanoate
Homo sapiens
pH 6.6, temperature not specified in the publication
0.001
N-tert-butyl-2-(2-chloro-6-methoxy-4-([(3-methyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)amino]methyl)phenoxy)acetamide
Homo sapiens
pH 6.6, temperature not specified in the publication
0.0033
(17alpha)-17-hydroxyandrost-4-en-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
7.3
(1H-indol-1-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
2.87
(2,3-dihydrocyclopenta[b]indol-4(1H)-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.001932
(2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
Homo sapiens
30°C, pH 6.2
0.00334
(2-oxo-8-phenyl-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
Homo sapiens
30°C, pH 6.2
0.000138
(2-oxo-8-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetic acid
Homo sapiens
30°C, pH 6.2
0.2572
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 7.0, 37°C
0.04141
(2R)-1-[(benzyloxy)carbonyl]-2,3-dihydro-1H-indole-2-carboxylic acid
Homo sapiens
-
0.00037
(2S)-7,4'-dihydroxy-5-methoxy-8-(gamma,gamma-dimethylallyl)-flavanone
Homo sapiens
-
-
0.00043
(3-methyl-1-oxo-5-phenylpyrimido[4,5-c]quinolin-2(1H)-yl)acetic acid
Homo sapiens
pH 7.5, 25°C
0.097
(3-sulfanyl-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
2.24
(3-[[(2-fluorophenyl)methyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
4.06
(3-[[2-oxo-2-(2,4,6-trimethylanilino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.0244
(4-hydroxy-3-methoxyphenyl)acetonitrile
Homo sapiens
-
IC50: 0.0244 mM
0.0634
(4-hydroxy-3-methoxyphenyl)methamine
Homo sapiens
-
IC50: 0.0634 mM
0.0414
(4-hydroxyphenyl)(6-hydroxypyrazin-2-yl)methanone
Homo sapiens
-
isolated from red ascidian Botryllus leachi, pyrazine derivative, IC50: 0.0414 mM
0.0214
(4-hydroxyphenyl)[4-(4-hydroxyphenyl)-1H-imidazol-2-yl]methanone
Homo sapiens
-
isolated from red ascidian Botryllus leachi, imidazole derivative, IC50: 0.0214 mM
11.46
(4-oxo-3,4-dihydro-5H-pyridazino[4,5-b]indol-5-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.019
(5Z)-3-chloro-4-(3,5-dibromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.019 mM
0.0008
(5Z)-3-chloro-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-4-(4-hydroxyphenyl)furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.0008 mM
0.02
(5Z)-4-(3,5-dibromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.020 mM
0.013
(5Z)-4-(3-bromo-4-hydroxyphenyl)-3-chloro-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.013 mM
0.048
(5Z)-4-(3-bromo-4-hydroxyphenyl)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.048 mM
0.017
(5Z)-4-(3-bromo-4-hydroxyphenyl)-5-[(3-bromo-4-hydroxyphenyl)methylidene]-3-chlorofuran-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.017 mM
0.057
(5Z)-5-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-4-(4-hydroxyphenyl)furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.057 mM
0.046
(5Z)-5-[(3-bromo-4-hydroxyphenyl)methylidene]-3-chloro-4-(4-hydroxyphenyl)furan-2(5H)-one
Homo sapiens
-
isolated from ascidians Ritterella rubra and Synoicum blochmanni, IC50: 0.046 mM
2.75
(6H-indolo[2,3-b]quinoxalin-6-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
9.95
(7H-indolo[2',3':5,6][1,2,4]triazino[2,3-a]benzimidazol-7-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.33
(8-methyl-3-[[2-oxo-2-(propylamino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.019
(E)-3-(5-(3-nitrophenyl)furan-2-yl)acrylic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0203
(Z)-2-(5-biphenyl-4-ylmethylene-2,4-dioxothiazolidin-3-yl)-N-hydroxyacetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.00734
(Z)-2-[5-(4-benzyloxybenzylidene)-2,4-dioxothiazolidin-3-yl]-N-hydroxyacetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.00652
(Z)-2-[5-(4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.0042
(Z)-N-hydroxy-2-(5-naphthalen-1-ylmethylene-2,4-dioxothiazolidin-3-yl)acetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.0127
(Z)-N-hydroxy-2-[2,4-dioxo-5-(3-phenoxybenzylidene)-thiazolidin-3-yl]acetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.00367
(Z)-N-hydroxy-2-[2,4-dioxo-5-(4-phenoxybenzylidene)-thiazolidin-3-yl]acetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.00179
(Z)-N-hydroxy-2-[5-(4-hydroxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetamide
Homo sapiens
in 0.25 M potassium phosphate buffer pH 6.8, at 37°C
0.07764
([2-[(4-methoxy-1-methyl-1H-indazol-3-yl)amino]-2-oxoethyl]sulfanyl)acetic acid
Homo sapiens
-
0.0111
1'-(4-fluorobenzene-1-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
Homo sapiens
pH 6.2, 33°C
0.00375
1'-(5-chlorothiophene-2-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
Homo sapiens
pH 6.2, 33°C
0.00776
1-(4-fluorophenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.00253
1-(4-methoxyphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.00872
1-(4-methylphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.00478
1-(5-chlorothiophen-2-yl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.008
1-O-Galloyl-beta-D-glucose
Homo sapiens
pH and temperature not specified in the publication
0.012
17alpha-estradiol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.003
17beta-estradiol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.03561
2,1,3-benzoxadiazol-5-yl 5-chlorothiophene-2-sulfonate
Homo sapiens
-
0.5271
2,2'-[sulfonylbis(benzene-4,1-diyliminomethylylidene)]dipropanedinitrile
Homo sapiens
-
4.41
2,5-dihydro-3H-[1,2,4]triazino[5,6-b]indole-3-thione
Homo sapiens
pH and temperature not specified in the publication
0.0303
2-(3,4-dimethoxyphenyl)-ethanoic acid
Homo sapiens
-
IC50: 0.0303 mM
0.0185
2-(4-hydroxy-3-methoxyphenyl)ethanoic acid
Homo sapiens
-
derived from ginger rhizom, Zingiber officinale, IC50: 0.0185 mM, suppresses nt only sorbitol accumulation in human erythrocytes
0.0192
2-(4-hydroxy-3-methoxyphenyl)ethanol
Homo sapiens
-
derived from ginger rhizom, Zingiber officinale, IC50: 0.0192 mM, suppresses sorbitol accumulation in human erythrocytes
0.0265
2-amino-4-oxo-3,4-dihydropteridine-7-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00086
2-oxo-3-(3,4,5-trihydroxyphenoxy)-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00757
2-oxo-3-(3,4,5-trimethoxyphenoxy)-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00857
2-oxo-3-phenoxy-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0251
2-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]-4-phenylbutanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00162
3'-(4-fluorobenzene-1-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
Homo sapiens
pH 6.2, 33°C
0.00491
3'-(5-chlorothiophene-2-sulfonyl)spiro[fluorene-9,4'-imidazolidine]-2',5'-dione
Homo sapiens
pH 6.2, 33°C
0.4812
3,4-dinitro-2,5-bis(phenylsulfanyl)thiophene
Homo sapiens
-
0.127
3,5-dichlorosalicylic acid
Homo sapiens
ALR2 in 50 mM potassium phosphate (pH 6.2)
53.54
3-(1H-indol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0765
3-(2,4-dihydroxyphenyl)-5-hydroxy-7-methoxy-6-(3-methylbut-2-en-1-yl)-4H-chromen-4-one
Homo sapiens
-
pH 7.0, 37°C
0.022
3-(2-phenylthiazole-4-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.00031
3-(3,4-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00568
3-(3,4-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00236
3-(3,5-dihydroxy-4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000087
3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0043
3-(3,5-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00453
3-(3-hydroxy-4,5-dimethoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0025
3-(3-hydroxy-4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00285
3-(3-hydroxy-5-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00768
3-(4-fluorophenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.283
3-(4-hydroxy-3-methoxyphenyl)propanol
Homo sapiens
-
IC50: 0.283 mM
0.00012
3-(4-hydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00268
3-(4-methoxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00831
3-(4-methoxyphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.00353
3-(4-methylphenyl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.1073
3-(4-nitrophenyl)-2-[(phenylsulfonyl)amino]propanoic acid
Homo sapiens
-
0.0019 - 0.014
3-(5-(3-(trifluormethyl)phenyl)thiophene-2-yl)propanoic acid
0.003
3-(5-(3-acetylphenyl)furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.016
3-(5-(3-aminophenyl)furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0068
3-(5-(3-methoxyphenyl)furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0054
3-(5-(3-methoxyphenyl)thiophene-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0057
3-(5-(3-methylphenyl)furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0049
3-(5-(3-methylphenyl)thiophene-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.004
3-(5-(3-methylsulfonyl)phenylfuran-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.00026
3-(5-(3-nitrophenyl)furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.00017
3-(5-(3-nitrophenyl)thiophene-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.002
3-(5-(3-trifluormethyl)phenylfuran-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.00047
3-(5-chlorothiophen-2-yl)-1,3-diazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH 6.2, 33°C
0.016
3-(5-phenylfuran-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0053
3-(5-phenylthiophene-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.031
3-(5-pyridine-2-yl-furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.019
3-(5-pyridine-3-yl-furan-2-yl)propanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.03108
3-benzyl-1-methyl-2-oxo-1,2-dihydroquinolin-4-yl 4-methylbenzenesulfonate
Homo sapiens
-
0.2808
3-[3,4-dihydroxy-5-(3-methylbut-2-en-1-yl)phenyl]-5,7-dihydroxy-6-(3-methylbut-2-en-1-yl)-4H-chromen-4-one
Homo sapiens
-
pH 7.0, 37°C
19.85
3-[3-[(diethylamino)methyl]-1H-indol-1-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.197
4-(4-hydroxy-3-methoxyphenyl)-2-butanone
Homo sapiens
-
IC50: 0.197 mM
0.642
4-(4-hydroxy-3-methoxyphenyl)butanol
Homo sapiens
-
IC50: 0.642 mM
0.0031
4-(5-(3-methylphenyl)thiophene-2-yl)butanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0064
4-(5-phenylthiophene-2-yl)butanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0016
4-androsten-17beta-ol-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0005
4-androstene-3,17-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.273
4-hydroxy-3-methoxyphenol
Homo sapiens
-
IC50: 0.273 mM
0.0244
4-hydroxy-3-methoxyphenyl methanol
Homo sapiens
-
IC50: 0.0244 mM
0.0041
4-oxo-4-(5-(3-methylphenyl)thiophene-2-yl)butanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0065
4-oxo-4-(5-phenylthiophen-2-yl)butanoic acid
Homo sapiens
in sodium phosphate buffer (100 mM, pH 6.2)
0.0025
4-pregenene-21-ol-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.017
4-pregnene-11beta,17alpha,21-triol-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.005
4-pregnene-11beta,21-diol-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0022
4-pregnene-17alpha,21-diol-3,11,20-trione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.022
4-pregnene-18-al-11beta,21-diol-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0255
4-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]butanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00119 - 0.00392
4-[3-(5-oxo-2,3-dihydro-5H-[1,3]thiazolo[3,2-a]pyrimidin-6-yl)-1,2,4-oxadiazol-5-yl]butanoic acid
0.1762
4-[5,7-dimethoxy-6-(3-methylbut-2-en-1-yl)-2H-chromen-3-yl]benzene-1,3-diol
Homo sapiens
-
pH 7.0, 37°C
0.1306
4-[7-hydroxy-5-methoxy-6-(3-methylbut-2-en-1-yl)-2H-chromen-3-yl]benzene-1,3-diol
Homo sapiens
-
pH 7.0, 37°C
0.0011
5-androsten-3beta-ol-17-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00023
5-cholenic acid-3beta-ol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0853
5-oxo-3-phenyl-5-(quinolin-2-ylamino)pentanoic acid
Homo sapiens
-
0.0117
5-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]pentanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0057
5alpha-Androstan-17alpha-ol-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00051
5alpha-androstan-17beta-ol-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0027
5alpha-Androstan-3alpha-ol-17-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00032
5alpha-Androstan-3beta-ol-17-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00039
5alpha-androstane-3,17-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0046
5alpha-androstane-3alpha,17beta-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00052
5alpha-Androstane-3beta,17beta-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.000064
5alpha-cholanic acid-3beta-ol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0005
5alpha-pregnan-3beta-ol-20-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00037
5alpha-pregnane-21-ol-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00044
5alpha-pregnane-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0042
5beta-androstan-17beta-ol-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0048
5beta-Androstan-3alpha-ol-17-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00033
5beta-androstan-3beta-ol-17-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0021
5beta-androstane-3,17-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0016
5beta-androstane-3beta,17beta-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.04
5beta-cholan-24-ol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.000052
5beta-cholanic acid
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.018
5beta-cholanic acid methyl ester
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00011
5beta-cholanic acid-3-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00021
5beta-cholanic acid-3alpha,12alpha-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00026
5beta-cholanic acid-3alpha,6alpha-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0022
5beta-cholanic acid-3alpha,7alpha,12alpha-triol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0011
5beta-cholanic acid-3alpha,7alpha-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00078
5beta-cholanic acid-3alpha,7beta-diol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00012
5beta-cholanic acid-3alpha-ol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.000027
5beta-cholanic acid-3beta-ol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00055
5beta-Pregnan-3alpha-ol-20-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00044
5beta-Pregnan-3beta-ol-20-one
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00078
5beta-pregnane-3,20-dione
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.000056
6-bromo-3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000023
6-chloro-3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00402
6-[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino]hexanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00079
8-lavandulylkaempferol
Homo sapiens
-
-
0.001
8-methoxy-N-[(1S)-2-methyl-1-(5-phenyl-1H-imidazol-2-yl)propyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000731
8-methoxy-N-[(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000899
8-methoxy-N-[[5-(4-methoxyphenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.003
bezafibrate
Homo sapiens
-
noncompetitive, IC50: 0.003 mM, recombinant enzyme
0.0007
butein
Homo sapiens
-
in 0.1 M sodium phosphate buffer (pH 6.2)
0.00086
ciprofibrate
Homo sapiens
-
competitive, IC50: 0.00086 mM, recombinant enzyme
0.0012
Clofibric acid
Homo sapiens
-
noncompetitive, IC50: 0.0012 mM, recombinant enzyme
0.1873
coptisine
Homo sapiens
-
in 100 mM sodium phosphate buffer (pH 6.2)
0.01 - 0.03
curcumin
0.00045
desmethylanhydroicaritin
Homo sapiens
-
-
0.000045 - 0.0013
epalrestat
0.1681
epiberberine
Homo sapiens
-
in 100 mM sodium phosphate buffer (pH 6.2)
0.025
estriol
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.0016
estrone
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00056
fenofibrate
Homo sapiens
-
competitive, IC50: 0.00056 mM, recombinant enzyme
0.000026 - 0.033
fidarestat
0.0525
folic acid
Homo sapiens
pH and temperature not specified in the publication
0.0065
gemfibrozil
Homo sapiens
-
noncompetitive, IC50: 0.0065 mM, recombinant enzyme
0.0071
glycochenodeoxycholic acid
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.00071
glycolithocholic acid
Homo sapiens
in 0.1 M potassium phosphate, pH 7.4, at 25°C
0.1542
groenlandicine
Homo sapiens
-
in 100 mM sodium phosphate buffer (pH 6.2)
0.00928
indomethacin
Homo sapiens
pH 6.2, temperature not specified in the publication, ALR2
0.0275
isoliquiritigenin
Homo sapiens
-
pH 7.0, 37°C
0.00027
kuraridin
Homo sapiens
-
-
0.00085
kushenol E
Homo sapiens
-
-
0.000005 - 0.027
lidorestat
0.0219
liquiritigenin
Homo sapiens
-
pH 7.0, 37°C
0.0006
lukianol B
Homo sapiens
-
IC50: 0.0006 mM
0.00028
minalrestat
Homo sapiens
ALR2 in 50 mM potassium phosphate (pH 6.2)
0.0175
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-beta-alanine
Homo sapiens
pH and temperature not specified in the publication
0.0124
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-alanine
Homo sapiens
pH and temperature not specified in the publication
0.069
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-isoleucine
Homo sapiens
pH and temperature not specified in the publication
0.0617
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-leucine
Homo sapiens
pH and temperature not specified in the publication
0.046
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-phenylalanine
Homo sapiens
pH and temperature not specified in the publication
0.0292
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-serine
Homo sapiens
pH and temperature not specified in the publication
0.216
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-tyrosine
Homo sapiens
pH and temperature not specified in the publication
0.0834
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.00197
N-(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)glycine
Homo sapiens
pH and temperature not specified in the publication
0.00367
N-cyclopropyl-N-[cyclopropyl(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.003072
N-cyclopropyl-N-[cyclopropyl(5-phenyl-1H-imidazol-2-yl)methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000222
N-cyclopropyl-N-[cyclopropyl[5-(pyridin-3-yl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000146
N-cyclopropyl-N-[cyclopropyl[5-(pyridin-3-yl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.009
N-galloyl beta-D-glucopyranosylamine
Homo sapiens
pH and temperature not specified in the publication
0.00022
N-[(1S)-1-[5-(4-bromophenyl)-1H-imidazol-2-yl]-2-methylpropyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000771
N-[(1S)-1-[5-(4-bromophenyl)-1H-imidazol-2-yl]-2-methylpropyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.00429
N-[(1S)-2-methyl-1-(5-phenyl-1H-imidazol-2-yl)propyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.002122
N-[(5-phenyl-1H-imidazol-2-yl)methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000732
N-[[5-(4-bromophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000091
N-[[5-(4-bromophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000337
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl](cyclopropyl)methyl]-N-cyclopropyl-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000031
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl](cyclopropyl)methyl]-N-cyclopropyl-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000114
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000065
N-[[5-(4-chlorophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.00042
N-[[5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000071
N-[[5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]-8-methoxy-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.000275
N-[[5-(4-methoxyphenyl)-1H-imidazol-2-yl]methyl]-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 6.2, 30°C
0.0241
N2-(2-methylaminobenzoyl)tetrahydro-1H-pyrido[3,4-b]indol-1-one
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0026
naringenin
Homo sapiens
pH 6.2, 25°C
0.16
piplartine
Homo sapiens
-
pH 7.4, 37°C
0.0387
pyrazolo[5,1-c][1,2,4]benzotriazin-8-yl dimethylcarbamate
Homo sapiens
-
0.00254 - 0.027
quercetin
0.0106
semilicoisoflavone B
Homo sapiens
-
pH 6.2, 37°C
0.00141 - 0.0036
sorbinil
0.0013
sulfuretin
Homo sapiens
-
in 0.1 M sodium phosphate buffer (pH 6.2)
0.000374
sulindac
Homo sapiens
pH 6.2, temperature not specified in the publication, ALR2
0.000279
sulindac sulfide
Homo sapiens
pH 6.2, temperature not specified in the publication, ALR2
0.000367
sulindac sulfone
Homo sapiens
pH 6.2, temperature not specified in the publication, ALR2
0.00239
Tolmetin
Homo sapiens
pH 6.2, temperature not specified in the publication, ALR2
0.00026
Tolrestat
Homo sapiens
ALR2 in 50 mM potassium phosphate (pH 6.2)
0.00006
zopolrestat
Homo sapiens
-
competitive, IC50: 0.00006 mM, recombinant enzyme
0.0426
[(2-amino-4-oxo-3,4-dihydropteridine-7-carbonyl)amino](phenyl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
3.46
[(5H-[1,2,4]triazino[5,6-b]indol-3-yl)sulfanyl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.000308
[2-oxo-8-[(E)-2-phenylethenyl]-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
13.76
[3-(2,2-dimethylpropanoyl)-1H-indol-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.00018
[3-(2,4-dihydroxyphenyl)-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00087
[3-(2,5-dihydroxyphenyl)-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000007 - 0.1
[3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
30.14
[3-[(diethylamino)methyl]-1H-indol-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
42.16
[3-[(dimethylamino)methyl]-2-methyl-1H-indol-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.00016
[3-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0001
[3-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00019
[3-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00021
[3-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0001
[3-[(E)-2-(4-hydroxyphenyl)ethenyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00006
[3-[(E)-2-(4-hydroxyphenyl)ethenyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
34.52
[3-[(morpholin-4-yl)methyl]-1H-indol-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
2.05
[3-[(propan-2-yl)sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
46.48
[3-[(pyrrolidin-1-yl)methyl]-1H-indol-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.00098
[3-[2-(4-hydroxy-3-methoxyphenyl)ethyl]-6-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00085
[3-[2-(4-hydroxy-3-methoxyphenyl)ethyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00051
[3-[2-(4-hydroxyphenyl)ethyl]-7-methoxy-2-oxoquinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0002
[5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
Homo sapiens
ALR2, pH 6.7, temperature not specified in the publication
0.00066
[5-(3-hydroxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
Homo sapiens
ALR2, pH 6.7, temperature not specified in the publication
0.0002
[5-(4-bromophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.00019
[5-(4-chlorophenyl)-1-oxo-3-propylpyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.00012
[5-(4-chlorophenyl)-3-ethyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.00041
[5-(4-chlorophenyl)-3-ethyl-9-fluoro-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.00021
[5-(4-chlorophenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.00035
[5-(4-chlorophenyl)-9-fluoro-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.000012 - 0.1012
[6-ethyl-3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
0.0194
[6-hydroxy-3-(4-hydroxyphenoxy)pyrazin-2-yl](4-hydroxyphenyl)methanone
Homo sapiens
-
isolated from red ascidian Botryllus leachi, pyrazine derivative, IC50: 0.0194 mM
0.00027
[6-methoxy-2-oxo-3-(2,4,6-trihydroxyphenyl)quinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000008 - 0.1
[6-methyl-3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acid
0.00017
[7-methoxy-2-oxo-3-(2,4,6-trihydroxyphenyl)quinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00092
[7-methoxy-2-oxo-3-[(E)-2-phenylethenyl]quinoxalin-1(2H)-yl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00105
[8-(4-formylphenyl)-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000774
[8-(4-methoxyphenyl)-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000167
[8-[(E)-2-(4-fluorophenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000188
[8-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000082
[8-[(E)-2-(4-hydroxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000208
[8-[(E)-2-(4-methoxyphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.00022
[8-[(E)-2-(4-methylphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000262
[8-[(E)-2-(4-nitrophenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.00017
[8-[(E)-2-(4-tert-butylphenyl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.000281
[8-[(E)-2-([1,1'-biphenyl]-4-yl)ethenyl]-2-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]acetic acid
Homo sapiens
30°C, pH 6.2
0.00026
[9-fluoro-5-(4-methoxyphenyl)-3-methyl-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 7.5, 25°C
0.05887
[[(4-methylphenyl)sulfonyl](2-thiophen-2-ylethyl)amino]acetic acid
Homo sapiens
-
additional information
additional information
Homo sapiens
-
gallic acid IC50: 0.0973 mg/ml, p-coumaric acid IC50: 0.1623 mg/ml, syringic acid IC50: 0.1721 mg/ml, trans-cinnamic acid IC50: 0.0681 mg/ml, p-catechuic acid IC50: 0.0427 mg/ml, quercetin IC50: 0.02523 mg/ml (in 50 mM sodium potassium phosphate buffer (pH 6.0) containing 5 mM beta-mercaptoethanol, 0.7 M NADPH, 0.4 M Li2SO4, and 2.5 mM of DL-glyceraldehyde)
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.475
-
-
1.32
-
purified enzyme, NADPH
1.68
-
-
10.2
-
-
13.6
-
lens epithelial cell extract
5.3
purified enzyme, pH 6.8, 37°C
7.333
-
purified enzyme
additional information
-
enzyme activity, and sorbitol, glucose, and fructose contents in mesangial cell, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6.7
-
-
6 - 7
-
aldehyde reduction
6.6
-
DL-glyceraldehyde + NADPH
6.7
assay at
7.4
-
assay at
9 - 10
using 0.1 mM geraniol as substrate
additional information
-
pH preference depends on the substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
at pH 5.5 and pH 7.5 about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
bone marrow endothelial, HBME, cells
Manually annotated by BRENDA team
-
recombinant enzyme
Manually annotated by BRENDA team
-
increased expression of the enzyme in sinusoidal lining cells of the tumor
Manually annotated by BRENDA team
-
lens epithelial cell line
Manually annotated by BRENDA team
-
lens epithelial cell line
Manually annotated by BRENDA team
-
healthy and diabetic livers, enzyme expression analysis, distribution in liver, expression is increased in acute and chromic liver disease, overview
Manually annotated by BRENDA team
-
in inflamed temporal arteries
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
inverse relationship between RUNX2 activity and AR expression, which is induced by hyperglycemia and supports a role for AR in the suppression of RUNX2 activity under hyperglycemic conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AK1C3_HUMAN
323
0
36853
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
gel filtration
32500
-
1 * 32500, SDS-PAGE in presence of urea and 2-mercaptoethanol
34000
34300
-
gel filtration
35700
-
x * 35700, electrospray ionisation mass spectrometry data
35727
-
x * 35727, sequence calculation
35800
-
-
36000
38000
39000
-
sucrose density gradient centrifugation, thin layer gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathionylation
-
the activity of AKR1B1 is regulated by nitric oxide and the de-nitrosylation of AKR1B1 is mediated or facilitated by intracellular reductants such as glutathione and ascorbate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with citrate and inhibitor fidarestat, resolution of 0.82 A. After the catalytic event, a rearrangement of a bound ligand can trigger the opening of the safety-belt loop of G213-S226, initiating the release of the oxidized cofactor
in complex with inhibitor IDD552, crystallized at pH 5 and 8
in complex with inhibitor zenarestat
in complex with inhibitors tolrestat, 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide and 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide. Unlike tolrestat, the naphthol[1,2-d]isothiazole inhibitors leave the specificity pocket in the closed state and ligand 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide extends the catalytic pocket by opening a novel subpocket. Inhibitor 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide provokes less pronounced induced-fit adaptations of the binding cavity
in complex with NADP+ and inhibitor 4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid, 1.43 A resolution. The inhibitor occupies the active site with its carboxylate head group located at the catalytic cavity. In complex with inhibitor {[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid at 1.55 A resolution. The nitro-aromatic moiety of both inhibitors occupies the specificity pocket of the enzyme, binding to the bottom of the pocket and provoking remarkable induced-fit adaptations
in complex with statil
in complex with the inhibitor IDD 594, hanging drop vapour diffusion method, using 40% (w/v) PEG 6000 in 50 mM diammonium hydrogen citrate at pH 5
molecular docking of glutathione analog gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine, into the binding pocket of aldose reductase. Backbone nitrogens of residues Ala299 and Leu300 form a tiny pocket gated by the thiol group of Cys298. The glycine moiety of gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine is able to displace the thiol group of Cys298 to make hydrogen bond interactions with the backbone of Ala299, Leu300, and Leu301
-
molecular docking of inhibitor 6-chloro-3-(3,5-dihydroxyphenoxy)-2-oxo-1,8-naphthyridine-1(2H)-carboxylic acid
molecular docking of inhibitor families. Flavonoids tend to bind aldose reductase in E and EC states, while sulfonyl-pyridazinones prefer ES and ECS states. Van der Waals and electrostatic interactions always have positive contributions for stabilizing flavonoids and sulfonyl-pyridazinones. The conserved feature for the aldose reductase binding pocket and the aldose reductase inhibitors is the aromatic stacking and hydrogen bonding
molecular docking of inhibitors
molecular modeling of complex with NADP+ and inhibitor (2Z)-3-(3,4-dihydroxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
purified recombinant ALR2, with the oxidized form of beta-NADPH, pH 5.0, 4°C, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
purified recombinant enzyme ALR2 in complex with inhibitor 17744184, hanging drop vapour diffusion method, mixing of 15 mg/mL ALR2 protein solution with reservoir solution containing 5% w/v PEG 6000, 5.15 mg/mL DTT, 0.66 mg/mL NADP+, and 50 mM diammonium hydrogen citrate, pH 5.0, equilibration against 1 mL of well solution containing 20% w/v PEG 6000 in 120 mM diammonium hydrogen citrate, pH 5.0, 3 days at 4°C and 2-4 days at 18°C, X-ray diffraction structure determination and analysis at 1.26 A resolution
purified recombinant enzyme in complex with 6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one, 20 mg/ml protein in 50 mM diammonium hydrogen citrate, pH 5.0, mixed with NADP+-containing solution in a ratio 1:3, hanging drop vapour diffusion method, soaking in 6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one solution, containing 5% v/v isopropanol, 5% v/v DMSO, 5% w/v beta-cyclodextrin, 25% w/v PEG 6000, 50 mM diammonium hydrogen citrate pH 5.0, and saturated pyridazinone-type inhibitor, 20°C, 3 days, X-ray diffraction structure determination and analysis at 0.95-1.43 A resolution, modeling
purified recombinant His-tagged ALR2 in complex with inhibitors sulindac, sulindac sulfide, sulindac sulfone, and tolmetin, hanging drop vapor diffusion method, 25 mg/ml enzyme with two equivalents of NADP+ and 7.5% PEG 6000 were equilibrated against a well containing 1 ml of 120 mM ammonium citrate, pH 5.0, 20% m/v PEG 6000, soaking of crystals in inhibitor saturated solution containing 25% m/v PEG 6000, 50 mM ammonium citrate, pH 5.0, and 5% v/v DMSO, X-ray diffraction structure determination and analysis
purified recombinant R268A mutant enzyme, hanging drop vapour diffusion method, 30 mg/ml protein in 5 mM phosphate, pH 7.0, mixing with equal volume of well solution containing 20% v/v PEG 6000, 25 mM MES, pH 6.0, and 16 mM ammonium sulfate, 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
purified recombinant wild-type enzyme and mutant AKR1B10 V301L holoenzyme in complex with inhibitor fidarestat and NADP+, X-ray diffraction structure determination and analysis 1.60 A resolution by replacement soaking of crystals containing inhibitor tolrestat for 14 days in 25 mM fidarestat dissolved in the reservoir solution. For crystallization of the enzyme with tolrestat by hanging-drop vapour diffusion method, 0.001 ml of 18 mg/ml protein solution containing 2 mM tolrestat is mixed with 0.001 ml of reservoir solution containing 100 mM sodium cacodylate, pH 9.0, and 30% v/v PEG, 6000, at 24°C
purified recombinant wild-type enzyme complexed with inhibitors phenylacetic acid, 2-hydroxyphenylacetic acid, 2,6-dichlorophenylacetic acid, hexanoic acid, and lipoic acid, hanging drop vapor diffusion method, 4°C, 23-25 mg/ml protein in 0.10 M sodium phosphate buffer, pH 7.0, mixed with well solution containing 20% w/v PEG 6000 and 50 mM sodium citrate, pH 5.0, microseeding, 1 month, crystal stabilization by 0.1 to 1.0% glutaraldehyde, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
-
single-crystal x-ray data, neutron Laue data analysis and quantum mechanical modeling of aldose reductase. Quantum model of catalysis
structural model
-
structures in complex with 2-carbamoyl-phenoxy-acetic acid derivatives. Opening of the protein-binding pocket occurs only once an appropriate substituent is attached to the parent substrate scaffold. Up to five water molecules entering the opened pocket cannot stabilize this state. Sole substitution with a benzyl group stabilizes the opened state, and the energetic barrier for opening is estimated to be about 5 kJ/mol. Additional decoration of the pocket-opening benzyl substituent with a nitro group results in a huge enthalpy-driven potency increase. An isosteric carboxylic acid group reduces the potency 1000fold, and binding occurs without pocket opening
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C298A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C298A/W219Y
C298S
C303D
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
C303S
F115Y
-
stable and active
F121P
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
G213P
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G213S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H110A
-
mutant enzyme
H110Q
-
mutant enzyme
K77M
-
mutant enzyme
L300A
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
L301M
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
R268A
-
site-directed mutagenesis, the mutant shows similar kinetics for the aldehyde substrate, but highly reduced affinity for the nucleotide cofactor, and reduced activity compared to the wild-type enzyme
R293A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S210A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S214A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S226A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S302R
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
T113A
-
stable and active
T113A/F115Y
-
10fold decrease in kcat value, does not bind to inhibitor (5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid
T113V
-
inhibition constants and vibrational frequencies of inhibitor (5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid in the active site
V301L
site-directed mutagenesis
V47I
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
W219A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W219E
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y48F
-
mutant enzyme
Y48S
-
mutant enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
4°C, unstable below
286240
5.1
-
90 min, 50% loss of activity
286241
6
-
unstable below
286241
6 - 9
-
4°C, several days, stable
286240
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing at temperatures above 50°C results in loss of activity
-
freezing of purified enzyme results in complete loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 4 weeks, little loss of activity
-
4°C, 2 weeks in 1% ampholines
-
4°C, 3 weeks, 50% loss of activity
-
4°C, several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Blue Sepharose column chromatography
expressed in baculovirus system
-
Ni-NTA resin column chromatography
-
nickel-charged Sepharose resin column chromatography
recombinant ALR2 from Escherichia coli, and recombinant AKR1B10 from Escherichia coli strain BL21 by anion exchange and affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS
recombinant His-tagged enzyme from Escherichia coli strain BL21 by metal affinity chromatography, removal of the His-tag by thrombin, and anion exchange chromatography to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by anion exchange chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by anion exchange chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21 gold (DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by anion exchange chromatography
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
wild type and expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in MCF-7 and HEK-293 cell
cloning from human placenta RNA by reverse transcriptase PCR and recombinant expression in Escherichia coli strain BL21(DE3)pLysS. The recombinant protein presents an additional methionine at the N-terminus as the sole modification compared to the native enzyme
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 (DE3) pLysS cells and in HeLa cells
expressed in Escherichia coli cells
expression in baculovirus system
-
expression in Escherichia coli
-
expression in Escherichia coli, with His-tag
-
expression in rat renal mesangial cells
-
expression of AKR1B10 in Escherichia coli strain BL21, and overexpression of ALR2 in Escherichia coli
expression of ALR2 in Escherichia coli
-
expression of His6-tagged ALR2 in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene AKR1B1, recombinant cardiomyocyte-specific overexpression of human enzyme in transgenic mice, adenoviral transduction. Expression in mice hearts leads to a decrease in histone deacetylase 3, HDAC3, levels accompanied by an increase in PPARgamma activity thereby contributing to lipid-enriched environment, enzyme expression leads to lipid accumulation. Human enzyme expression leads to reduced histone deacetylase 3 corepressor complexes with consequent increases in RARB in the nucleus and derepression of its target gene expression
gene AKR1B1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene AKR1B1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 gold (DE3)
gene AKR1B10, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
overexpression
-
overexpression of His-tagged enzyme in Escherichia coli strain BL21
-
overexpression of the enzyme in lens epithelial cells
-
overexpression of the enzyme in mice
-
transgenic C57BL6 background mice overexpressing human aldose reductase exhibit increased JAK2 and STAT5 activation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aldose reductase is upregulated in hyperglycemia
fidarestat significantly inhibits the enzyme activity as well as the enzyme expression
inhibition of the enzyme activity also inhibits the expression of the enzyme protein in xenograft tissue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
AKR1B10 may have a potential role as a tumor marker
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Das, B.; Srivastava, S.K.
Purification and properties of aldose reductase and aldehyde reductase II from human erythrocyte
Arch. Biochem. Biophys.
238
670-679
1985
Homo sapiens
Manually annotated by BRENDA team
Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.
Purification and characterization of human testis aldose and aldehyde reductase
Int. J. Biochem.
23
421-428
1991
Homo sapiens
Manually annotated by BRENDA team
Srivastava, S.K.; Ansari, N.H.; Hair, G.A.; Das, B.
Aldose and aldehyde reductases in human tissues
Biochim. Biophys. Acta
800
220-227
1984
Homo sapiens
Manually annotated by BRENDA team
Wermuth, B.; von Wartburg, J.P.
Aldose reductase from human tissues
Methods Enzymol.
89
181-186
1982
Homo sapiens
Manually annotated by BRENDA team
Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.
Purification and characterization of human-brain aldose reductase
Eur. J. Biochem.
127
279-284
1982
Homo sapiens
Manually annotated by BRENDA team
O'Brien, M.M.; Schofield, P.J.
Polyol-pathway enzymes of human brain. Partial purification and properties of aldose reductase and hexonate dehydrogenase
Biochem. J.
187
21-30
1980
Homo sapiens
Manually annotated by BRENDA team
Clements, R.S.; Winegrad, A.I.
Purification of alditol: NADP oxidoreductase from human placenta
Biochem. Biophys. Res. Commun.
47
1473-1479
1972
Homo sapiens
Manually annotated by BRENDA team
Ansari, N.H.; Bhatnagar, A.; Liu, S.; Srivastava, S.K.
Purification and characterization of aldose reductase and aldehyde reductase from human kidney
Biochem. Int.
25
755-765
1991
Homo sapiens
Manually annotated by BRENDA team
Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe, D.; Petsko, G.A.; Gabbay, K.H.
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme
Biochemistry
33
2021-2032
1994
Homo sapiens
Manually annotated by BRENDA team
Sato, S.; Old, S.; Carper, D.; Kador, P.F.
Purification and characterization of recombinant human placental and rat lens aldose reductases expressed in Escherichia coli
Adv. Exp. Med. Biol.
5
259-268
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera, T.; Tanimoto, T.
Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system
Biochim. Biophys. Acta
1078
171-178
1991
Homo sapiens
Manually annotated by BRENDA team
Petrash, J.M.; Tarle, I.; Wilson, D.K.; Quiocho, F.A.
Aldose reductase catalysis and crystallography
Diabetes
43
955-959
1994
Homo sapiens
Manually annotated by BRENDA team
Kinoshita, T.; Miyake, H.; Fujii, T.; Takakura, S.; Goto, T.
The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat
Acta Crystallogr. Sect. D
58
622-626
2002
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Ruiz, F.; Hazemann, I.; Mitschler, A.; Joachimiak, A.; Schneider, T.; Karplus, M.; Podjarny, A.
The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48
Acta Crystallogr. Sect. D
60
1347-1354
2004
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Srivastava, S.K.; Ramana, K.V.; Chandra, D.; Srivastava, S.; Bhatnagar, A.
Regulation of aldose reductase and the polyol pathway activity by nitric oxide
Chem. Biol. Interact.
143-144
333-340
2003
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Doorn, J.A.; Srivastava, S.K.; Petersen, D.R.
Aldose reductase catalyzes reduction of the lipid peroxidation product 4-oxonon-2-enal
Chem. Res. Toxicol.
16
1418-1423
2003
Homo sapiens (P15121)
Manually annotated by BRENDA team
Ramana, K.V.; Friedrich, B.; Bhatnagar, A.; Srivastava, S.K.
Aldose reductase mediates cytotoxic signals of hyperglycemia and TNF-alpha in human lens epithelial cells
FASEB J.
17
315-317
2003
Homo sapiens
Manually annotated by BRENDA team
Hwang, Y.C.; Kaneko, M.; Bakr, S.; Liao, H.; Lu, Y.; Lewis, E.R.; Yan, S.; Ii, S.; Itakura, M.; Rui, L.; Skopicki, H.; Homma, S.; Schmidt, A.M.; Oates, P.J.; Szabolcs, M.; Ramasamy, R.
Central role for aldose reductase pathway in myocardial ischemic injury
FASEB J.
18
1192-1199
2004
Homo sapiens
Manually annotated by BRENDA team
Ramana, K.V.; Bhatnagar, A.; Srivastava, S.K.
Aldose reductase regulates TNF-alpha-induced cell signaling and apoptosis in vascular endothelial cells
FEBS Lett.
570
189-194
2004
Homo sapiens
Manually annotated by BRENDA team
Cecconi, I.; Scaloni, A.; Rastelli, G.; Moroni, M.; Vilardo, P.G.; Costantino, L.; Cappiello, M.; Garland, D.; Carper, D.; Petrash, J.M.; Del Corso, A.; Mura, U.
Oxidative modification of aldose reductase induced by copper ion. Definition of the metal-protein interaction mechanism
J. Biol. Chem.
277
42017-42027
2002
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Srivastava, S.; Spite, M.; Trent, J.O.; West, M.B.; Ahmed, Y.; Bhatnagar, A.
Aldose reductase-catalyzed reduction of aldehyde phospholipids
J. Biol. Chem.
279
53395-53406
2004
Homo sapiens
Manually annotated by BRENDA team
Zaher, N.; Nicolaou, I.; Demopoulos, V.J.
Pyrrolylbenzothiazole derivatives as aldose reductase inhibitors
J. Enzyme Inhib.
17
131-135
2002
Homo sapiens
Manually annotated by BRENDA team
El-Kabbani, O.; Ramsland, P.; Darmanin, C.; Chung, R.P.; Podjarny, A.
Structure of human aldose reductase holoenzyme in complex with statil: an approach to structure-based inhibitor design of the enzyme
Proteins
50
230-238
2003
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Sotriffer, C.A.; Kramer, O.; Klebe, G.
Probing flexibility and "induced-fit" phenomena in aldose reductase by comparative crystal structure analysis and molecular dynamics simulations
Proteins
56
52-66
2004
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Kaneko, M.; Bucciarelli, L.; Hwang, Y.C.; Lee, L.; Yan, S.F.; Schmidt, A.M.; Ramasamy, R.
Aldose reductase and AGE-RAGE pathways: key players in myocardial ischemic injury
Ann. N. Y. Acad. Sci.
1043
702-709
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Jiang, H.; Wang, X.F.; Fang, L.; Tang, C.; Zhu, Y.; Wang, X.
Upregulation of aldose reductase by homocysteine in type II alveolar epithelial cells
Biochem. Biophys. Res. Commun.
337
1084-1091
2005
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Balendiran, G.K.; Rajkumar, B.
Fibrates inhibit aldose reductase activity in the forward and reverse reactions
Biochem. Pharmacol.
70
1653-1663
2005
Homo sapiens
Manually annotated by BRENDA team
Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison, D.H.
The structure of Apo R268A human aldose reductase: Hinges and latches that control the kinetic mechanism
Biochim. Biophys. Acta
1748
201-212
2005
Homo sapiens
Manually annotated by BRENDA team
Brownlee, J.M.; Carlson, E.; Milne, A.C.; Pape, E.; Harrison, D.H.
Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes
Bioorg. Chem.
34
424-444
2006
Homo sapiens
Manually annotated by BRENDA team
Tammali, R.; Ramana, K.V.; Singhal, S.S.; Awasthi, S.; Srivastava, S.K.
Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin e2 production in human colon cancer cells
Cancer Res.
66
9705-9713
2006
Homo sapiens
Manually annotated by BRENDA team
Kang, E.S.; Kim, H.J.; Paek, K.S.; Jang, H.S.; Chang, K.C.; Lee, J.H.; Nishinaka, T.; Yabe-Nishimura, C.; Seo, H.G.
Phorbol ester up-regulates aldose reductase expression in A549 cells: a potential role for aldose reductase in cell cycle modulation
Cell. Mol. Life Sci.
62
1146-1155
2005
Homo sapiens
Manually annotated by BRENDA team
Srivastava, S.; Tammali, R.; Chandra, D.; Greer, D.A.; Ramana, K.V.; Bhatnagar, A.; Srivastava, S.K.
Regulation of lens aldose reductase activity by nitric oxide
Exp. Eye Res.
81
664-672
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Pladzyk, A.; Ramana, K.V.; Ansari, N.H.; Srivastava, S.K.
Aldose reductase prevents aldehyde toxicity in cultured human lens epithelial cells
Exp. Eye Res.
83
408-416
2006
Homo sapiens
Manually annotated by BRENDA team
Hwang, Y.C.; Shaw, S.; Kaneko, M.; Redd, H.; Marrero, M.B.; Ramasamy, R.
Aldose reductase pathway mediates JAK-STAT signaling: a novel axis in myocardial ischemic injury
FASEB J.
19
795-797
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Drel, V.R.; Pacher, P.; Stevens, M.J.; Obrosova, I.G.
Aldose reductase inhibition counteracts nitrosative stress and poly(ADP-ribose) polymerase activation in diabetic rat kidney and high-glucose-exposed human mesangial cells
Free Radic. Biol. Med.
40
1454-1465
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Brown, K.E.; Broadhurst, K.A.; Mathahs, M.M.; Kladney, R.D.; Fimmel, C.J.; Srivastava, S.K.; Brunt, E.M.
Immunodetection of aldose reductase in normal and diseased human liver
Histol. Histopathol.
20
429-436
2005
Homo sapiens
Manually annotated by BRENDA team
Kato, A.; Higuchi, Y.; Goto, H.; Kizu, H.; Okamoto, T.; Asano, N.; Hollinshead, J.; Nash, R.J.; Adachi, I.
Inhibitory effects of Zingiber officinale Roscoe derived components on aldose reductase activity in vitro and in vivo
J. Agric. Food Chem.
54
6640-6644
2006
Homo sapiens
Manually annotated by BRENDA team
Kaiserova, K.; Srivastava, S.; Hoetker, J.D.; Awe, S.O.; Tang, X.L.; Cai, J.; Bhatnagar, A.
Redox activation of aldose reductase in the ischemic heart
J. Biol. Chem.
281
15110-15120
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Steuber, H.; Zentgraf, M.; Podjarny, A.; Heine, A.; Klebe, G.
High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group
J. Mol. Biol.
356
45-56
2006
Homo sapiens (P15121)
Manually annotated by BRENDA team
Manzanaro, S.; Salva, J.; de la Fuente, J.A.
Phenolic marine natural products as aldose reductase inhibitors
J. Nat. Prod.
69
1485-1487
2006
Homo sapiens
Manually annotated by BRENDA team
Jiang, T.; Che, Q.; Lin, Y.; Li, H.; Zhang, N.
Aldose reductase regulates TGF-beta1-induced production of fibronectin and type IV collagen in cultured rat mesangial cells
Nephrology
11
105-112
2006
Homo sapiens
Manually annotated by BRENDA team
Biadene, M.; Hazemann, I.; Cousido, A.; Ginell, S.; Joachimiak, A.; Sheldrick, G.M.; Podjarny, A.; Schneider, T.R.
The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop
Acta Crystallogr. Sect. D
63
665-672
2007
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Rakowitz, D.; Piccolruaz, G.; Pirker, C.; Matuszczak, B.
Novel aldose reductase inhibitors derived from 6-[[(diphenylmethylene)amino]oxy]hexanoic acid
Arch. Pharm.
340
202-208
2007
Homo sapiens
Manually annotated by BRENDA team
Webb, L.J.; Boxer, S.G.
Electrostatic fields near the active site of human aldose reductase: 1. New inhibitors and vibrational stark effect measurements
Biochemistry
47
1588-1598
2008
Homo sapiens
Manually annotated by BRENDA team
Lee, Y.S.; Kang, Y.H.; Jung, J.Y.; Kang, I.J.; Han, S.N.; Chung, J.S.; Shin, H.K.; Lim, S.S.
Inhibitory constituents of aldose reductase in the fruiting body of Phellinus linteus
Biol. Pharm. Bull.
31
765-768
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Tammali, R.; Ramana, K.V.; Srivastava, S.K.
Aldose reductase regulates TNF-alpha -induced PGE2 production in human colon cancer cells
Cancer Lett.
252
299-306
2007
Homo sapiens
Manually annotated by BRENDA team
Steuber, H.; Heine, A.; Klebe, G.
Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution
J. Mol. Biol.
368
618-638
2007
Homo sapiens (P15121)
Manually annotated by BRENDA team
Steuber, H.; Zentgraf, M.; La Motta, C.; Sartini, S.; Heine, A.; Klebe, G.
Evidence for a novel binding site conformer of aldose reductase in ligand-bound state
J. Mol. Biol.
369
186-197
2007
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Steuber, H.; Heine, A.; Podjarny, A.; Klebe, G.
Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features
J. Mol. Biol.
379
991-1016
2008
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Wang, S.; Yan, J.; Hao, D.; Niu, X.; Cheng, M.
Synthesis and activity of a new series of (Z)-3-phenyl-2-benzoylpropenoic acid derivatives as aldose reductase inhibitors
Molecules
12
885-895
2007
Rattus norvegicus, Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Blakeley, M.P.; Ruiz, F.; Cachau, R.; Hazemann, I.; Meilleur, F.; Mitschler, A.; Ginell, S.; Afonine, P.; Ventura, O.N.; Cousido-Siah, A.; Haertlein, M.; Joachimiak, A.; Myles, D.; Podjarny, A.
Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase
Proc. Natl. Acad. Sci. USA
105
1844-1848
2008
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Endo, S.; Matsunaga, T.; Mamiya, H.; Ohta, C.; Soda, M.; Kitade, Y.; Tajima, K.; Zhao, H.T.; El-Kabbani, O.; Hara, A.
Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids
Arch. Biochem. Biophys.
487
1-9
2009
Homo sapiens (O60218), Homo sapiens
Manually annotated by BRENDA team
Jung, H.A.; Yoon, N.Y.; Bae, H.J.; Min, B.S.; Choi, J.S.
Inhibitory activities of the alkaloids from Coptidis Rhizoma against aldose reductase
Arch. Pharm. Res.
31
1405-1412
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lee, E.H.; Song, D.G.; Lee, J.Y.; Pan, C.H.; Um, B.H.; Jung, S.H.
Inhibitory effect of the compounds isolated from Rhus verniciflua on aldose reductase and advanced glycation endproducts
Biol. Pharm. Bull.
31
1626-1630
2008
Homo sapiens
Manually annotated by BRENDA team
Chethan, S.; Dharmesh, S.M.; Malleshi, N.G.
Inhibition of aldose reductase from cataracted eye lenses by finger millet (Eleusine coracana) polyphenols
Bioorg. Med. Chem.
16
10085-10090
2008
Homo sapiens
Manually annotated by BRENDA team
Maccari, R.; Ottana, R.; Ciurleo, R.; Rakowitz, D.; Matuszczak, B.; Laggner, C.; Langer, T.
Synthesis, induced-fit docking investigations, and in vitro aldose reductase inhibitory activity of non-carboxylic acid containing 2,4-thiazolidinedione derivatives
Bioorg. Med. Chem.
16
5840-5852
2008
Homo sapiens (P15121)
Manually annotated by BRENDA team
Carbone, V.; Zhao, H.T.; Chung, R.; Endo, S.; Hara, A.; El-Kabbani, O.
Correlation of binding constants and molecular modelling of inhibitors in the active sites of aldose reductase and aldehyde reductase
Bioorg. Med. Chem.
17
1244-1250
2009
Homo sapiens (P15121)
Manually annotated by BRENDA team
Baba, S.P.; Wetzelberger, K.; Hoetker, J.D.; Bhatnagar, A.
Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation
Chem. Biol. Interact.
178
250-258
2009
Homo sapiens
Manually annotated by BRENDA team
Eisenmann, M.; Steuber, H.; Zentgraf, M.; Altenkaemper, M.; Ortmann, R.; Perruchon, J.; Klebe, G.; Schlitzer, M.
Structure-based optimization of aldose reductase inhibitors originating from virtual screening
ChemMedChem
4
809-819
2009
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Del Corso, A.; Cappiello, M.; Mura, U.
From a dull enzyme to something else: facts and perspectives regarding aldose reductase
Curr. Med. Chem.
15
1452-1461
2008
Homo sapiens
Manually annotated by BRENDA team
Cosconati, S.; Marinelli, L.; La Motta, C.; Sartini, S.; Da Settimo, F.; Olson, A.J.; Novellino, E.
Pursuing aldose reductase inhibitors through in situ cross-docking and similarity-based virtual screening
J. Med. Chem.
52
5578-5581
2009
Homo sapiens (P15121)
Manually annotated by BRENDA team
Wang, Z.; Ling, B.; Zhang, R.; Suo, Y.; Liu, Y.; Yu, Z.; Liu, C.
Docking and molecular dynamics studies toward the binding of new natural phenolic marine inhibitors and aldose reductase
J. Mol. Graph. Model.
28
162-169
2009
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Jung, H.A.; Yoon, N.Y.; Kang, S.S.; Kim, Y.S.; Choi, J.S.
Inhibitory activities of prenylated flavonoids from Sophora flavescens against aldose reductase and generation of advanced glycation endproducts
J. Pharm. Pharmacol.
60
1227-1236
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Zhang, Y.; Huang, P.; Jiang, T.; Zhao, J.; Zhang, N.
Role of aldose reductase in TGF-beta1-induced fibronectin synthesis in human mesangial cells
Mol. Biol. Rep.
37
2735-2742
2010
Homo sapiens
Manually annotated by BRENDA team
Reddy, G.B.; Satyanarayana, A.; Balakrishna, N.; Ayyagari, R.; Padma, M.; Viswanath, K.; Petrash, J.M.
Erythrocyte aldose reductase activity and sorbitol levels in diabetic retinopathy
Mol. Vis.
14
593-601
2008
Homo sapiens
Manually annotated by BRENDA team
Lee, Y.S.; Kim, S.H.; Jung, S.H.; Kim, J.K.; Pan, C.H.; Lim, S.S.
Aldose reductase inhibitory compounds from Glycyrrhiza uralensis
Biol. Pharm. Bull.
33
917-921
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Van Zandt, M.C.; Doan, B.; Sawicki, D.R.; Sredy, J.; Podjarny, A.D.
Discovery of [3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acids as highly potent and selective inhibitors of aldose reductase for treatment of chronic diabetic complications
Bioorg. Med. Chem. Lett.
19
2006-2008
2009
Homo sapiens
Manually annotated by BRENDA team
Carbone, V.; Giglio, M.; Chung, R.; Huyton, T.; Adams, J.; Maccari, R.; Ottana, R.; Hara, A.; El-Kabbani, O.
Structure of aldehyde reductase in ternary complex with a 5-arylidene-2,4-thiazolidinedione aldose reductase inhibitor
Eur. J. Med. Chem.
45
1140-1145
2010
Homo sapiens (P15121)
Manually annotated by BRENDA team
Koukoulitsa, C.; Bailly, F.; Pegklidou, K.; Demopoulos, V.J.; Cotelle, P.
Evaluation of aldose reductase inhibition and docking studies of 6-nitro and 6,6-dinitrorosmarinic acids
Eur. J. Med. Chem.
45
1663-1666
2010
Homo sapiens (P15121)
Manually annotated by BRENDA team
Muthenna, P.; Suryanarayana, P.; Gunda, S.K.; Petrash, J.M.; Reddy, G.B.
Inhibition of aldose reductase by dietary antioxidant curcumin: mechanism of inhibition, specificity and significance
FEBS Lett.
583
3637-3642
2009
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
D'Souza, D.R.; Salib, M.M.; Bennett, J.; Mochin-Peters, M.; Asrani, K.; Goldblum, S.E.; Renoud, K.J.; Shapiro, P.; Passaniti, A.
Hyperglycemia regulates RUNX2 activation and cellular wound healing through the aldose reductase polyol pathway
J. Biol. Chem.
284
17947-17955
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, H.Y.; Liu, S.S.; Qin, L.T.; Mo, L.Y.
CoMFA and CoMSIA analysis of 2,4-thiazolidinediones derivatives as aldose reductase inhibitors
J. Mol. Model.
15
837-845
2009
Homo sapiens
Manually annotated by BRENDA team
Ramana, K.V.; Tammali, R.; Srivastava, S.K.
Inhibition of aldose reductase prevents growth factor-induced G1-S phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells
Mol. Cancer Ther.
9
813-824
2010
Homo sapiens
Manually annotated by BRENDA team
Kato, A.; Yasuko, H.; Goto, H.; Hollinshead, J.; Nash, R.; Adachi, I.
Inhibitory effect of rhetsinine isolated from Evodia rutaecarpa on aldose reductase activity
Phytomedicine
16
258-261
2009
Homo sapiens
Manually annotated by BRENDA team
Tammali, R.; Reddy, A.B.; Srivastava, S.K.; Ramana, K.V.
Inhibition of aldose reductase prevents angiogenesis in vitro and in vivo
Angiogenesis
14
209-221
2011
Homo sapiens
Manually annotated by BRENDA team
Rao, V.R.; Muthenna, P.; Shankaraiah, G.; Akileshwari, C.; Babu, K.H.; Suresh, G.; Babu, K.S.; Chandra Kumar, R.S.; Prasad, K.R.; Yadav, P.A.; Petrash, J.M.; Reddy, G.B.; Rao, J.M.
Synthesis and biological evaluation of new piplartine analogues as potent aldose reductase inhibitors (ARIs)
Eur. J. Med. Chem.
57
344-361
2012
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Zhang, L.; Zhai, J.; Chen, Y.; Luo, H.; Hu, X.
The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase
FEBS Lett.
586
55-59
2012
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Tammali, R.; Saxena, A.; Srivastava, S.K.; Ramana, K.V.
Aldose reductase inhibition prevents hypoxia-induced increase in hypoxia-inducible factor-1alpha (HIF-1alpha) and vascular endothelial growth factor (VEGF) by regulating 26 S proteasome-mediated protein degradation in human colon cancer cells
J. Biol. Chem.
286
24089-24100
2011
Homo sapiens
Manually annotated by BRENDA team
Schuster, D.; Kowalik, D.; Kirchmair, J.; Laggner, C.; Markt, P.; Aebischer-Gumy, C.; Stroehle, F.; Moeller, G.; Wolber, G.; Wilckens, T.; Langer, T.; Odermatt, A.; Adamski, J.
Identification of chemically diverse, novel inhibitors of 17beta-hydroxysteroid dehydrogenase type 3 and 5 by pharmacophore-based virtual screening
J. Steroid Biochem. Mol. Biol.
125
148-161
2011
Homo sapiens (P42330)
Manually annotated by BRENDA team
Balestri, F.; Cappiello, M.; Moschini, R.; Rotondo, R.; Buggiani, I.; Pelosi, P.; Mura, U.; Del-Corso, A.
L-Idose: an attractive substrate alternative to D-glucose for measuring aldose reductase activity
Biochem. Biophys. Res. Commun.
456
891-895
2015
Homo sapiens (P15121), Homo sapiens, Bos taurus (P16116), Bos taurus
Manually annotated by BRENDA team
Balestri, F.; Cappiello, M.; Moschini, R.; Rotondo, R.; Abate, M.; Del-Corso, A.; Mura, U.
Modulation of aldose reductase activity by aldose hemiacetals
Biochim. Biophys. Acta
1850
2329-2339
2015
Homo sapiens (P15121), Homo sapiens, Bos taurus (P16116), Bos taurus
Manually annotated by BRENDA team
Saito, R.; Suzuki, S.; Sasaki, K.
Pterin-7-carboxamides as a new class of aldose reductase inhibitors
Bioorg. Med. Chem. Lett.
26
4870-4874
2016
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Thiagarajan, D.; Ananthakrishnan, R.; Zhang, J.; OShea, K.M.; Quadri, N.; Li, Q.; Sas, K.; Jing, X.; Rosario, R.; Pennathur, S.; Schmidt, A.M.; Ramasamy, R.
Aldose reductase acts as a selective derepressor of PPARgamma and the retinoic acid receptor
Cell Rep.
15
181-196
2016
Homo sapiens (P15121)
Manually annotated by BRENDA team
Ruiz, F.X.; Cousido-Siah, A.; Mitschler, A.; Farres, J.; Pares, X.; Podjarny, A.
X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP+ and the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity
Chem. Biol. Interact.
202
178-185
2013
Homo sapiens (O60218), Homo sapiens (P15121)
Manually annotated by BRENDA team
Gopinath, G.; Sankeshi, V.; Perugu, S.; Alaparthi, M.D.; Bandaru, S.; Pasala, V.K.; Chittineni, P.R.; Krupadanam, G.L.; Sagurthi, S.R.
Design and synthesis of chiral 2H-chromene-N-imidazolo-amino acid conjugates as aldose reductase inhibitors
Eur. J. Med. Chem.
124
750-762
2016
Homo sapiens (P15121)
Manually annotated by BRENDA team
Yadav, U.C.; Ramana, K.V.; Srivastava, S.K.
Aldose reductase regulates acrolein-induced cytotoxicity in human small airway epithelial cells
Free Radic. Biol. Med.
65
15-25
2013
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Baba, S.P.; Hoetker, J.D.; Merchant, M.; Klein, J.B.; Cai, J.; Barski, O.A.; Conklin, D.J.; Bhatnagar, A.
Role of aldose reductase in the metabolism and detoxification of carnosine-acrolein conjugates
J. Biol. Chem.
288
28163-28179
2013
Homo sapiens (P15121), Homo sapiens, Mus musculus (P45376), Mus musculus
Manually annotated by BRENDA team
Li, L.; Chang, K.C.; Zhou, Y.; Shieh, B.; Ponder, J.; Abraham, A.D.; Ali, H.; Snow, A.; Petrash, J.M.; LaBarbera, D.V.
Design of an amide N-glycoside derivative of beta-glucogallin: a stable, potent, and specific inhibitor of aldose reductase
J. Med. Chem.
57
71-77
2014
Homo sapiens (P15121), Mus musculus (P45376)
Manually annotated by BRENDA team
Stefek, M.; Soltesova Prnova, M.; Majekova, M.; Rechlin, C.; Heine, A.; Klebe, G.
Identification of novel aldose reductase inhibitors based on carboxymethylated mercaptotriazinoindole scaffold
J. Med. Chem.
58
2649-2657
2015
Homo sapiens (P15121)
Manually annotated by BRENDA team
Rechlin, C.; Scheer, F.; Terwesten, F.; Wulsdorf, T.; Pol, E.; Fridh, V.; Toth, P.; Diederich, W.E.; Heine, A.; Klebe, G.
Price for opening the transient specificity pocket in human aldose reductase upon ligand binding structural, thermodynamic, kinetic, and computational analysis
ACS Chem. Biol.
12
1397-1415
2017
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Rivelli, J.F.; Ochoa, A.L.; Santander, V.S.; Nigra, A.; Previtali, G.; Casale, C.H.
Regulation of aldose reductase activity by tubulin and phenolic acid derivates
Arch. Biochem. Biophys.
654
19-26
2018
Homo sapiens (P15121)
Manually annotated by BRENDA team
Salem, M.G.; Abdel Aziz, Y.M.; Elewa, M.; Elshihawy, H.A.; Said, M.M.
Molecular modelling and synthesis of spiroimidazolidine-2,4-diones with dual activities as hypoglycemic agents and selective inhibitors of aldose reductase
Bioorg. Chem.
79
131-144
2018
Homo sapiens (P15121)
Manually annotated by BRENDA team
Chen, H.; Zhang, X.; Zhang, X.; Fan, Z.; Liu, W.; Lei, Y.; Zhu, C.; Ma, B.
Dihydrobenzoxazinone derivatives as aldose reductase inhibitors with antioxidant activity
Bioorg. Med. Chem.
28
115699
2020
Homo sapiens (P15121)
Manually annotated by BRENDA team
Hao, X.; Han, Z.; Li, Y.; Li, C.; Wang, X.; Zhang, X.; Yang, Q.; Ma, B.; Zhu, C.
Synthesis and structure-activity relationship studies of phenolic hydroxyl derivatives based on quinoxalinone as aldose reductase inhibitors with antioxidant activity
Bioorg. Med. Chem. Lett.
27
887-892
2017
Homo sapiens (P15121)
Manually annotated by BRENDA team
Cui, F.; Liu, L.; Tang, H.; Yang, K.; Li, Y.
Construction of explicit models to correlate the structure and the inhibitory activity of aldose reductase Flavonoids and sulfonyl-pyridazinones as inhibitors
Chem. Biol. Drug Des.
89
482-491
2017
Homo sapiens (P15121)
Manually annotated by BRENDA team
Papastavrou, N.; Chatzopoulou, M.; Ballekova, J.; Cappiello, M.; Moschini, R.; Balestri, F.; Patsilinakos, A.; Ragno, R.; Stefek, M.; Nicolaou, I.
Enhancing activity and selectivity in a series of pyrrol-1-yl-1-hydroxypyrazole-based aldose reductase inhibitors The case of trifluoroacetylation
Eur. J. Med. Chem.
130
328-335
2017
Rattus norvegicus, Homo sapiens (P15121)
Manually annotated by BRENDA team
Crespo, I.; Gimenez-Dejoz, J.; Porte, S.; Cousido-Siah, A.; Mitschler, A.; Podjarny, A.; Pratsinis, H.; Kletsas, D.; Pares, X.; Ruiz, F.X.; Metwally, K.; Farres, J.
Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase
Eur. J. Med. Chem.
152
160-174
2018
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team
Khan, M.S.; Qais, F.A.; Rehman, M.T.; Ismail, M.H.; Alokail, M.S.; Altwaijry, N.; Alafaleq, N.O.; AlAjmi, M.F.; Salem, N.; Alqhatani, R.
Mechanistic inhibition of non-enzymatic glycation and aldose reductase activity by naringenin Binding, enzyme kinetics and molecular docking analysis
Int. J. Biol. Macromol.
159
87-97
2020
Homo sapiens (P15121)
Manually annotated by BRENDA team
Sekhon, G.; Singh, B.; Singh, R.
Role of Cys-298 in specific recognition of glutathione by aldose reductase
J. Biomol. Struct. Dyn.
FEHLT
1-9
2021
Homo sapiens
Manually annotated by BRENDA team
Hao, X.; Qi, G.; Ma, H.; Zhu, C.; Han, Z.
Novel 2-phenoxypyrido[3,2-b]pyrazin-3(4H)-one derivatives as potent and selective aldose reductase inhibitors with antioxidant activity
J. Enzyme Inhib. Med. Chem.
34
1368-1372
2019
Homo sapiens (P15121)
Manually annotated by BRENDA team
D'Andrea, F.; Sartini, S.; Piano, I.; Franceschi, M.; Quattrini, L.; Guazzelli, L.; Ciccone, L.; Orlandini, E.; Gargini, C.; La Motta, C.; Nencetti, S.
Oxy-imino saccharidic derivatives as a new structural class of aldose reductase inhibitors endowed with anti-oxidant activity
J. Enzyme Inhib. Med. Chem.
35
1194-1205
2020
Homo sapiens (P15121), Homo sapiens
Manually annotated by BRENDA team