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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Sus scrofa and UniProt Accession P50578
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1.1.1.2 alcohol dehydrogenase (NADP+)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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Word Map
- 1.1.1.2
- horse
- dehydrogenases
- reductases
- hydroxylase
- steroid
- nad+
- aldose
- akr1b10
- nicotinamide
- aniline
- aminopyrine
- n-demethylase
- akr1c2
- acetaldehyde
- pyrazole
-
nadh-cytochrome
-
drug-metabolizing
-
benzoapyrene
-
hydride
- benzphetamine
- ethylmorphine
-
mixed-function
-
1.1.1.1
- 7-ethoxycoumarin
- beta-naphthoflavone
-
udp-glucuronyltransferase
-
p-nitroanisole
- 4-methylpyrazole
-
3alpha-hydroxysteroids
-
coenzyme-binding
-
dihydrodiols
- 3-methylcholanthrene
-
n-demethylation
-
ethoxyresorufin
- hydroxysteroids
- acrolein
- hexobarbital
-
p-450-dependent
-
zinc-bound
- 17beta-hsds
- analysis
- sorbinil
- cyclohexanol
- medicine
- agriculture
- trifluoroethanol
- 5alpha-dihydrotestosterone
- ketosteroid
- synthesis
-
17beta-hydroxysteroids
- industry
- o-quinones
- tolrestat
-
3alpha
-
phosphorescence
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-DG-reducing enzyme
-
-
-
-
ADH
-
-
-
-
Alcohol dehydrogenase [NADP+]
-
-
-
-
aldehyde reductase
-
-
-
-
aldehyde reductase (NADPH2)
-
-
-
-
Aldo-keto reductase family 1 member A1
-
-
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
high-Km aldehyde reductase
-
-
-
-
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
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
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
9028-12-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-pyridinecarboxaldehyde + NADPH
3-pyridinemethanol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
286165, 286167, 286168, 286171, 286172, 286174, 286176, 286177, 286178, 286179, 286181, 286182, 286196
-
-
r
L-glyceraldehyde + NADPH
glycerol + NADP+
-
-
-
-
r
p-carboxybenzaldehyde + NADPH
p-carboxybenzyl alcohol + NADP+
-
-
-
-
r
p-hydroxyphenylacetaldehyde + NADPH + H+
p-hydroxyphenylethanol + NADP+
-
-
-
-
r
p-hydroxyphenylglycolaldehyde + NADPH
4-hydroxyphenylethylalcohol + NADP+
-
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
L-gulonic acid + NADP+
D-glucuronic acid + NADPH
-
-
-
-
r
L-gulonic acid + NADPH
D-glucuronic acid + NADP+
-
-
-
-
r
p-nitrobenzaldehyde + NADPH
p-nitrobenzylalcohol + NADP+
-
-
-
-
r
p-nitrobenzaldehyde + NADPH
p-nitrobenzylalcohol + NADP+
-
cofactor NADPH
-
-
r
additional information
?
-
-
5-hydroxyindol-3-ylacetaldehyde is no substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
L-glyceraldehyde + NADPH
glycerol + NADP+
-
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20alpha-hydroxysteroid dehydrogenase
competitive inhibition, the inhibitor forms a 10fold stronger binding interaction with the catalytic residue (Tyr55), non-conserved hydrogen bonding interaction with His222, and additional van der Waals contacts with the non-conserved C-terminal residues Leu306, Leu308 and Phe311 that contribute to the inhibitor's selectivity advantage for 20alpha-hydroxysteroid dehydrogenase over 3,5-dichlorosalicylic acid
-
3,5-dichlorosalicylic acid
mixed type of competitive and non-competitive patterns with respect to the substrate. The inhibitor forms a network of hydrogen bonds with the active site residues Trp22, Tyr50, His113, Trp114 and Arg312. Is a less potent inhibitor of ALR1 (256fold) when compared to 20alpha-hydroxysteroid dehydrogenase
[5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
i.e. CMD, a potent inhibitor of ALR2, but not for ALR1. For binding to ALR1, the partially disordered inhibitor forms a tight network of hydrogen bonds with the active site residues Tyr50 and His113 and NADPH, 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-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
crystallization data. The rotameric state of the conserved residue Trp220 in aldehyde reductase ALR1, i.e Trp 219 in aldose reductase ALR2, is important in forming a pi-stacking interaction with the inhibitor in aldose reductase and contributes to the difference in the binding of the inhibitor to the enzymes
[5-(3-hydroxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
-
additional information
-
enzyme active site interactions with the 3-carboxymethoxy-4-methoxy-phenyl moiety of the inhibitor, binding structure, overview
-
additional information
enzyme active site interactions with the 3-carboxymethoxy-4-methoxy-phenyl moiety of the inhibitor, binding structure, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0054
[5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
Sus scrofa
ALR1, pH not specified in the publication, temperature not specified in the publication
0.037
[5-(3-hydroxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
Sus scrofa
ALR1, pH not specified in the publication, temperature not specified in the publication
0.0054
[5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid
Sus scrofa
25°C, pH 6.7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
286150, 286165, 286166, 286167, 286168, 286170, 286172, 286173, 286174, 286176, 286177, 286178, 286180, 286181, 286182, 286185, 286189
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AK1A1_PIG
325
0
36582
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
-
gel filtration, ultracentrifugation, specific activity corresponding to molecular weight
30200
33000
34000
43700
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 22°C by vapor-diffusion using the hanging drop method. ALR1 in ternary complex with the coenzyme NADPH and 3,5-dichlorosalicylic acid, at a resolution of 2.41 A
purified aldehyde reductase, ALR1, in ternary complex with NADPH and [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid, hanging drop method, 17-18 mg/ml protein in 5 mM Tris-HCl, pH 6.5, containing 5 mM 2-mercaptoethanol, mixed with NADPH and inhibitor in a 1:20:3molar ratio, the reservoir solution contains 2.0 M ammonium sulfate, and 0.1 M Tris-HCl buffer, pH 8.5, 10 days, X-ray diffraction structure determination and analysis at 1.99 A resolution
hanging drop method, with NADPH, ammonium sulfate, Tris HCl-buffer, pH 8.1, buffer C, maximum side: 0.3 mm x 0.1 mm x 0,1 mm after 1 week
-
in ternary complex with NADPH and a 5-arylidene-2,4-thiazolidinedione aldose reductase inhibitor, [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid to 1.99 A resolution. The partially disordered inhibitor forms a tight network of hydrogen bonds with the active site residues Tyr50 and His113 and coenzyme. pi-Stacking interactions with several conserved active site tryptophan residues and hydrogen-bonding interactions with the non-conserved C-terminal residue Pro301 in aldehyde reductase ALR1 contribute to inhibitor selectivity. In particular for the potent inhibitor [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid, the rotameric state of the conserved residue Trp220 in ALR1, i.e Trp 219 in aldose reductase, is important in forming a pi-stacking interaction with the inhibitor in aldose reductase and contributes to the difference in the binding of the inhibitor to the enzymes
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several months if stored as an ammonium sulfate precipitate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aldehyde reductase I and II from brain, no recuctase II activity could be detected in pig kidney
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
daunorubicin, a cancer chemotherapeutic agent can be reduced by aldehyde reductase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
Flynn, T.G.; Shires, J.; Walton, D.J.
Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney. Amino acid composition, reactivity of cysteinyl residues, and stereochemistry of D-glyceraldehyde reduction
J. Biol. Chem.
250
2933-2940
1975
Oryctolagus cuniculus, Sus scrofa
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
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
Davidson, W.S.; Flynn, T.G.
Kinetics and mechanism of action of aldehyde reductase from pig kidney
Biochem. Soc. Trans.
576
943-945
1978
Pecten maximus, Sus scrofa
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
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
Turner, A.J.; Hryszko, J.
Isolation and characterization of rat liver aldehyde reductase
Biochim. Biophys. Acta
613
256-265
1980
Rattus norvegicus, Sus scrofa
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
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
Daly, A.K.; Mantle, T.J.
Purification and characterization of the multiple forms of aldehyde reductase in ox kidney
Biochem. J.
205
373-380
1982
Bos taurus, Cavia porcellus, Sus scrofa
Daly, A.K.; Mantle, T.J.
The kinetic mechanism of the major form of ox kidney aldehyde reductase with D-glucuronic acid
Biochem. J.
205
381-388
1982
Bos taurus, Saccharomyces cerevisiae, Sus scrofa
Branlant, G.
Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens
Eur. J. Biochem.
129
99-104
1982
Sus scrofa
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
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
Magnien, A.; Branlant, G.
The kinetics and mechanism of pig-liver aldehyde reductase. Comparative studies with pyridine-3-aldehyde and p-carboxybenzaldehyde
Eur. J. Biochem.
131
375-381
1983
Sus scrofa
Kovar, J.; Plocek, J.
Purification of aldehyde reductase 1 from pig liver
J. Chromatogr.
351
371-375
1986
Sus scrofa
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
Ye, Q.; Hyndman, D.; Green, N.; Li, X.; Korithoski, B.; Jia, Z.; Flynn, T.G.
Crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding
Proteins
44
12-19
2001
Sus scrofa
Cromlish, J.A.; Yoshimoto, C.K.; Flynn, T.G.
Purification and characterization of four NADPH-dependent aldehyde reductases from pig brain
J. Neurochem.
44
1477-1484
1985
Sus scrofa
El-Kabbani, O.; Carbone, V.; Darmanin, C.; Oka, M.; Mitschler, A.; Podjarny, A.; Schulze-Briese, C.; Chung, R.P.
Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity
J. Med. Chem.
48
5536-5542
2005
Sus scrofa
Petroval, T.; Steuber, H.; Hazemann, I.; Cousido-Siah, A.; Mitschler, A.; Chung, R.; Oka, M.; Klebe, G.; El-Kabbani, O.; Joachimiak, A.; Podjarny, A.
Factorizing selectivity determinants of inhibitor binding toward aldose and aldehyde reductases: structural and thermodynamic properties of the aldose reductase mutant Leu300Pro-fidarestat complex
J. Med. Chem.
48
5659-5665
2005
Sus scrofa
Carbone, V.; Chung, R.; Endo, S.; Hara, A.; El-Kabbani, O.
Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor 3,5-dichlorosalicylic acid: implications for inhibitor binding and selectivity
Arch. Biochem. Biophys.
479
82-87
2008
Sus scrofa (P50578)
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
Sus scrofa, Sus scrofa (P50578)
EXTERNAL LINKS (specific for EC-Number 1.1.1.2)
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