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Information on EC 1.1.1.184 - carbonyl reductase (NADPH) and Organism(s) Sus scrofa and UniProt Accession Q8WNV7
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1.1.1.184 carbonyl reductase (NADPH)IUBMB Comments
Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)].
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Word Map
- 1.1.1.184
- polyketide
- reductases
-
anthracycline
-
aldo-keto
-
ketosynthase
- cardiotoxicity
-
actinorhodin
-
6-deoxyerythronolide
-
enoylreductase
- doxorubicinol
-
ketoreduction
- n-acetylcysteamine
-
triketide
-
mycolactone
-
buruli
- synthesis
-
stereocenters
- 4-chloro-3-oxobutanoate
-
angucycline
-
kreds
- ulcerans
-
s-4-chloro-3-hydroxybutanoate
-
ketoacyl
-
stereocontrol
- daunorubicinol
- medicine
- diagnostics
- industry
- drug development
- food industry
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
ketoreductase, carbonyl reductase 1, aldehyde reductase i, nadph-dependent carbonyl reductase, carbonyl reductase 3, hcbr1, tetrameric carbonyl reductase, tm1743, prostaglandin 9-ketoreductase, chcr3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
15-hydroxyprostaglandin dehydrogenase [NADP+]
-
-
-
-
Adipocyte P27 protein
-
-
-
-
aldehyde reductase 1
-
-
-
-
aldehyde reductase I
-
-
-
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ALR3
-
-
-
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AP27
-
-
-
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carbonyl reductase
carbonyl reductase (NADPH)
-
-
-
-
LCR
-
-
-
-
NADPH-carbonyl reductase
-
-
-
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NADPH-dependent carbonyl reductase
-
-
-
-
nonspecific NADPH-dependent carbonyl reductase
-
-
-
-
prostaglandin 9-ketoreductase
-
-
-
-
Prostaglandin-E2 9-reductase
-
-
-
-
reductase, carbonyl
-
-
-
-
xenobiotic ketone reductase
-
-
-
-
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
carbonyl reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
secondary-alcohol:NADP+ oxidoreductase
Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)].
CAS REGISTRY NUMBER
COMMENTARY
77106-95-7
-
89700-36-7
-
89700-37-8
-
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
1,4-benzoquinone + NADPH
? + NADP+
-
native and recombinant enzymes, low activity
-
-
?
1,4-naphthoquinone + NADPH + H+
? + NADP+
-
native and recombinant enzymes, low activity
-
-
?
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanol + NADP+
i.e. mequindox, synthetic quinoxaline derivative, inhibitory to several Gram-positive and Gram-negative bacteria
-
-
?
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanol + NADP+
-
-
-
?
2-benzoylpyridine + NADPH
(S)-alpha-phenyl-2-pyridylmethanol + NADP+
-
highly stereoselective reaction, native and recombinant enzymes, low activity
-
-
?
4-benzoylpyridine + NADPH + H+
S-(-)-phenylpyridin-4-yl-methynol + NADP+
-
stereoselective reduction
-
-
?
4-nitroacetophenone + NADPH
1-(4-nitrophenyl)ethanol + NADP+
-
native and recombinant enzymes, low activity
-
-
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzylalcohol + NADP+
-
native and recombinant enzymes
-
-
?
9,10-phenanthrenequinone + NADPH
? + NADP+
-
best substrate, recombinant enzyme
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
recombinant enzyme
-
-
?
hexaphenone + NADPH
1-phenylhexan-1-ol + NADP+
-
native and recombinant enzymes
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyridine-3-aldehyde + NADPH
pyridin-3-ylbutanol + NADP+
-
native and recombinant enzymes, low activity
-
-
?
3-benzoylpyridine + NADPH
(S)-alpha-phenyl-3-pyridylmethanol + NADP+
-
recombinant enzyme
-
-
?
3-benzoylpyridine + NADPH
(S)-alpha-phenyl-3-pyridylmethanol + NADP+
-
highly stereoselective reaction, native and recombinant enzymes
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
-
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
recombinant enzyme
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
highly stereoselective reaction, native and recombinant enzymes
-
-
?
4-hexanoylpyridine + NADPH + H+
1-(pyridin-4-yloxy)hexan-1-ol + NADP+
-
recombinant enzyme
-
-
?
4-hexanoylpyridine + NADPH + H+
1-(pyridin-4-yloxy)hexan-1-ol + NADP+
-
native and recombinant enzymes
-
-
?
n-butyrophenone + NADPH
1-phenylbutan-1-ol + NADP+
-
native and recombinant enzymes, low activity
-
-
?
propiophenone + NADPH
1-phenylpropan-1-ol + NADP+
-
native and recombinant enzymes, low activity
-
-
?
pyridine-4-aldehyde + NADPH + H+
pyridin-4-ylmethanol + NADP+
-
recombinant enzyme
-
-
?
pyridine-4-aldehyde + NADPH + H+
pyridin-4-ylmethanol + NADP+
-
native and recombinant enzymes
-
-
?
valerophenone + NADPH
1-phenylpentan-1-ol + NADP+
-
native and recombinant enzymes
-
-
?
additional information
?
-
-
catalyzes pro-S stereoselective hydrogen transfer from NADPH
-
-
?
additional information
?
-
-
substrate specificity, no activity with 3-nitroacetophenone and 4-acetylpyridine, catalytic activity of the recombinant enzyme is similar to the native enzyme
-
-
?
additional information
?
-
-
the enzyme plays a role in superoxide formation through redox cycling of 9,10-phenanthrenequinone and, to a lesser extent, of adrenochrome in pig heart
-
-
?
additional information
?
-
-
the enzyme catalyses the NADPH-linked reduction of a variety of carbonyl compounds to their secondary alcohols
-
-
?
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
4-benzoylpyridine + NADPH + H+
S-(-)-phenylpyridin-4-yl-methynol + NADP+
-
stereoselective reduction
-
-
?
additional information
?
-
-
the enzyme plays a role in superoxide formation through redox cycling of 9,10-phenanthrenequinone and, to a lesser extent, of adrenochrome in pig heart
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
pro-4S hydrogen atom of the nicotinamide ring of NADPH is transferred to the substrate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
butyrophenone
-
inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
heptanophenone
-
inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
hexanophenone
-
competitive. Inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
propiophenone
-
inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
valerophenone
-
inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
additional information
-
the inhibitory potencies of alkyl 4-pyridyl ketones increases with an increase in the number up to five carbon atoms in the alkyl group, and 4-hexanoylpyridine is the most potent inhibitor of the enzyme activity. The inhibitory potencies of 4-heptanoylpyridine and 4-octanoylpyridine are lower than that of 4-hexanoylpyridine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fatty acids
-
with carbon chain length greater than nine at pH 7.0 activate, e.g. arachidonic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
additional information
-
enzyme activation by arachidonic acid shifts pH-optimum from 5.8 to 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
ciliated cells, nonciliated bronchiolar cells, Type II alveolar pneumocytes, epithelial cells of the ducts of the bronchial gland
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
C-terminal peroxisomal targeting sequence 1 of each subunit is involved in intersubunit interactions and buried in the interior of the tetrameric enzyme
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). DHRS4_PIG
279
0
29919
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
ribbon diagram of tertiary structure, diagrams of additional members of SDR family
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal peroxisomal targeting sequence 1 of each subunit is involved in intersubunit interactions and buried in the interior of the tetrameric enzyme
crystallization to crystal forms I and II in the presence of NADPH. Form I crystals belong to the tetragonal space group P42, and diffract to 1.5 A resolution. Form II crystals belong to the tetragonal space group P41212, and diffract to 2.2 A resolution
-
purified and dialyzed recombinant enzyme complexed with cofactor, 3 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM NADPH, hanging drop vapour diffusion method, 0.002 ml of protein and crystallization solutions are mixed at 20°C, and equilibrated against 0.5 ml reservoir solution, which contains 2.2 M sodium citrate and 20%(v/v) glycerol in 100 mM HEPES buffer, pH 7.5 or 1.4 M ammonium sulfate and 20%(v/v) glycerol in 100 mM MES buffer pH 6.0, resulting in two different tetragonal crystal forms, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.2 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mutation of C-terminal peroxisomal targeting sequence SRL to SKL, SHL, SLL, and SL. Mutants SLL and SL are not catalytically active. Mutant SHL is gradually inactivated during incubation at 0°C. Both mutants SHL and SKL are tetramers and show kinetic parameters similar to wild-type
additional information
-
mutation of C-terminal peroxisomal targeting sequence SRL to SKL, SHL, SLL, and SL. Mutants SLL and SL are not catalytically active. Mutant SHL is gradually inactivated during incubation at 0°C. Both mutants SHL and SKL are tetramers and show kinetic parameters similar to wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activation by arachidonic acid leads to a decrease in thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, gel filtration, and affinity and hydroxylapatite chromatography, followed by ultrafiltration, the protein easily precipitates at concentraions of above 3.3 mg/ml
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
expression of the heart enzyme in Escherichia coli BL21(DE3), assembly to tetrameric form
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
mequindox, inhibitor of several Gram-positive and Gram-negative bacteria, is reduced by carbonyl reductase CBR1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oritani, H.; Deyashiki, Y.; Nakayama, T.; Hara, A.; Sawada, H.; Matsuura, K.; Bunai, Y.; Ohya, I.
Purification and characterization of pig lung carbonyl reductase
Arch. Biochem. Biophys.
292
539-547
1992
Sus scrofa
Naganuma, H.; Kondo, J.I.; Kawahara, Y.
Enantiospecific assay for mammalian carbonyl reductase by liquid chromatography with fluorescence detection
J. Chromatogr.
532
65-74
1990
Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Hara, A.; Oritani, H.; Deyashiki, Y.; Nakayama, T.; Sawada, H.
Activation of carbonyl reductase from pig lung by fatty acids
Arch. Biochem. Biophys.
292
548-554
1992
Sus scrofa
Ghosh, D.; Sawicki, M.; Pletnev, V.; Erman, M.; Ohno, S.; Nakajin, S.; Duax, W.L.
Porcine carbonyl reductase: structural basis for a functional monomer in short chain dehydrogenases/reductases
J. Biol. Chem.
276
18457-18463
2001
Sus scrofa
Forrest, G.L.; Gonzalez, B.
Carbonyl reductase
Chem. Biol. Interact.
129
21-40
2000
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Schieber, A.; Frank, R.W.; Ghisla, S.
Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase
Eur. J. Biochem.
206
491-502
1992
Homo sapiens, Sus scrofa
Usami, N.; Ishikura, S.; Abe, H.; Nagano, M.; Uebuchi, M.; Kuniyasu, A.; Otagiri, M.; Nakayama, H.; Imamura, Y.; Hara, A.
Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase
Chem. Biol. Interact.
143-144
353-361
2003
Sus scrofa
Shimada, H.; Fujiki, S.; Oginuma, M.; Asakawa, M.; Okawara, T.; Kato, K.; Yamamura, S.; Akita, H.; Hara, A.; Imamura, Y.
Stereoselective reduction of 4-benzoylpyridine by recombinant pig heart carbonyl reductase
J. Mol. Catal. B
23
29-35
2003
Sus scrofa
-
Aoki, K.; Tanaka, N.; Ishikura, S.; Araki, N.; Imamura, Y.; Hara, A.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic studies of pig heart carbonyl reductase
Acta Crystallogr. Sect. F
62
1037-1040
2006
Sus scrofa
Oginuma, M.; Shimada, H.; Imamura, Y.
Involvement of carbonyl reductase in superoxide formation through redox cycling of adrenochrome and 9,10-phenanthrenequinone in pig heart
Chem. Biol. Interact.
155
148-154
2005
Sus scrofa
Imamura, Y.; Narumi, R.; Shimada, H.
Inhibition of carbonyl reductase activity in pig heart by alkyl phenyl ketones
J. Enzyme Inhib. Med. Chem.
22
105-109
2007
Sus scrofa
Tanaka, N.; Aoki, K.; Ishikura, S.; Nagano, M.; Imamura, Y.; Hara, A.; Nakamura, K.T.
Molecular basis for peroxisomal localization of tetrameric carbonyl reductase
Structure
16
388-397
2008
Sus scrofa (Q8WNV7), Sus scrofa
Tang, X.; Mu, P.; Wu, J.; Jiang, J.; Zhang, C.; Zheng, M.; Deng, Y.
Carbonyl reduction of mequindox by chicken and porcine cytosol and cloned carbonyl reductase 1
Drug Metab. Dispos.
40
788-795
2012
Gallus gallus (F1N8Y3), Gallus gallus, Sus scrofa (Q28960), Sus scrofa
Shimada, H.; Tanigawa, T.; Matayoshi, K.; Katakura, K.; Babazono, K.; Takayama, H.; Murahashi, T.; Akita, H.; Higuchi, T.; Eto, M.; Imamura, Y.
Comparative inhibition of tetrameric carbonyl reductase activity in pig heart cytosol by alkyl 4-pyridyl ketones
J. Enzyme Inhib. Med. Chem.
29
397-400
2014
Sus scrofa
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