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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Homo sapiens

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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:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome c reductase, aldo-keto reductase, liver alcohol dehydrogenase, adh-1, adh-2, short-chain alcohol dehydrogenase, lbadh, nadph-dependent aldehyde reductase, cbadh, tsadh319, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-DG-reducing enzyme
-
-
-
-
ADH
-
-
-
-
Alcohol dehydrogenase [NADP+]
-
-
-
-
aldehyde reductase
-
-
-
-
aldehyde reductase (NADPH2)
-
-
-
-
aldo-keto reductase
-
-
Aldo-keto reductase family 1 member A1
-
-
-
-
ALDR
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
high-Km aldehyde reductase
-
-
-
-
L-hexonate dehydrogenase
-
-
low-Km aldehyde reductase
-
-
-
-
NADP-alcohol dehydrogenase
-
-
-
-
NADP-aldehyde reductase
-
-
-
-
NADP-dependent aldehyde reductase
-
-
-
-
NADPH-aldehyde reductase
-
-
-
-
NADPH-dependent aldehyde reductase
-
-
-
-
nonspecific succinic semialdehyde reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
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
(+)-camphorquinone + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
3-deoxyglucosone + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
r
3-pyridinecarboxaldehyde + NADPH
3-pyridinemethanol + NADP+
show the reaction diagram
-
-
-
-
r
4-hydroxy-3-methoxybenzyl alcohol + NADP+
4-hydroxy-3-methoxybenzaldehyde + NADPH
show the reaction diagram
-
-
-
-
r
4-hydroxybutyrate + NADP+
4-ketobutyrate + NADPH
show the reaction diagram
-
-
-
-
r
benzaldehyde + NADPH
benzyl alcohol + NADP+
show the reaction diagram
camphorquinone + NADPH + H+
1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
show the reaction diagram
-
-
-
-
?
D-galactose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-glucose + NADPH
? + NADP+
show the reaction diagram
-
placenta aldehyde reductase I
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
show the reaction diagram
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
D-lactaldehyde + NADPH + H+
propane-1,2-diol + NADP+
show the reaction diagram
-
-
-
-
r
D-xylose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
daunorubicin + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
iodohexadecanal + NADPH
iodohexadecanol + NADP+
show the reaction diagram
-
-
-
-
r
L-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
m-nitrobenzaldehyde + NADPH
m-nitrobenzylalcohol + NADP+
show the reaction diagram
-
-
-
-
r
methylglyoxal + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
r
mevaldate + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
n-butyraldehyde + NADPH
n-butanol + NADP+
show the reaction diagram
-
-
-
-
r
p-carboxybenzaldehyde + NADPH
p-carboxybenzyl alcohol + NADP+
show the reaction diagram
p-chlorobenzaldehyde + NADPH + H+
p-chlorobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
r
p-nitrobenzaldehyde + NADPH
p-nitrobenzylalcohol + NADP+
show the reaction diagram
phenylethanediol + NADP+
?
show the reaction diagram
-
-
-
-
r
phenylethanol + NADP+
phenylacetaldehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
propane-1,2-diol + NADP+
lactaldehyde + NADPH
show the reaction diagram
-
-
-
-
r
propionaldehyde + NADPH
propanol + NADP+
show the reaction diagram
sodium D-glucuronate + NADPH + H+
sodium L-gulonate + 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-glucuronate + NADPH
L-gulonate + NADP+
show the reaction diagram
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
L-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide phosphate
-
-
NADH
-
aldehyde reductase I
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
100 mM, aldehyde reductase II slightly stimulated
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
-
2,3-dimethylsuccinic acid
-
-
3,3'-tetramethylenglutaric acid
AL1576
Alrestatin
Amaranth
-
-
arachidonic acid
-
-
ATP-ribose
-
competitive inhibition
benzodiazepine
-
-
carbamazepine
-
-
Chromone
-
-
diethyldicarbonate
-
kidney aldehyde reductase
Diphenic acid
-
-
Ethacrynic acid
-
-
ethylphenylhydantoin
-
-
FK366
haematin
-
-
indigo carmine
-
-
Indocyanine green
-
-
Li2SO4
N-ethylmaleimide
-
-
NaCl
-
aldehyde reductase I and II
NADP+
-
competitive inhibition
p-hydroxymercuribenzoate
-
-
p-mercuribenzoate
phenacemide
-
-
Phenobarbital
-
-
phenolsulfophthalein
-
-
ponalrestat
quercetrin
-
-
Rose bengal
-
-
sodium phenobarbital
sodium valproate
-
-
sorbinil
Sulfobromophthalein
-
-
Tolrestat
zopolrestat
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 8.61
3-Pyridinecarboxaldehyde
0.023 - 9.09
benzaldehyde
0.083 - 7.69
Butyraldehyde
1.4
Camphorquinone
-
-
543
D-galactose
-
aldehyde reductase II
215
D-glucose
-
AR I
4.2 - 364
D-glucuronate
500
D-xylose
-
aldehyde reductase II
1.5 - 76
DL-glyceraldehyde
2.5 - 2.53
glucuronate
0.07 - 7.59
glyceraldehyde
2.4
m-nitrobenzaldehyde
-
-
1.3
methylglyoxal
-
-
0.013 - 0.05
NADPH
0.025 - 4
p-Carboxybenzaldehyde
0.94
p-chlorobenzaldehyde
-
-
0.029 - 5.9
p-nitrobenzaldehyde
0.008 - 14.54
propionaldehyde
2.95
sodium D-glucuronate
0.17 - 18
Succinic semialdehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.148
4-Hydroxy-3-methoxybenzyl alcohol
-
-
0.0733
benzylalcohol
-
-
0.0283
glycerol
-
-
9.5
p-nitrobenzaldehyde
-
-
0.08
phenylethanediol
-
-
0.0283
Phenylethanol
-
-
0.0433
Propane-1,2-diol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.3
-
pure aldehyde reductase
15.7
-
-
29.62
-
aldehyde reductase II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
reduction of p-nitrobenzaldehyde in presence of NADPH
6.7 - 6.8
-
aldehyde reductase II
7
-
aldehyde reductase II
9 - 9.5
-
oxidation of benzyl alcohol in presence of NADP+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
aldehyde reductase II
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AK1A1_HUMAN
325
0
36573
Swiss-Prot
other Location (Reliability: 3)
V9HWI0_HUMAN
325
0
36573
TrEMBL
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
32000
32500
32700
-
aldehyde reductase II, gel filtration
33000
-
1 * 33000, aldehyde reductase II, SDS-PAGE
33600
-
sedimentation analysis
35000
36200
-
gel filtration
36300
-
ultracentrifugation
38000
-
SDS-PAGE
39000
-
1 * 32500 + 1 * 39000
39400
-
1 * 39400, SDS-PAGE
44000
-
gel filtration
45000
-
-
72000
-
gel filtration
74000
-
aldehyde reductase I, gel filtration
90000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
presence of NADPH or NADP+ prevents loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, freezing of the purified enzymes results in almost complete loss of activity, purified aldehyde reductase II is stable in 10 mM sodium phosphate buffer, pH 7, for 2-3 month, but appears to lose activity rapidly thereafter, purified aldehyde reductase I retains enzyme activity in the same buffer for about 3 months, after which enzyme activity declines
-
4°C stable for several months but loss of activity with a concomitant enzyme precipitation occurs upon freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aldehyde reductase I and II
-
aldehyde reductase II
-
wild-type aldehyde reductase and mutant A H112Q
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhatnagar, A.; Das, B.; Liu, S.Q.; Srivastava, S.K.
Human liver aldehyde reductase: pH dependence of steady-state kinetic parameters
Arch. Biochem. Biophys.
287
329-336
1991
Homo sapiens
Manually annotated by BRENDA team
Shinoda, M.; Mori, S.; Shintani, S.; Ishikura, S.; Hara, A.
Inhibition of human aldehyde reductase by drugs for testing the function of liver and kidney
Biol. Pharm. Bull.
22
741-744
1999
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Wermuth, B.; Muench, J.D.B.; von Wartburg, J.P.
Purification and properties of NADPH-dependent aldehyde reductase from human liver
J. Biol. Chem.
252
3821-3828
1977
Equus sp., Homo sapiens, Pecten maximus, 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
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
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
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
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
Das, B.; Srivastava, S.K.
Purification and properties of aldehyde reductases from human placenta
Biochim. Biophys. Acta
840
324-333
1985
Cavia porcellus, Homo sapiens
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
Barski, O.A.; Gabbay, K.H.; Grimshaw, C.E.; Bohren, K.M.
Mechanism of human aldehyde reductase: characterization of the active site pocket
Biochemistry
34
11264-11275
1995
Homo sapiens
Manually annotated by BRENDA team
Barski, O.A.; Gabbay, K.H.; Bohren, K.M.
The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity
Biochemistry
35
14276-14280
1996
Homo sapiens (P14550)
Manually annotated by BRENDA team
Bogin, O.; Peretz, M.; Burstein, Y.
Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids
Protein Sci.
6
450-458
1997
Saccharomyces cerevisiae, Thermoanaerobacter brockii, Equus sp., Homo sapiens
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
Lo, H.S.; Chang, C.J.
Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica
J. Parasitol.
68
372-377
1982
Entamoeba histolytica, Homo sapiens
Manually annotated by BRENDA team
Das, B.; Song, H.P.; Ansari, N.H.; Hair, G.A.; Srivastava, S.K.
Purification and properties of aldose reductase and aldehyde reductase II from human lens
Lens Res.
4
309-335
1987
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