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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Rattus norvegicus and UniProt Accession P51635

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EC Tree
IUBMB Comments
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P51635
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome c reductase, aldo-keto reductase, liver alcohol dehydrogenase, adh-1, adh-2, short-chain alcohol dehydrogenase, lbadh, cbadh, nadph-dependent aldehyde reductase, tsadh319, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alcohol dehydrogenase [NADP(+)]
UniProt
aldehyde reductase
-
aldose reductase
-
3-DG-reducing enzyme
-
-
-
-
ADH
-
-
-
-
Alcohol dehydrogenase [NADP+]
-
-
-
-
aldehyde reductase
aldehyde reductase (NADPH2)
-
-
-
-
Aldo-keto reductase family 1 member A1
-
-
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
daunorubicin reductase
-
-
hexogenate dehydrogenase
-
-
high-Km aldehyde reductase
-
-
-
-
low-Km aldehyde reductase
-
-
-
-
mevaldate reductase
-
-
NADP-alcohol dehydrogenase
-
-
-
-
NADP-aldehyde reductase
-
-
-
-
NADP-dependent aldehyde reductase
-
-
-
-
NADPH-aldehyde reductase
-
-
-
-
NADPH-cytochrome c reductase
-
-
NADPH-dependent aldehyde reductase
-
-
-
-
nonspecific succinic semialdehyde reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:NADP+ oxidoreductase
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-12-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose + NADPH + H+
sorbitol + NADP+
show the reaction diagram
-
-
-
?
D-glucuronate + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
r
DL-glyceraldehyde + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NADPH
? + NADP+
show the reaction diagram
-
low Km reductase
-
-
r
3-pyridinecarboxaldehyde + NADPH
3-pyridinemethanol + NADP+
show the reaction diagram
-
-
-
-
r
4-nitroacetophenone + NADPH + H+
1-(4-nitrophenyl)ethanol + NADP+
show the reaction diagram
-
-
-
-
r
4-pyridinecarboxaldehyde + NADPH
4-pyridinemethanol + NADP+
show the reaction diagram
-
-
-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
-
-
-
-
?
benzalacetone + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NADPH
benzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
r
chloral hydrate + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
show the reaction diagram
D-glucuronate + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
r
D-glucuronolactone + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
D-xylose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
daunorubicin + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
ethylacetoacetate + NADPH
ethyl L-(+)-3-hydroxybutyrate + NADP+
show the reaction diagram
-
-
-
-
?
glycerol + NADP+
DL-glyceraldehyde + NADPH + H+
show the reaction diagram
L-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
L-gulonic acid + NADP+
D-glucuronic acid + NADPH
show the reaction diagram
-
-
-
-
r
L-gulonic acid + NADPH
D-glucuronic acid + NADP+
show the reaction diagram
-
-
-
-
r
methylglyoxal + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
r
n-decanal + NADPH + H+
n-decanol + NADP+
show the reaction diagram
-
-
-
-
r
n-dodecanal + NADPH + H+
n-dodecanol + NADP+
show the reaction diagram
-
-
-
-
r
n-hexadecanal + NADPH + H+
n-hexadecanol + NADP+
show the reaction diagram
-
-
-
-
r
n-octadecanal + NADPH + H+
n-octadecanol + NADP+
show the reaction diagram
-
-
-
-
r
n-octanal + NADPH + H+
n-octanol + NADP+
show the reaction diagram
n-tetradecanal + NADPH + H+
n-tetradecanol + NADP+
show the reaction diagram
-
-
-
-
r
p-carboxybenzaldehyde + NADPH
p-carboxybenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
r
p-hydroxyphenylacetaldehyde + NADPH + H+
p-hydroxyphenylethanol + NADP+
show the reaction diagram
-
-
-
-
r
p-hydroxyphenylglycolaldehyde + NADPH
4-hydroxyphenylethylalcohol + NADP+
show the reaction diagram
-
-
-
-
r
p-nitrobenzaldehyde + NADPH
p-nitrobenzylalcohol + NADP+
show the reaction diagram
propionaldehyde + NADPH
propanol + NADP+
show the reaction diagram
-
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose + NADPH + H+
sorbitol + NADP+
show the reaction diagram
-
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
show the reaction diagram
-
-
-
-
r
D-glucuronate + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
ethylacetoacetate + NADPH
ethyl L-(+)-3-hydroxybutyrate + NADP+
show the reaction diagram
-
-
-
-
?
L-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
L-gulonic acid + NADP+
D-glucuronic acid + NADPH
show the reaction diagram
-
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3-benzyl-2-oxoquinoxalin-1(2H)-yl)acetic acid
32.8% inhibition at 0.010 mM
1-(4-nitrobenzyl)-3-(4-(2-morpholinoethyl) piperazin-1-yl)quinoxalin-2(1H)-one
23% inhibition
1-(4-nitrobenzyl)-3-(4-(3-(trifluoromethyl) phenyl)piperazin-1-yl) quinoxalin-2(1H)-one
43% inhibition
1-(4-nitrobenzyl)-3-(4-(4-methoxyphenyl) piperazin-1-yl)quinoxalin-2(1H)-one
26% inhibition
1-(4-nitrobenzyl)-3-(4-(pyrazin-2-yl) piperazin-1-yl)quinoxalin-2(1H)-one
24% inhibition
1-(4-nitrobenzyl)-3-styrylquinoxalin-2(1H)-one
30% inhibition
2-(2-oxo-3-phenethylquinoxalin-1(2H)-yl) acetic acid
-
2-(2-oxo-3-styrylquinoxalin-1(2H)-yl) acetic acid
-
2-(3,7-bis(4-fluorophenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
41.0% inhibition at 0.010 mM
2-(3-(2,4-difluorophenylamino)-6-nitro-2-oxoquinoxalin-1(2H)-yl) acetic acid
-
2-(3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
36.6% inhibition at 0.010 mM
2-(3-(3-(tert-butylamino)-3-oxoprop-1-en-1-yl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
-
2-(3-(3-indolyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
32.3% inhibition at 0.010 mM
2-(3-(4-(4-methoxyphenyl) piperazin-1-yl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
-
2-(3-(4-bromothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)acetic acid
12.8% inhibition at 0.010 mM
2-(3-(4-chlorothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)acetic acid
42.4% inhibition at 0.010 mM
2-(3-(4-fluorophenethyl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
-
2-(3-(4-fluorophenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
31.8% inhibition at 0.010 mM
2-(3-(4-fluorostyryl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
-
2-(3-(4-fluorostyryl)-6-nitro-2-oxoquinoxalin-1(2H)-yl)acetic acid
-
2-(3-(4-hydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
34.6% inhibition at 0.010 mM
2-(3-phenoxy-2-oxoquinoxalin-1(2H)-yl)acetic acid
6.6% inhibition at 0.010 mM
2-(3-phenyl-2-oxoquinoxalin-1(2H)-yl)acetic acid
25.4% inhibition at 0.010 mM
2-(3-thiophenoxy-2-oxoquinoxalin-1(2H)-yl)acetic acid
32.2% inhibition at 0.010 mM
2-(6-bromo-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
38.1% inhibition at 0.010 mM
2-(6-bromo-3-(4-bromothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
8.7% inhibition at 0.010 mM
2-(6-chloro-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
46.5% inhibition at 0.010 mM
2-(6-chloro-3-(4-fluorostyryl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
-
2-(6-fluoro-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
42.5% inhibition at 0.010 mM
2-(7-(4-fluorobenzyl)-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
11.6% inhibition at 0.010 mM
2-(7-bromo-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
35.9% inhibition at 0.010 mM
2-(7-bromo-3-(3-indolyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
17.5% inhibition at 0.010 mM
2-(7-bromo-3-(4-bromothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
24.0% inhibition at 0.010 mM
2-(7-bromo-3-(4-chlorothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
10.2% inhibition at 0.010 mM
2-(7-chloro-2-oxo-3-styrylquinoxalin-1(2H)-yl) acetic acid
-
2-(7-chloro-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
44.5% inhibition at 0.010 mM
2-(7-chloro-3-(2-benzothiophene)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
53.3% inhibition at 0.010 mM
2-(7-chloro-3-(4-bromothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
14.1% inhibition at 0.010 mM
2-(7-chloro-3-(4-chlorothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
17.3% inhibition at 0.010 mM
2-(7-chloro-3-(4-fluorophenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
23.6% inhibition at 0.010 mM
2-(7-fluoro-3-(2,4-dihydroxyphenyl)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
46.2% inhibition at 0.010 mM
2-(7-fluoro-3-(4-bromothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
45.5% inhibition at 0.010 mM
2-(7-fluoro-3-(4-chlorothiophenoxy)-2-oxoquinoxalin-1(2H)-yl)-acetic acid
29.5% inhibition at 0.010 mM
2-(7-fluoro-3-(4-fluorophenyl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
35.8% inhibition at 0.010 mM
3-(4-fluorostyryl)-1-(4-nitrobenzyl) quinoxalin-2(1H)-one
24% inhibition
3-(benzo[b] thiophen-3-yl)-1-(4-nitrobenzyl)quinoxalin-2(1H)-one
32% inhibition
epalrestat
73.6% inhibition at 0.010 mM
N-(tert-butyl)-3-(4-(4-nitrobenzyl)-3-oxo-3, 4-dihydroquinoxalin-2-yl) acryl amide
36% inhibition
[2-oxo-3-(2-phenylethyl)quinoxalin-1(2H)-yl]acetic acid
22.0% inhibition at 0.010 mM
[2-oxo-3-[(Z)-2-phenylethenyl]quinoxalin-1(2H)-yl]acetic acid
32.0% inhibition at 0.010 mM
[3-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
32.6% inhibition at 0.010 mM
[3-[(E)-2-(4-hydroxyphenyl)ethenyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
42.4% inhibition at 0.010 mM
[3-[(E)-2-(4-methoxyphenyl)ethenyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
21.8% inhibition at 0.010 mM
[3-[2-(4-hydroxyphenyl)ethyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
12.2% inhibition at 0.010 mM
[7-fluoro-3-[(E)-2-(4-hydroxyphenyl)ethenyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
36.2% inhibition at 0.010 mM
[7-fluoro-3-[2-(4-hydroxyphenyl)ethyl]-2-oxoquinoxalin-1(2H)-yl]acetic acid
23.0% inhibition at 0.010 mM
(1H-indol-1-yl)acetic acid
-
(2,3-dihydrocyclopenta[b]indol-4(1H)-yl)acetic acid
-
(3-sulfanyl-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
(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-oxo-3,4-dihydro-5H-pyridazino[4,5-b]indol-5-yl)acetic acid
-
(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
-
(8-methyl-3-[[2-oxo-2-(propylamino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
-
2',5'-ADP
-
-
2,4-dimethylglutaric acid
-
-
2,5-dihydro-3H-[1,2,4]triazino[5,6-b]indole-3-thione
-
3,3'-tetramethylenglutaric acid
-
-
3,3-dimethylglutaric acid
-
-
3-(1H-indol-1-yl)propanoic acid
-
3-[3-[(diethylamino)methyl]-1H-indol-1-yl]propanoic acid
-
Alrestatin
Blue dextran
-
-
-
chlorpromazine
-
-
Cibacron blue F3GA
-
-
epalrestat
-
-
lidorestat
binding mode, overview
ONO-2235
-
-
Procion Reed HE3B
-
-
quercetin
-
-
[(5H-[1,2,4]triazino[5,6-b]indol-3-yl)sulfanyl]acetic acid
-
[3-(2,2-dimethylpropanoyl)-1H-indol-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-[(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
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine
-
-
Trifluperazine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
4-Nitroacetophenone
-
-
1.2
4-Pyridinecarboxaldehyde
-
enzyme from kidney, brain or liver
3.8
acetaldehyde
-
-
2.5
Benzalacetone
-
-
4.5
benzaldehyde
-
-
29
Chloral hydrate
-
-
2.2 - 43
D-glucuronate
670 - 2080
D-xylose
1.3 - 8.35
DL-glyceraldehyde
24 - 25
ethyl acetoacetate
0.03
hexadecanal
-
-
0.07
n-decanal
-
-
0.019 - 0.02
n-dodecanal
0.008
n-hexadecanal
-
-
0.004
n-octadecanal
-
-
0.77
n-octanal
-
-
0.014
n-tetradecanal
-
-
0.003 - 0.006
NADPH
0.21
octanal
-
-
0.031
p-Carboxybenzaldehyde
-
-
0.91
p-hydroxyphenylacetaldehyde
-
-
0.059
p-hydroxyphenylglycolaldehyde
-
-
0.0026 - 0.31
p-nitrobenzaldehyde
3.3
propionaldehyde
-
-
0.26
pyridine 3-aldehyde
-
-
0.13 - 10.9
Succinic semialdehyde
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000143
2-(2-oxo-3-phenethylquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00082
2-(2-oxo-3-styrylquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.000283
2-(3-(2,4-difluorophenylamino)-6-nitro-2-oxoquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00186
2-(3-(3-(tert-butylamino)-3-oxoprop-1-en-1-yl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00753
2-(3-(4-(4-methoxyphenyl) piperazin-1-yl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00114
2-(3-(4-fluorophenethyl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00143
2-(3-(4-fluorostyryl)-2-oxoquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.000362
2-(3-(4-fluorostyryl)-6-nitro-2-oxoquinoxalin-1(2H)-yl)acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00066
2-(6-chloro-3-(4-fluorostyryl)-2-oxoquinoxalin-1(2H)-yl)acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.00388
2-(7-chloro-2-oxo-3-styrylquinoxalin-1(2H)-yl) acetic acid
Rattus norvegicus
pH 7.2, 37°C, ALR1
0.0802
(1H-indol-1-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0048
(2,3-dihydrocyclopenta[b]indol-4(1H)-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0406
(3-sulfanyl-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0012
(3-[[(2-fluorophenyl)methyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0235
(3-[[2-oxo-2-(2,4,6-trimethylanilino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.049
(4-oxo-3,4-dihydro-5H-pyridazino[4,5-b]indol-5-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0248
(6H-indolo[2,3-b]quinoxalin-6-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0151
(7H-indolo[2',3':5,6][1,2,4]triazino[2,3-a]benzimidazol-7-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0196
(8-methyl-3-[[2-oxo-2-(propylamino)ethyl]sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl)acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0118
3-(1H-indol-1-yl)propanoic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0067
3-[3-[(diethylamino)methyl]-1H-indol-1-yl]propanoic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0684
[3-(2,2-dimethylpropanoyl)-1H-indol-1-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0381
[3-[(diethylamino)methyl]-1H-indol-1-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0223
[3-[(dimethylamino)methyl]-2-methyl-1H-indol-1-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0325
[3-[(morpholin-4-yl)methyl]-1H-indol-1-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0141
[3-[(propan-2-yl)sulfanyl]-5H-[1,2,4]triazino[5,6-b]indol-5-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0192
[3-[(pyrrolidin-1-yl)methyl]-1H-indol-1-yl]acetic acid
Rattus norvegicus
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
211
-
hexadecanal as substrate
5.9
-
liver enzyme
6
-
brain enzyme
9.59
-
high-Km aldehyde reductase from brain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
ALR2 is the first rate-determining enzyme in the polyol pathway and catalyzes the reduction of glucose to sorbitol in the presence of NADPH as a cofactor. Sorbitol is in turn converted into fructose with accompanied reduction of NAD+ by sorbitol dehydrogenase. Under normal circumstances, glucose is predominantly converted to glucose-6-phosphate by hexokinase and then enters the glycolytic pathway, whereas only a small amount of glucose is metabolized through the polyol pathway due to a relatively low affinity of ALR2 for this substrate. During hyperglycemia, the polyol metabolic pathway is activated and the increased flux of glucose through the polyol pathway triggers the accumulation of sorbitol, which mainly happens in tissues demonstrating insulin-independent uptake of glucose, such as lens, kidney, retina, and peripheral nerves
physiological function
ALR1 is present in all tissues and plays an important role in detoxification
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AK1A1_RAT
325
0
36506
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000 - 40000
-
-
32000
33000
34000
-
1 * 34000, SDS-PAGE
37000
-
1 * 37000, SDS-PAGE
38800
-
gel filtration
41000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
-
286175
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
-
at 40°C for 10 min enzyme retains about 90% of its activity towards D-glucuronate, after 10 min at 50% activity decreases to less than 5%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C when stored frozen there is negligible loss of activity after 6 months, but repeated freezing and thawing results in loss of activity
-
4°C loses activity only slowly over several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme partially from lens and kidney
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tabakoff, B.; Erwin, G.
Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain
J. Biol. Chem.
245
3263-3268
1970
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Bosron, W.F.; Prairie, R.L.
Triphosphopyridine nucleotide-linked aldehyde reductase I. Purification and properties of the enzyme from pig kidney cortex
J. Biol. Chem.
217
4480-4485
1972
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Turner, A.J.; Tipton, K.F.
The characterization of two reduced nicotinamide-adenine dinucleotide phosphate-linked aldehyde reductases from pig brain
Biochem. J.
130
765-772
1972
Bos taurus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Davidson, W.S.; Weihrauch, L.; Flynn, T.G.
Purification and compositional relatedness of aldehyde reductase from several species
Biochem. Soc. Trans.
576
940-943
1978
Saccharomyces cerevisiae, Drosophila melanogaster, Gallus sp., Homo sapiens, Pecten maximus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Branlant, G.M; Biellmann, J.F.
Purification and some properties of aldehyde reductases from pig liver
Eur. J. Biochem.
105
611-621
1980
Equus sp., Ovis aries, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Morpeth, F.F.; Dickinson, F.M.
Some properties of pig kidney-cortex aldehyde reductase
Biochem. J.
191
619-626
1980
Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Turner, A.J.; Hryszko, J.
Isolation and characterization of rat liver aldehyde reductase
Biochim. Biophys. Acta
613
256-265
1980
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Rivett, A.J.; Smith, I.L.; Tipton, K.F.
Purification of the high-Km aldehyde reductase from rat brain and liver and from ox brain
Biochem. J.
197
473-481
1981
Bos taurus, Cricetinae, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sawada, H.; Hara, A.; Nakayama, T.; Hayashibara, M.
Kinetic mechanisms in the reduction of aldehydes and ketones catalyzed by rabbit liver aldehyde reductases and hydroxysteroid dehydrogenases
J. Biochem.
92
185-191
1982
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Flynn, T.G.
Aldehyde reductases: Monomeric NADPH-dependent oxidoreductases with multifunctional potential
Biochem. Pharmacol.
31
2705-2712
1982
Saccharomyces cerevisiae, Cavia porcellus, Oryctolagus cuniculus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Petrash, J.M.; Srivastava, S.K.
Purification and properties of human liver aldehyde reductases
Biochim. Biophys. Acta
707
105-114
1982
Bos taurus, Gallus sp., Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Markus, H.B.; Raducha, M.; Harris, H.
Tissue distribution of mammalian aldose reductase and related enzymes
Biochem. Med.
29
31-45
1983
Canis lupus familiaris, Cavia porcellus, Cavia porcellus Hartley, Felis sp., Gallus sp., Homo sapiens, Mus musculus, Mus musculus B10.A, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus, Saimiri, Sus scrofa
Manually annotated by BRENDA team
Takahashi, N.; Saito, T.; Tomita, K.
Purification and properties of an NADPH-linked aldehyde reductase from rat kidney
Biochim. Biophys. Acta
748
444-452
1983
Bos taurus, Cavia porcellus, Rattus norvegicus
Manually annotated by BRENDA team
Hara, A.; Deyashiki, Y.; Nakayama, T.; Sawada, H.
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
Eur. J. Biochem.
133
207-214
1983
Bos taurus, Gallus sp., Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
De Jongh, K.S.; Schofield, P.J.; Edwards, M.R.
Kinetic mechanism of sheep liver NADPH-dependent aldehyde reductase
Biochem. J.
242
143-150
1987
Bos taurus, Ovis aries, Rattus norvegicus
Manually annotated by BRENDA team
Kawasaki, N.; Tanimoto, T.; Tanaka, A.
Characterization of aldose reductase and aldehyde reductase from rat testis
Biochim. Biophys. Acta
996
30-36
1989
Rattus norvegicus
Manually annotated by BRENDA team
Ohta, M.; Tanimoto, T.; Tanaka, A.
Localization, isolation and properties of three NADPH-dependent aldehyde reducing enzymes from dog kidney
Biochim. Biophys. Acta
1078
395-403
1991
Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Udovikova, E.A.; Wojtczak, L.
Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex
Int. J. Biochem. Cell Biol.
30
597-608
1998
Rattus norvegicus
Manually annotated by BRENDA team
Reyes, E.; Erwin, V.
Distribution and properties of NADPH-linked aldehyde reductases from rat brain synaptosomes
Neurochem. Res.
2
87-97
1977
Rattus norvegicus
Manually annotated by BRENDA team
Cash, C.; Maitre, M.; Mandel, P.
Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate
J. Neurochem.
33
1169-1175
1979
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Takahashi, N.; Saito, T.; Goda, Y.; Tomita, K.
Characterization of microsomal NADPH-dependent aldehyde reductase from rat brain
J. Biochem.
99
513-519
1986
Rattus norvegicus
Manually annotated by BRENDA team
Hussain, S.; Parveen, S.; Hao, X.; Zhang, S.; Wang, W.; Qin, X.; Yang, Y.; Chen, X.; Zhu, S.; Zhu, C.; Ma, B.
Structure-activity relationships studies of quinoxalinone derivatives as aldose reductase inhibitors
Eur. J. Med. Chem.
80
383-392
2014
Rattus norvegicus (P51635), Rattus norvegicus Wistar (P51635)
Manually annotated by BRENDA team
Qin, X.; Hao, X.; Han, H.; Zhu, S.; Yang, Y.; Wu, B.; Hussain, S.; Parveen, S.; Jing, C.; Ma, B.; Zhu, C.
Design and synthesis of potent and multifunctional aldose reductase inhibitors based on quinoxalinones
J. Med. Chem.
58
1254-1267
2015
Rattus norvegicus (P51635), Rattus norvegicus Wistar (P51635)
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
Rattus norvegicus (P07943), Rattus norvegicus Wistar (P07943)
Manually annotated by BRENDA team