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Information on EC 1.1.1.184 - carbonyl reductase (NADPH) and Organism(s) Rattus norvegicus and UniProt Accession B2GV72

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EC Tree
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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This record set is specific for:
Rattus norvegicus
UNIPROT: B2GV72
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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
Reaction Schemes
hide
R-CHOH-R'
+
NADP+
=
R-CO-R'
+
NADPH
+
H+
+
=
+
+
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbonyl reductase 3
-
15-hydroxyprostaglandin dehydrogenase [NADP+]
-
-
-
-
Adipocyte P27 protein
-
-
-
-
aldehyde reductase 1
-
-
-
-
aldehyde reductase I
-
-
-
-
ALR3
-
-
-
-
AP27
-
-
-
-
carbonyl reductase
-
-
-
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carbonyl reductase (NADPH)
-
-
-
-
LCR
-
-
-
-
microsomal carbonyl reductase
-
-
NADPH-carbonyl reductase
-
-
-
-
NADPH-dependent carbonyl reductase
-
-
-
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nonspecific NADPH-dependent carbonyl reductase
-
-
-
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prostaglandin 9-ketoreductase
-
-
-
-
Prostaglandin-E2 9-reductase
-
-
-
-
reductase, carbonyl
-
-
-
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xenobiotic ketone reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
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 hide
77106-95-7
-
89700-36-7
-
89700-37-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
show the reaction diagram
-
-
-
?
5alpha-androstane-17beta-ol-3-one + NADPH
? + NADP+
show the reaction diagram
-
-
-
?
5alpha-androstane-3,17-dione + NADPH
? + NADP+
show the reaction diagram
-
-
-
?
menadione + NADPH
? + NADP+
show the reaction diagram
-
-
-
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
show the reaction diagram
-
-
-
?
4-(6-methoxy-2-benzoxazolyl)acetophenone + NADPH
?
show the reaction diagram
-
-
-
-
?
4-benzoylpyridine + NADPH
?
show the reaction diagram
-
-
-
-
?
acetohexamide + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
prostaglandin A1-GSH + NADPH
?
show the reaction diagram
-
only enzyme forms T3, V1, V2
-
-
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
show the reaction diagram
-
-
-
?
trans-4-phenyl-3-buten-2-one + NADPH
trans-4-phenyl-3-buten-2-ol + NADP+
show the reaction diagram
-
also reacts with NADH, produces only R-enatiomer
-
-
?
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
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
show the reaction diagram
-
-
-
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
no activity with NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chlorpromazine
-
-
dicoumarol
-
-
Disulfiram
-
-
Ethacrynic acid
-
inhibition of enzyme forms V1, V2 and T3
Furosemide
-
inhibition of V1, V2 and T3
indomethacin
-
-
p-hydroxymercuribenzoate
-
-
quercetin
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000015 - 0.0000018
4-benzoylpyridine
0.0000003
menadione
wild-type and mutant W230P
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.183 - 0.23
4-benzoylpyridine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Sprague-Dawley rats
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mucosal epithelium cells
Manually annotated by BRENDA team
additional information
-
overview
Manually annotated by BRENDA team
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?
CRB3_RAT
277
0
30841
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
x * 32000, enzyme form T1, SDS-PAGE
33000
-
rat, different enzyme forms from testis and vas deferens, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W230P
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Ni2+ chelating affinity column chromatography
2 forms from vas deferens: V1, V2
-
3 forms from testis: T1, T2, T3
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
3 forms from rat testis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okita, R.T.; Okita, J.R.
Prostaglandin-metabolizing enzymes during pregnancy: characterization of NAD+-dependent prostaglandin dehydrogenase, carbonyl reductase, and cytochrome P450-dependent prostaglandin omega-hydroxylase
CRC Crit. Rev. Biochem.
31
101-126
1996
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Iwata, N.; Inazu, N.; Takeo, S.; Satoh, T.
Carbonyl reductases from rat testis and vas deferens. Purification, properties and localization
Eur. J. Biochem.
193
75-81
1990
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Okamoto, Y.; Kitamura, S.; Takeshita, M.; Ohta, S.
Microsomal carbonyl reductase responsible for reduction of 4-phenyl-3-buten-2-one in rats
IUBMB Life
48
543-547
1999
Rattus norvegicus
Manually annotated by BRENDA team
Forrest, G.L.; Gonzalez, B.
Carbonyl reductase
Chem. Biol. Interact.
129
21-40
2000
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Wermuth, B.; Mader-Heinemann, G.; Ernst, E.
Cloning and expression of carbonyl reductase from rat testis
Eur. J. Biochem.
228
473-479
1995
Rattus norvegicus
Manually annotated by BRENDA team
Imamura, Y.; Shimada, H.
Differential pharmacokinetics of acetohexamide in male Wistar-Imamichi and Sprague-Dawley rats: role of microsomal carbonyl reductase
Biol. Pharm. Bull.
28
185-187
2005
Rattus norvegicus
Manually annotated by BRENDA team
Miura, T.; Itoh, Y.; Takada, M.; Tsutsui, H.; Yukimura, T.; Nishinaka, T.; Terada, T.
Investigation of the role of the amino acid residue at position 230 for catalysis in monomeric carbonyl reductase 3
Chem. Biol. Interact.
178
211-214
2009
Cricetulus griseus, Homo sapiens, Rattus norvegicus (B2GV72)
Manually annotated by BRENDA team