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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Mus musculus and UniProt Accession Q9JII6

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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:
Mus musculus
UNIPROT: Q9JII6
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The taxonomic range for the selected organisms is: Mus musculus
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
-
-
-
-
AKR1A4
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-
Alcohol dehydrogenase [NADP+]
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-
-
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aldehyde reductase
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-
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aldehyde reductase (NADPH2)
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-
-
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Aldo-keto reductase family 1 member A1
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-
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
high-Km aldehyde reductase
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-
-
-
L-hexonate dehydrogenase
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-
low-Km aldehyde reductase
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-
-
-
NADP-alcohol dehydrogenase
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-
-
-
NADP-aldehyde reductase
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-
-
-
NADP-dependent aldehyde reductase
-
-
-
-
NADPH-aldehyde reductase
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-
-
-
NADPH-dependent aldehyde reductase
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-
-
-
nonspecific succinic semialdehyde reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
-
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-glucuronate + NADPH
?
show the reaction diagram
0.1 M phosphat buffer, pH 7.0
-
-
?
D-glucuronate + NADPH + H+
?
show the reaction diagram
0.1 M phosphate buffer, pH 7.0
-
-
?
glucuronate + NADPH
?
show the reaction diagram
-
-
-
?
glucuronate + NADPH + H+
?
show the reaction diagram
-
-
-
?
(2E,4E)-hexa-2,4-dienal + NAD(P)H + H+
(2E,4E)-6-hydroxyhexa-2,4-dienal + NAD(P)+
show the reaction diagram
-
-
-
-
?
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
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
glucuronate + NADPH
?
show the reaction diagram
-
-
-
?
glucuronate + NADPH + H+
?
show the reaction diagram
-
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
L-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AL-1576
pyrazole
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
(2E,4E)-hexa-2,4-dienal
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pH 7.4, 25°C, with NAD(P)H
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
AL-1576
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
fetal kidney, 10fold higher enzymatic activity observed compared with other tissues
Manually annotated by BRENDA team
represents as much as 1% of total cytosolic protein in the kidney
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
proximal tubules, high concentration
Manually annotated by BRENDA team
low concentration
Manually annotated by BRENDA team
proximal tubules
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AK1A1_MOUSE
325
0
36587
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in vector pET28a
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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.; Papusha, V.Z.; Ivanova, M.M.; Rudman, D.M.; Finegold, M.J.
Developmental expression and function of aldehyde reductase in proximal tubules of the kidney
Am. J. Physiol. Renal Physiol.
289
F200-F207
2005
Mus musculus (Q9JII6), Mus musculus C57BL/6 (Q9JII6)
Manually annotated by BRENDA team
Short, D.M.; Lyon, R.; Watson, D.G.; Barski, O.A.; McGarvie, G.; Ellis, E.M.
Metabolism of trans, trans-muconaldehyde, acytotoxic metabolite of benzene, in mouse liver by alcohol dehydrogenase Adh1 and aldehyde reductase AKR1A4
Toxicol. Appl. Pharmacol.
210
163-170
2006
Mus musculus
Manually annotated by BRENDA team