Any feedback?
Information on EC 1.1.1.184 - carbonyl reductase (NADPH) and Organism(s) Homo sapiens and UniProt Accession P16152
for references in articles please use BRENDA:EC1.1.1.184Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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+)].
Specify your search results
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: Homo sapiens
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
carbonyl reductase 1
-
CBR1
-
15-hydroxyprostaglandin dehydrogenase [NADP+]
-
-
-
-
Adipocyte P27 protein
-
-
-
-
aldehyde reductase 1
-
-
-
-
aldehyde reductase I
-
-
-
-
ALR3
-
-
-
-
AP27
-
-
-
-
carbonyl reductase
carbonyl reductase (NADPH)
-
-
-
-
CBR3
LCR
-
-
-
-
NADPH-carbonyl reductase
-
-
-
-
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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
molecular modeling and enzyme-substrate docking studies, reaction mechanism with anthracyclin substrates
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
13-deoxydoxorubicin + NADPH + H+
?
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
3-glutathionyl-4-hydroxynonanal + NADP+
3-glutathionyl nonanoic-delta-lactone + NADPH + H+
-
oxidation of the hemiacetal form of 3-glutathionyl-4-hydroxynonanal, generating the 3-glutathionyl nonanoic-delta-lactone
-
?
3-glutathionyl-4-hydroxynonanal + NADP+
3-glutathionyl-1,4-dihydroxynonane + NADPH + H+
-
-
-
?
3-glutathionyl-4-hydroxynonanal hemiacetal + NADPH + H+
3-glutathionyl-gamma-nonanolactone + NADP+
-
-
-
?
3-glutathionyl-hexanal + NADPH + H+
3-glutathionyl-hexan-1-ol + NADP+
-
-
-
?
3-glutathionyl-nonanal + NADPH + H+
3-glutathionyl-nonan-1-ol + NADP+
-
-
-
?
3-glutathionyl-propanal + NADPH + H+
3-glutathionyl-propan-1-ol + NADP+
-
-
-
?
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone + NADPH + H+
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol + NADP+
-
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-phenyl(pyridin-4-yl)methanol + NADP+
-
-
-
?
6-(4-acetyl-5-fluoropyridin-3-yl)-3,4-dihydro-1,8-naphthyridine-1(2H)-carboxamide + NADPH + H+
6-[5-fluoro-4-[(1R)-1-hydroxyethyl]pyridin-3-yl]-3,4-dihydro-1,8-naphthyridine-1(2H)-carboxamide + NADP+
selective substrate of human carbonyl reductase 1
-
-
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
-
-
-
-
?
4-methylnitrosamino-1-(3-pyridyl)-1-butanone + NADPH + H+
4-methylnitrosamino-1-(3-pyridyl)-1-butanol + NADP+
-
i.e. NNK, genotoxic compound from tobacco smoke, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184
-
-
r
4-oxo-2-nonenal + NADPH + H+
? + NADP+
-
9% of the activity with 9,10-phenanthrenequinone
-
-
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + 4-hydroxynon-2-enal + 1-hydroxynon-2-en-4-one + NADP+
-
molecular modeling of substrate binding in the active site
product identification, 4-hydroxynon-2-enal is the major product
-
?
bupropion + NADPH + H+
erythrohydrobupropion + NADP+
-
-
in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
-
?
bupropion + NADPH + H+
threohydrobupropion + NADP+
-
-
in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
-
?
glutathione-4-oxononanal + NADPH + H+
glutathione-4-hydroxynonanal + NADP+
-
conjugate, molecular modeling of substrate binding in the active site
-
-
?
menadione + NADPH + H+
? + NADP+
-
48% of the activity with 9,10-phenanthrenequinone
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
S-nitrosoglutathione + NADPH + H+
? + NADP+
no substrate for wild-type, but substrate for mutants D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, and Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S
-
-
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
-
-
-
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
-
-
-
-
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
CBR1 is a predominant hepatic doxorubicin reductase
-
-
?
menadione + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
menadione + NADPH + H+
?
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
mitroxantrone + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
mitroxantrone + NADPH + H+
?
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
naphthazarin + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
naphthazarin + NADPH + H+
?
an anthracyclin, formation of a 13-hydroxy-anthracyclin
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
-
-
-
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
-
-
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
-
-
-
?
4-oxonon-2-enal + NADPH + H+
1-hydroxynon-2-en-4-one + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
4-oxonon-2-enal + NADPH + H+
4-hydroxynon-2-enal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
-
-
-
?
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
oracin + NADPH + H+
dihydrooracin + NADP+
-
a cytostatic drug, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184, stereochemical ratio of 3:1 for R:S enantiomers of the pro-chiral carbonyl centre of oracin, inactivation of the anti-cancer drug
-
-
r
oracin + NADPH + H+
dihydrooracin + NADP+
-
a cytostatic drug, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184, stereochemical ratio of 3:1 for R:S enantiomers of the pro-chiral carbonyl centre of oracin, inactivation reaction
-
-
r
additional information
?
-
CBR1 3'-untranslated region polymorphism 1096G-A in DNA samples from whites, and livers with homozygous G/G genotypes show a trend toward higher CBR1 mRNA levels compared with samples with heterozygous G/A genotypes. CBR1 1096G-A genotype status is associated with CBR1 protein levels
-
-
?
additional information
?
-
-
CBR1 3'-untranslated region polymorphism 1096G-A in DNA samples from whites, and livers with homozygous G/G genotypes show a trend toward higher CBR1 mRNA levels compared with samples with heterozygous G/A genotypes. CBR1 1096G-A genotype status is associated with CBR1 protein levels
-
-
?
additional information
?
-
no doxorubicin or menadione reduction is catalyzed by CBR3
-
-
?
additional information
?
-
-
no doxorubicin or menadione reduction is catalyzed by CBR3
-
-
?
additional information
?
-
single nucleotide polymorphism V88I and P131S mutations exhibit a 20 to 40% decrease in catalytic efficiency (kcat/Km) compared with that for the wild-type enzyme
-
-
?
additional information
?
-
-
single nucleotide polymorphism V88I and P131S mutations exhibit a 20 to 40% decrease in catalytic efficiency (kcat/Km) compared with that for the wild-type enzyme
-
-
?
additional information
?
-
the presence of the glutathionyl moiety in the substrates appears as a necessary requirement for the susceptibility by hCBR1. The corresponding alkanals and alkenals, and the cysteinyl and gamma-glutamyl-cysteinylalkanals adducts are either ineffective or very poorly active as CBR1 substrates
-
-
?
additional information
?
-
-
the presence of the glutathionyl moiety in the substrates appears as a necessary requirement for the susceptibility by hCBR1. The corresponding alkanals and alkenals, and the cysteinyl and gamma-glutamyl-cysteinylalkanals adducts are either ineffective or very poorly active as CBR1 substrates
-
-
?
additional information
?
-
-
no activity with 1-hydroxynon-2-en-4-one and 4-hydroxynon-2-enal
-
-
?
additional information
?
-
-
the enzyme interconvertes 11-oxo-glucocorticoids to their 11-hydroxy metabolites, reaction of EC 1.1.1.146, but is also active as carbonyl reductase, EC 1.1.1.184, in detoxification of xenobiotic carbonyl compounds reducing them to alcohols that are easier to conjugate and eliminate
-
-
?
additional information
?
-
-
the enzyme is responsible for detoxifcation of reactive aldehydes, CR has a potential physiological role for neuroprotection in humans and represents a signifcant pathway for the detoxifcation of reactive aldehydes derived from lipid peroxidation, CR is essential for neuronal cell survival and to confer protection against oxidative stress-induced brain degeneration, overview
-
-
?
additional information
?
-
-
the enzyme metabolizes prostaglandins, steroids, quinines, and anthracycline antibiotics, enzyme expression is inversely associated with tumor progression and angiogenesis
-
-
?
additional information
?
-
-
the enzyme is active with steroids and prostaglandins
-
-
?
additional information
?
-
-
the enzyme shows pluripotent substrate specificity being active as 11beta-hydroxysteroid dehydrogenase, EC 1.1.1.146, and carbonyl reductase, EC 1.1.1.184
-
-
?
additional information
?
-
-
no activity with 5alpha-androstane-3alpha-ol-17-one
-
-
?
additional information
?
-
-
carbonyl reductase oxidizes the hydroxyl group of 3-glutathionyl-4-hydroxynonanal in its hemiacetal form, with the formation of the corresponding 3-glutathionyl nonanoic-delta-lactone. The enzyme is practically inactive toward trans-4-hydroxy-2-nonenal, buthionine sulfoximine, N-acetylcysteine
-
-
?
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
daunorubicin + NADPH + H+
daunorubicinol + NADP+
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
menadione + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
mitroxantrone + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
naphthazarin + NADPH + H+
?
reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
-
-
?
4-methylnitrosamino-1-(3-pyridyl)-1-butanone + NADPH + H+
4-methylnitrosamino-1-(3-pyridyl)-1-butanol + NADP+
-
i.e. NNK, genotoxic compound from tobacco smoke, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184
-
-
r
4-oxonon-2-enal + NADPH + H+
1-hydroxynon-2-en-4-one + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
4-oxonon-2-enal + NADPH + H+
4-hydroxynon-2-enal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
metabolic inactivation of the lipid peroxidation product, pathway overview
-
-
?
oracin + NADPH + H+
dihydrooracin + NADP+
-
a cytostatic drug, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184, stereochemical ratio of 3:1 for R:S enantiomers of the pro-chiral carbonyl centre of oracin, inactivation of the anti-cancer drug
-
-
r
additional information
?
-
-
the enzyme interconvertes 11-oxo-glucocorticoids to their 11-hydroxy metabolites, reaction of EC 1.1.1.146, but is also active as carbonyl reductase, EC 1.1.1.184, in detoxification of xenobiotic carbonyl compounds reducing them to alcohols that are easier to conjugate and eliminate
-
-
?
additional information
?
-
-
the enzyme is responsible for detoxifcation of reactive aldehydes, CR has a potential physiological role for neuroprotection in humans and represents a signifcant pathway for the detoxifcation of reactive aldehydes derived from lipid peroxidation, CR is essential for neuronal cell survival and to confer protection against oxidative stress-induced brain degeneration, overview
-
-
?
additional information
?
-
-
the enzyme metabolizes prostaglandins, steroids, quinines, and anthracycline antibiotics, enzyme expression is inversely associated with tumor progression and angiogenesis
-
-
?
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
Zinc
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-1-(2,4-dihydroxyphenyl)-3-(2',4',6-trihydroxy-5'-[(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]biphenyl-3-yl)prop-2-en-1-one
-
3-(2-(2,4-dihydroxyphenyl)-1-[hydroxy(4-hydroxyphenyl)methyl]-2-oxoethyl)-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
3-[2,3-dihydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-5,7-dihydroxy-4H-chromen-4-one
-
3-[2-(2,4-dihydroxyphenyl)-1-(4-hydroxybenzyl)-2-oxoethyl]-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
7-monohydroxyethylrutoside
inhibits the activity of CBR1 V88 and CBR1 I88 in a concentration-dependent manner. It acts as a competitive CBR1 inhibitor when using daunorubicin as a substrate and acts as an uncompetitive CBR1 inhibitor for the small quinone substrate menadione. It inhibits the binding of NADPH in an uncompetitive manner for both substrates
14,16-dihydroxy-3,8-dimethyl-3,4,5,6,9,10-hexahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
-
zearalenone analogue
18beta-glycyrrhetinic acid
-
inhibits the reduction of bupropion in liver microsomes
4-oxonon-2-enal
-
the substrate is also a mechanism-based inhibitor of the enzyme resulting in 50% inactivation of the enzyme-NADPH complex, presence of cofactor is required for inhibition
glycyrrhetinic acid
-
inhibits both 11beta-hydroxysteroid dehydrogenase and carbonyl reductase activities of the enzyme potently
S-nitrosoglutathione
substrate inhibition above 5 * Km, enzyme is covalantly modified. Treatment with dithiothreitol, but not with ascorbic acid, rescues the activity
S-nitrosoglutathione
treatment leads concentration-dependent S-glutathionylation of cysteines at positions 122, 150, 226, 227. Residues C226/C227 form a disulfide bond. Treatment results in a 25fold decrease in kcat with menadione, 4-benzoylpyridine, 2,3-hexanedione, daunorubicinand 1,4-naphthoquinone, with concomitant increase in kcat for substrates containing a 1,2-diketo group in a ring structure. Except for 9,10-phenanthrenequinone, all changes in kcat are at least in part compensated for by a similar change in Km, overall yielding no drastic changes in catalytic efficiency
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
CR expression is upregulated in brains suffering from Alzheimers disease
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.117
1,2-naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.117
1,2-naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.032
1,4-Naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.032
1,4-Naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.06
2,3-Hexanedione
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.06
2,3-Hexanedione
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
5.85
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
7.84
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
wild-type, pH 7.4, 37°C
0.016
4-benzoylpyridine
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.016
4-benzoylpyridine
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.0128
9,10-phenanthrenequinone
mutant C227S, pH 7.4, temperature not specified in the publication
0.018
9,10-phenanthrenequinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.018
9,10-phenanthrenequinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.0354
9,10-phenanthrenequinone
wild-type, pH 7.4, temperature not specified in the publication
0.028
S-nitrosoglutathione
wild-type, pH 7.4, temperature not specified in the publication
0.81
S-nitrosoglutathione
mutant C227S, pH 7.4, temperature not specified in the publication
0.0043
9,10-phenanthrenequinone
residues 142-143, 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0089
9,10-phenanthrenequinone
residues 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0092
9,10-phenanthrenequinone
residues 97-98, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0393
9,10-phenanthrenequinone
residues 142-143, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0564
9,10-phenanthrenequinone
residues 230, 236244 of CBR3 exchanged to the corresponding amino acids of CBR1
0.078
9,10-phenanthrenequinone
wild-type CBR3 and mutant V244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0225
isatin
residues 142-143, 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0315
isatin
residues 142-143, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0327
isatin
residues 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1
0.0471
isatin
residues 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
0.055
isatin
residues 97-98, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
1.6
isatin
residues 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1
4
isatin
wild-type CBR3 and mutant V244M. Residues 262-277, 236-244/262-277 or 230 of CBR3 exchanged to the corresponding amino acids of CBR1
0.832
S-nitrosoglutathione
mutant Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S, pH 7.4, temperature not specified in the publication
1.09
S-nitrosoglutathione
mutant P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244PpH 7.4, temperature not specified in the publication
2.93
S-nitrosoglutathione
mutant D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, pH 7.4, temperature not specified in the publication
additional information
additional information
recombinant enzyme, steady-state kinetics, molecular modeling and substrate docking studies
-
additional information
additional information
-
the glucocorticoid and xenobiotic reductase activities show cooperative kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
1,2-naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
6.7
1,2-naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.25
1,4-Naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.28
1,4-Naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.32
2,3-Hexanedione
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
1.52
2,3-Hexanedione
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
1
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
2.02
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
wild-type, pH 7.4, 37°C
0.25
4-benzoylpyridine
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.3
4-benzoylpyridine
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
5.25
9,10-phenanthrenequinone
wild-type, pH 7.4, temperature not specified in the publication
6.7
9,10-phenanthrenequinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
9.77
9,10-phenanthrenequinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
36.2
9,10-phenanthrenequinone
mutant C227S, pH 7.4, temperature not specified in the publication
2.02
S-nitrosoglutathione
mutant C227S, pH 7.4, temperature not specified in the publication
2.62
S-nitrosoglutathione
wild-type, pH 7.4, temperature not specified in the publication
5.05
S-nitrosoglutathione
mutant D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, pH 7.4, temperature not specified in the publication
10.83
S-nitrosoglutathione
mutant P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244PpH 7.4, temperature not specified in the publication
20.45
S-nitrosoglutathione
mutant Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S, pH 7.4, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56.7
1,2-naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
56.7
1,2-naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
8.7
1,4-Naphthoquinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
8.7
1,4-Naphthoquinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
25
2,3-Hexanedione
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
0.17
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
0.25
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
wild-type, pH 7.4, 37°C
15.7
4-benzoylpyridine
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
15.7
4-benzoylpyridine
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
148.3
9,10-phenanthrenequinone
wild-type, pH 7.4, temperature not specified in the publication
533
9,10-phenanthrenequinone
after treatment with S-nitrosoglutathione, pH 7.4, 25°C
533
9,10-phenanthrenequinone
enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C
2828
9,10-phenanthrenequinone
mutant C227S, pH 7.4, temperature not specified in the publication
2.5
S-nitrosoglutathione
mutant C227S, pH 7.4, temperature not specified in the publication
93.45
S-nitrosoglutathione
wild-type, pH 7.4, temperature not specified in the publication
1.72
S-nitrosoglutathione
mutant D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, pH 7.4, temperature not specified in the publication
9.93
S-nitrosoglutathione
mutant P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244PpH 7.4, temperature not specified in the publication
24.58
S-nitrosoglutathione
mutant Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S, pH 7.4, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0105
4-amino-1-tert-butyl-3-(2-hydroxyphenyl)pyrazolo[3,4-d]pyrimidine
for doxorubicin metabolism
0.67
S-nitrosoglutathione
wild-type, pH 7.4, temperature not specified in the publication
0.00004
14,16-dihydroxy-3,8-dimethyl-3,4,5,6,9,10-hexahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
-
pH 6.9, temperature not specified in the publication
0.05
7-monohydroxyethylrutoside
CBR1 V88 with cofactor NADPH, with a fixed 0.4 mM daunorubicin concentration
0.14
7-monohydroxyethylrutoside
CBR1 V88 with cofactor NADPH, with a fixed 0.15 mM menadione concentration
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0042
(2E)-1-(2,4-dihydroxyphenyl)-3-(2',4',6-trihydroxy-5'-[(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]biphenyl-3-yl)prop-2-en-1-one
Homo sapiens
pH 7.4, 37°C
0.0036
3-(2-(2,4-dihydroxyphenyl)-1-[hydroxy(4-hydroxyphenyl)methyl]-2-oxoethyl)-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
pH 7.4, 37°C
0.0061
3-[2,3-dihydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-5,7-dihydroxy-4H-chromen-4-one
Homo sapiens
pH 7.4, 37°C
0.0011
3-[2-(2,4-dihydroxyphenyl)-1-(4-hydroxybenzyl)-2-oxoethyl]-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
pH 7.4, 37°C
0.0013
4-amino-1-tert-butyl-3-(2-hydroxyphenyl)pyrazolo[3,4-d]pyrimidine
Homo sapiens
for menadione metabolism
0.00021
14,16-dihydroxy-3,8-dimethyl-3,4,5,6,9,10-hexahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
Homo sapiens
-
pH 6.9, temperature not specified in the publication
0.034
3',4',7-tris[O-(2-hydroxyethyl)]rutin
Homo sapiens
CBR1 I88 with ddoxorubicin as substrate
0.053
3',4',7-tris[O-(2-hydroxyethyl)]rutin
Homo sapiens
CBR1 V88 with doxorubicin as substrate
0.214
3',4',7-tris[O-(2-hydroxyethyl)]rutin
Homo sapiens
CBR1 I88 with daunorubicin as substrate
0.383
3',4',7-tris[O-(2-hydroxyethyl)]rutin
Homo sapiens
CBR1 V88 with daunorubicin as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantitative enzyme expression analysis in 59 samples of non-small-cell lung cancer, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GM10853, GM10845, GM10857, GM10858, GM10860, GM17240, GM16654, GM16688, and GM16689
-
enzyme expression analysis, 59 different samples
black and white donors, show similar CBR1 mRNA and protein levels. CBR1 1096G-A polymorphism is common in samples from white donors
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
carbonyl reductase 1 generating 20beta-dihydrocortisol is a pathway modulating glucocorticoid receptor activation and providing enzymatic protection against excessive GR activation in obesity
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). CBR1_HUMAN
277
0
30375
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
additional information
additional information
molecular modeling and generation of a three-dimensional structural model
additional information
-
enzyme from human liver indistinguishable from enzyme from brain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in presence of S-nitrosoglutathione, S-glutathionylation of cysteines at positions 122, 150, 226, 227 occurs. GSNO treatment of CBR1 results in a 25-fold decrease in kcat with menadione, 4-benzoylpyridine, 2,3-hexanedione, daunorubicin and 1,4-naphthoquinone and an increased kcat for substrates containing a 1,2-diketo group in a ring structure such as 1,2-naphthoquinone, 9,10-phenanthrenequinone, isatin
additional information
-
in presence of S-nitrosoglutathione, S-glutathionylation of cysteines at positions 122, 150, 226, 227 occurs. GSNO treatment of CBR1 results in a 25-fold decrease in kcat with menadione, 4-benzoylpyridine, 2,3-hexanedione, daunorubicin and 1,4-naphthoquinone and an increased kcat for substrates containing a 1,2-diketo group in a ring structure such as 1,2-naphthoquinone, 9,10-phenanthrenequinone, isatin
additional information
presence of a disulfide bond between neighboring residues Cys226 and Cys227
additional information
-
presence of a disulfide bond between neighboring residues Cys226 and Cys227
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational docking experiments for four inhibitors. For flavonoid inhibitors, the flavonoid skeleton is the binding part of the molecule and sugar moieties are pointing outward, giving rise to a stabilizing effect
in complex with glutathione, in the absence of its substrates or inhibitors. The glutathione molecule contributes to the substrate selectivity and protects the catalytic center of hCBR1 through a switch-like mechanism. Glutathione directly binds with hCBR1 when theres no substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C227S
displays a similar kcat, but a 30fold higher Km value for S-nitrosoglutathione, and does not show substrate inhibition
D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P
mutations introduce activity towards S-nitrosoglutathione
P230W
P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P
mutations introduce activity towards S-nitrosoglutathione
Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S
mutations introduce activity towards S-nitrosoglutathione
V244M
V88I
-
functional genetic polymorphism. Mutation results in CBR1 isoforms with different binding affinities for cofactor NADPH and inhibitor rutin as well as different maximal velocities for reaction with daunorubicin and prostaglandin E2
additional information
P230W
active towards isatin and 9,10-phenanthrenequinone as the wild-type
P230W
-
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
V244M
-
naturally occuring polymorphism in isozyme CBR3, the isozyme CBR M244 may reflect a faster association-dissociation rate for NADPH/NADP+ per catalytic cycle, residue 244 is not involved in direct cofactor interaction, overview
V244M
inactive towards menadione, active towards isatin and 9,10-phenanthrenequinone as the wild-type
additional information
residues of CBR3 exchanged to the corresponding amino acids of CBR1. Mutation of nine residues (236-244) in the vicinity of the catalytic center and a proline (P230) in CBR3 to the corresponding residues of CBR1 reveals a much higher kcat/Km value (5.7 micromol/min) towards isatin
additional information
residues of CBR3 exchanged to the corresponding amino acids of CBR1. Mutation of nine residues (236-244) in the vicinity of the catalytic center and a proline (P230) in CBR3 to the corresponding residues of CBR1 reveals a much higher kcat/Km value (5.7 micromol/min) towards isatin
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CBR1 coding regions excised from a pOTB7 recombinant plasmid and subcloned into pET28a vector. Constructs gave rise to a human CBR1 enzyme with a 6x-His tag separated by an 18-amino acid residue linker on the amino terminus. A factor Xa site inserted at the amino terminus between the linker and CBR1 gene. The pET28a constructs of the CBR1 wild-type and variant enzymes heat-shock transformed into Escherichia coli BL21 (DE3) pLysS-competent cells and expressed under the control of an IPTG-inducible T7 polymerase
expression in Escherichia coli
from a liver cDNA library, overexpression in Escherichia coli as His-tagged enzyme
-
isozyme CBR3 V244M, genotyping and polymorphism distribution in 10 different ethnic groups, overview, expression of isozymes CBR V244 and CBR M244 in Escherichia coli strain BL21(DE3)
-
quantitative enzyme expression analysis in 59 samples of non-small-cell lung cancer, overview
-
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
the single nucleotide polymorphisms in the human CBR1 gene generating the V88I and P131S mutations may prove to be clinically useful genetic biomarkers for guiding anthracycline therapy in cancer patients to minimize adverse effects
diagnostics
-
expression of CBR mRNA is a significant prognostic factor in nonsmall-cell lung cancer and is inversely associated with tumor progression and angiogenesis
medicine
-
antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion in liver. Menadione and 18beta-glycyrrhetinic acid are inhibitory
drug development
CBR1 inhibition can improve the therapeutic response to doxorubicin and reduce its side effects
drug development
the cardioprotectant 7-monohydroxyethylrutoside inhibits CBR1 activity. CBR1 V88I genotype status and the type of anthracycline substrate dictate the inhibition of CBR1 activity. Inhibition of CBR1 activity shall be considered during the development of novel cardioprotectants against anthracycline-related cardiotoxicity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wermuth, B.
Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
J. Biol. Chem.
256
1206-1213
1981
Homo sapiens
Bohren, K.M.; von Wartburg, J.P.; Wermuth, B.
Inactivation of carbonyl reductase from human brain by phenylglyoxal and 2,3-butanedione: a comparison with aldehyde reductase and aldose reductase
Biochim. Biophys. Acta
916
185-192
1987
Homo sapiens
Bohren, K.M.; von Wartburg, J.P.; Wermuth, B.
Kinetics of carbonyl reductase from human brain
Biochem. J.
244
165-171
1987
Homo sapiens
Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.
Carbonyl reductase from human testis: purification and comparison with carbonyl reductase from human brain and rat testis
Biochim. Biophys. Acta
1116
50-56
1992
Homo sapiens
Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.; Gabbay, K.H.
Expression, crystallization and preliminary crystallographic analysis of human carbonyl reductase
J. Mol. Biol.
244
659-664
1994
Homo sapiens
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
Wermuth, B.; Platts, K.L.; Seidel, A.; Oesch, F.
Carbonyl reductase provides the enzymatic basis of quinone detoxication in man
Biochem. Pharmacol.
35
1277-1282
1986
Homo sapiens
Doorn, J.A.; Maser, E.; Blum, A.; Claffey, D.J.; Petersen, D.R.
Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal
Biochemistry
43
13106-13114
2004
Homo sapiens
Maser, E.
Neuroprotective role for carbonyl reductase?
Biochem. Biophys. Res. Commun.
340
1019-1022
2006
Drosophila melanogaster, Homo sapiens
Takenaka, K.; Ogawa, E.; Oyanagi, H.; Wada, H.; Tanaka, F.
Carbonyl reductase expression and its clinical significance in non-small-cell lung cancer
Cancer Epidemiol. Biomarkers Prev.
14
1972-1975
2005
Homo sapiens
Slupe, A.; Williams, B.; Larson, C.; Lee, L.M.; Primbs, T.; Bruesch, A.J.; Bjorklund, C.; Warner, D.L.; Peloquin, J.; Shadle, S.E.; Gambliel, H.A.; Cusack, B.J.; Olson, R.D.; Charlier, H.A.
Reduction of 13-deoxydoxorubicin and daunorubicinol anthraquinones by human carbonyl reductase
Cardiovasc. Toxicol.
5
365-376
2005
Homo sapiens (P16152)
Lakhman, S.S.; Ghosh, D.; Blanco, J.G.
Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)
Drug Metab. Dispos.
33
254-257
2005
Homo sapiens
Maser, E.; Wsol, V.; Martin, H.J.
11beta-Hydroxysteroid dehydrogenase type 1: purification from human liver and characterization as carbonyl reductase of xenobiotics
Mol. Cell. Endocrinol.
248
34-37
2006
Homo sapiens
Carlquist, M.; Frejd, T.; Gorwa-Grauslund, M.F.
Flavonoids as inhibitors of human carbonyl reductase 1
Chem. Biol. Interact.
174
98-108
2008
Homo sapiens (P16152), Homo sapiens
Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.; Blanco, J.G.
A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity
Drug Metab. Dispos.
35
973-980
2007
Homo sapiens
Miura, T.; Nishinaka, T.; Terada, T.
Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1
Mol. Cell. Biochem.
315
113-121
2008
Homo sapiens (O75828), Homo sapiens
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)
El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann, U.; Martin, H.J.; Maser, E.
Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis
Chem. Biol. Interact.
178
234-241
2009
Homo sapiens (O75828), Homo sapiens (P16152)
Kassner, N.; Huse, K.; Martin, H.J.; Goedtel-Armbrust, U.; Metzger, A.; Meineke, I.; Brockmoeller, J.; Klein, K.; Zanger, U.M.; Maser, E.; Wojnowski, L.
Carbonyl reductase 1 is a predominant doxorubicin reductase in the human liver
Drug Metab. Dispos.
36
2113-2120
2008
Homo sapiens (P16152), Homo sapiens
Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs, K.W.
Two nonsynonymous single nucleotide polymorphisms of human carbonyl reductase 1 demonstrate reduced in vitro metabolism of daunorubicin and doxorubicin
Drug Metab. Dispos.
37
1107-1114
2009
Homo sapiens (P16152), Homo sapiens
Gonzalez-Covarrubias, V.; Zhang, J.; Kalabus, J.L.; Relling, M.V.; Blanco, J.G.
Pharmacogenetics of human carbonyl reductase 1 (CBR1) in livers from black and white donors
Drug Metab. Dispos.
37
400-407
2009
Homo sapiens (P16152), Homo sapiens
Gonzalez-Covarrubias, V.; Kalabus, J.L.; Blanco, J.G.
Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER)
Pharm. Res.
25
1730-1734
2008
Homo sapiens (P16152), Homo sapiens
Zimmermann, T.; Niesen, F.; Pilka, E.; Knapp, S.; Oppermann, U.; Maier, M.
Discovery of a potent and selective inhibitor for human carbonyl reductase 1 from propionate scanning applied to the macrolide zearalenone
Bioorg. Med. Chem.
17
530-536
2009
Homo sapiens
Staab, C.A.; Hartmanova, T.; El-Hawari, Y.; Ebert, B.; Kisiela, M.; Wsol, V.; Martin, H.J.; Maser, E.
Studies on reduction of S-nitrosoglutathione by human carbonyl reductases 1 and 3
Chem. Biol. Interact.
191
95-103
2011
Homo sapiens (O75828), Homo sapiens (P16152)
Hartmanova, T.; Tambor, V.; Len?o, J.; Staab-Weijnitz, C.A.; Maser, E.; Wsol, V.
S-nitrosoglutathione covalently modifies cysteine residues of human carbonyl reductase 1 and affects its activity
Chem. Biol. Interact.
202
136-145
2013
Homo sapiens (P16152), Homo sapiens
Molnari, J.; Myers, A.
Carbonyl reduction of bupropion in human liver
Xenobiotica
42
550-561
2012
Homo sapiens
Moschini, R.; Peroni, E.; Rotondo, R.; Renzone, G.; Melck, D.; Cappiello, M.; Srebot, M.; Napolitano, E.; Motta, A.; Scaloni, A.; Mura, U.; Del-Corso, A.
NADP(+)-dependent dehydrogenase activity of carbonyl reductase on glutathionylhydroxynonanal as a new pathway for hydroxynonenal detoxification
Free Radic. Biol. Med.
83
66-76
2015
Homo sapiens
Rotondo, R.; Moschini, R.; Renzone, G.; Tuccinardi, T.; Balestri, F.; Cappiello, M.; Scaloni, A.; Mura, U.; Del-Corso, A.
Human carbonyl reductase 1 as efficient catalyst for the reduction of glutathionylated aldehydes derived from lipid peroxidation
Free Radic. Biol. Med.
99
323-332
2016
Homo sapiens (P16152), Homo sapiens
Liang, Q.; Liu, R.; Du, S.; Ding, Y.
Structural insights on the catalytic site protection of human carbonyl reductase 1 by glutathione
J. Struct. Biol.
192
138-144
2015
Homo sapiens (P16152), Homo sapiens
Barracco, V.; Moschini, R.; Renzone, G.; Cappiello, M.; Balestri, F.; Scaloni, A.; Mura, U.; Del-Corso, A.
Dehydrogenase/reductase activity of human carbonyl reductase 1 with NADP(H) acting as a prosthetic group
Biochem. Biophys. Res. Commun.
522
259-263
2020
Homo sapiens (P16152), Homo sapiens
Moschini, R.; Rotondo, R.; Renzone, G.; Balestri, F.; Cappiello, M.; Scaloni, A.; Mura, U.; Del-Corso, A.
Kinetic features of carbonyl reductase 1 acting on glutathionylated aldehydes
Chem. Biol. Interact.
276
127-132
2017
Homo sapiens (P16152), Homo sapiens
Ramsden, D.; Smith, D.; Arenas, R.; Frederick, K.; Cerny, M.A.
Identification and characterization of a selective human carbonyl reductase 1 substrate
Drug Metab. Dispos.
46
1434-1440
2018
Homo sapiens (P16152), Homo sapiens
Morgan, R.A.; Beck, K.R.; Nixon, M.; Homer, N.Z.M.; Crawford, A.A.; Melchers, D.; Houtman, R.; Meijer, O.C.; Stomby, A.; Anderson, A.J.; Upreti, R.; Stimson, R.H.; Olsson, T.; Michoel, T.; Cohain, A.; Ruusalepp, A.; Schadt, E.E.; Bjoerkegren, J.L.M.; Andrew, R.; Kenyon, C.J.; Hadoke, P.W.F.; Odermatt, A.; Keen, J.
Carbonyl reductase 1 catalyzes 20beta-reduction of glucocorticoids, modulating receptor activation and metabolic complications of obesity
Sci. Rep.
7
10633
2017
Equus caballus, Homo sapiens (P16152), Homo sapiens, Mus musculus (P48758)
Kandeel, M.; Al-Taher, A.; Al-Nazawi, M.; Ohhashi, K.
Substructural dynamics of the phase-I drug metabolizing enzyme, carbonyl reductase 1, in response to various substrate and inhibitor configurations
Trop. J. Pharm. Res.
18
1635-1641
2019
Homo sapiens (P16152)
-
EXTERNAL LINKS (specific for EC-Number 1.1.1.184)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
