Any feedback?
No. of entries
Information on EC 1.1.1.184 - carbonyl reductase (NADPH)
for references in articles please use BRENDA:EC1.1.1.184
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
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+)].
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
- 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
showSynonyms
ketoreductase, carbonyl reductase 1, aldehyde reductase i, nadph-dependent carbonyl reductase, carbonyl reductase 3, hcbr1, tetrameric carbonyl reductase, tm1743, prostaglandin 9-ketoreductase, chcr3, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R) specific carbonyl reductase
(S)-specific carbonyl reductase
15-hydroxyprostaglandin dehydrogenase [NADP+]
-
-
-
-
2,5-diketo-D-gluconic acid reductase
Adipocyte P27 protein
-
-
-
-
aldehyde reductase 1
-
-
-
-
aldehyde reductase I
-
-
-
-
aldo-keto reductase
ALR3
-
-
-
-
AP27
-
-
-
-
carbonyl reductase
carbonyl reductase (NADPH)
-
-
-
-
carbonyl reductase 1
carbonyl reductase 3
carbonyl reductase S1
CBR1
CBR3
CR
crc1
Gox0644
Gox1615
LCR
-
-
-
-
NADP+-dependent ADH
NADPH-carbonyl reductase
-
-
-
-
NADPH-dependent carbonyl reductase
NADPH-dependent carbonyl reductase S1
NCCR
nonspecific NADPH-dependent carbonyl reductase
-
-
-
-
prostaglandin 9-ketoreductase
-
-
-
-
Prostaglandin-E2 9-reductase
-
-
-
-
reductase S1
reductase, carbonyl
-
-
-
-
SCR
SRED
Tm1743
Tm_1743
xenobiotic ketone reductase
-
-
-
-
YGL039w1
YGL039w2
YtbE
YueD
additional information
carbonyl reductase
-
-
-
-
carbonyl reductase 1
-
CBR1
-
NADPH-dependent carbonyl reductase
-
-
-
-
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
additional information
-
the enzyme belongs to the short-chain dehydrogenases/reductases family
additional information
-
the enzyme is a member of the short-chain dehydrogenase/reductase family
additional information
Starmerella magnoliae AKU4643
-
the enzyme is a member of the short-chain dehydrogenase/reductase family
-
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
-
-
-
-
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
stereospecifc reaction mechanism
-
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
ordered bi bi mechanism, in which NADPH binds first and NADP+ leaves last
-
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
stereoselective enzyme, reaction mechanism and substrate binding model, formation of a hydrophobic channel induced by NADPH binding
-
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
substrate specificity, enantioselectivity, and enzyme-substrate docking studies, Ser133 and Tyr177 are important
-
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
molecular modeling and enzyme-substrate docking studies, reaction mechanism with anthracyclin substrates
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+
substrate specificity, enantioselectivity, and enzyme-substrate docking studies, Ser133 and Tyr177 are important
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+)].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
77106-95-7
-
89700-36-7
-
89700-37-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-3-[5-(4-fluorophenyl)-1,5-dioxopentyl]-4-phenyl-2-oxazolidinone + NADPH + H+
(4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one + NADP+
-
Substrates: 99.1% conversion
Products: -
Products: -
?
(R)-1-phenyl-1,2-ethanediol + NADH + H+
2-hydroxyacetophenone + NAD+
Substrates: -
Products: -
Products: -
r
1,4-benzoquinone + NADPH
? + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanol + NADP+
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanol + NADP+
1-(3-nitrosophenyl)ethan-1-one + NADPH + H+
1-(3-nitrosophenyl)ethan-1-ol + NADP+
-
Substrates: 86% conversion after 24 h, 99% R-enantiomeric excess
Products: -
Products: -
?
1-(4-chlorophenyl)ethanone + NADPH + H+
(S)-1-(4-chlorophenyl)ethanol + NADP+
-
Substrates: -
Products: 86% conversion, 99% enantiomeric excess
Products: 86% conversion, 99% enantiomeric excess
?
1-(4-nitrosophenyl)ethan-1-one + NADPH + H+
1-(4-nitrosophenyl)ethan-1-ol + NADP+
-
Substrates: 30% conversion after 24 h, 73% S-enantiomeric excess
Products: -
Products: -
?
1-adamantyl methyl ketone + NADPH + H+
1-adamantyl methyl alcohol + NADP+
-
Substrates: reduction of the sterically bulky ketone to the corresponding alcohol with excellent optical purity
Products: -
Products: -
?
1-butanal + NADPH + H+
1-butanol + NADP+
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propanedione + NADPH
? + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
1-phenylethanone + NADPH + H+
(S)-1-phenylethanol + NADP+
-
Substrates: -
Products: 60% conversion, 99% enantiomeric excess
Products: 60% conversion, 99% enantiomeric excess
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
13-deoxydoxorubicin + NADPH + H+
?
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
2 4-fluoroacetophenone + 2 NADPH + 2 H+
(1S)-1-(4-fluorophenyl)ethanol + (1R)-1-(4-fluorophenyl)ethanol + 2 NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 46% enantiomeric excess, mutant Q245H, (S)-configuration with 92%, mutant Q245P, with 90%, mutant Q245L, with 93% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 46% enantiomeric excess, mutant Q245H, (S)-configuration with 92%, mutant Q245P, with 90%, mutant Q245L, with 93% enantiomeric excess, respectively
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
Substrates: -
Products: -
Products: -
?
2'-fluoroacetophenone + NADPH + H+
? + NADP+
-
Substrates: 20.2% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
2'-methoxyacetophenone + NADPH + H+
1-(2-methoxyphenyl)ethanol + NADP+
-
Substrates: reduction of the sterically bulky ketone to the corresponding alcohol with excellent optical purity
Products: -
Products: -
?
2,2,2-trifluoro-1-phenylethan-1-one + NADPH + H+
2,2,2-trifluoro-1-phenylethan-1-ol + NADP+
2,2,2-trifluoroacetophenone + NADPH + H+
alpha-(trifluoromethyl)benzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2,2-dimethylcyclohexanone-1,3-dione + NADPH + H+
(S)-3-hydroxy-2,2-dimethylcyclohexanone + NADP+
-
Substrates: -
Products: -
Products: -
?
2,2-dimethylpropiophenone + NADPH + H+
2,2-dimethylpropiophenol + NADP+
-
Substrates: -
Products: over 90% chiral purity of the alcohol product
Products: over 90% chiral purity of the alcohol product
?
2,3-butanediol + NADP+
acetoin + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2,3-heptanedione + NADPH + H+
? + NADP+
Substrates: 18.8% of the activity with dihydroxyacetone
Products: -
Products: -
?
2,4-octanedione + NADPH + H+
(S)-2-hydroxy-4-octanone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(3,4,6-tri-[3,4,5,6-tetrahydro])phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(1,3-dioxo-1,3,4,5,6,7-hexahydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(3,5-difluoro)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(4,7-difluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(3-fluoro)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(4-fluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(3-fluoro)phthalimido-methyl-3-oxobutanoate + NADPH + H+
methyl (3R)-2-[(4-fluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(3-methoxy)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-3-hydroxy-2-[(4-methoxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(4-fluoro)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(5-fluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(4-methyl)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-3-hydroxy-2-[(5-methyl-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(4-methyl)phthalimido-methyl-3-oxobutanoate + NADPH + H+
methyl (3R)-3-hydroxy-2-[(5-methyl-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-(4-tert-butyl)phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(5-tert-butyl-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-benzoylpyridine + NADPH
(S)-alpha-phenyl-2-pyridylmethanol + NADP+
-
Substrates: highly stereoselective reaction, native and recombinant enzymes, low activity
Products: -
Products: -
?
2-bromo-aceto-2-chlorophenone + NADPH
(R)-2-bromo-1-(2-chlorophenyl)ethanol + NADP+
-
Substrates: stereospecific enzyme
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-bromo-aceto-3-chlorophenone + NADPH
(R)-2-bromo-1-(3-chlorophenyl)ethanol + NADP+
-
Substrates: stereospecific enzyme
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-bromo-aceto-4-chlorophenone + NADPH
(R)-2-bromo-1-(4-chlorophenyl)ethanol + NADP+
-
Substrates: stereospecific enzyme
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-bromo-acetophenone + NADPH
(R)-2-bromo-1-phenylethanol + NADP+
-
Substrates: i.e. phenacyl bromide, stereospecific enzyme
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-bromobenzaldehyde + NADPH + H+
2-bromobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
2-chloro-1-(3,4-dichlorophenyl)ethan-1-one + NADPH + H+
2-chloro-1-(3,4-dichlorophenyl)ethan-1-ol + NADP+
2-chloro-aceto-3-chlorophenone + NADPH
(R)-2-chloro-1-(3-chlorophenyl)ethanol + NADP+
-
Substrates: i.e. 3-chlorophenacyl chloride
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-chlorobenzaldehyde + NADPH + H+
2-chlorobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2-cyanobenzaldehyde + NADPH + H+
2-cyanobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
2-fluorobenzaldehyde + NADPH + H+
2-fluorobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
2-halo-acetophenone + NADPH
(R)-2-halo-1-phenylethanol + NADP+
-
Substrates: i.e. phenacyl halide, stereospecific enzyme
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
Products: product reacts spontaneously to the (R)-styrene oxide derivative in NaOH
?
2-hydroxy-3-butanone + NADPH
2,3-dihydroxybutanol + NADP+
Substrates: -
Products: -
Products: -
?
2-nitrobenzaldehyde + NADPH
2-nitrobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2-oxo-2-phenylacetaldehyde + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
2-oxo-2-phenylacetaldehyde + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-2-phenylacetic acid + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2-oxobutyric acid + NADPH
2-hydroxybutyric acid + NADP+
-
Substrates: low activity
Products: -
Products: -
?
2-phthalimido-ethyl-3-oxobutanoate + NADPH + H+
ethyl (3R)-2-[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3-hydroxybutanoate + NADP+
-
Substrates: reduction of the beta-keto group to stereospecifically give the (R)-alcohol
Products: -
Products: -
?
3'-fluoroacetophenone + NADPH + H+
? + NADP+
-
Substrates: 18.8% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
3,5-bis(trifluoromethyl) acetophenone + NADPH + H+
(R)-[3,5-bis(trifluoromethyl)phenyl] ethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
3-bromobenzaldehyde + NADPH + H+
3-bromobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
3-chlorobenzaldehyde + NADPH + H+
3-chlorobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzaldehyde + NADPH + H+
3-fluorobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-4-hydroxynonanal + NADP+
3-glutathionyl nonanoic-delta-lactone + NADPH + H+
Substrates: -
Products: oxidation of the hemiacetal form of 3-glutathionyl-4-hydroxynonanal, generating the 3-glutathionyl nonanoic-delta-lactone
Products: 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+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-4-hydroxynonanal hemiacetal + NADPH + H+
3-glutathionyl-gamma-nonanolactone + NADP+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-hexanal + NADPH + H+
3-glutathionyl-hexan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-nonanal + NADPH + H+
3-glutathionyl-nonan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-propanal + NADPH + H+
3-glutathionyl-propan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
3-nitroacetophenone + NADPH
1-(3-nitrophenyl)ethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzaldehyde + NADPH
3-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzaldehyde + NADPH
3-nitrobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzaldehyde + NADPH + H+
3-nitrobenzyl alcohol + NADP+
Substrates: 7.0% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
3-oxo-3-(2,4-difluorophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(2,4-difluorophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 92% yield, 98% enantiomeric excess
Products: 92% yield, 98% enantiomeric excess
?
3-oxo-3-(3-methoxyphenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(3-methoxyphenyl)propanenitrile + NADP+
-
Substrates: -
Products: 89% yield, 97% enantiomeric excess
Products: 89% yield, 97% enantiomeric excess
?
3-oxo-3-(3-nitrophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(3-nitrophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 87% yield, 99% enantiomeric excess
Products: 87% yield, 99% enantiomeric excess
?
3-oxo-3-(4-bromophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-bromophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 88% yield, 99% enantiomeric excess
Products: 88% yield, 99% enantiomeric excess
?
3-oxo-3-(4-chlorophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-chlorophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 90% yield, 99% enantiomeric excess
Products: 90% yield, 99% enantiomeric excess
?
3-oxo-3-(4-cyanophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-cyanophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 90% yield, 99% enantiomeric excess
Products: 90% yield, 99% enantiomeric excess
?
3-oxo-3-(4-fluorophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-fluorophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 90% yield, 99% enantiomeric excess
Products: 90% yield, 99% enantiomeric excess
?
3-oxo-3-(4-methylphenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-methylphenyl)propanenitrile + NADP+
-
Substrates: -
Products: 90% yield, 98% enantiomeric excess
Products: 90% yield, 98% enantiomeric excess
?
3-oxo-3-(4-nitrophenyl)propanenitrile + NADPH
(R)-3-hydroxy-3-(4-nitrophenyl)propanenitrile + NADP+
-
Substrates: -
Products: 86% yield, 99% enantiomeric excess
Products: 86% yield, 99% enantiomeric excess
?
3-oxo-3-phenylpropanenitrile + NADPH
(R)-3-hydroxy-3-phenylpropanenitrile + NADP+
-
Substrates: -
Products: 85% yield, 98% enantiomeric excess
Products: 85% yield, 98% enantiomeric excess
?
4'-fluoroacetophenone + NADPH + H+
? + NADP+
-
Substrates: 12.4% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
4-(6-methoxy-2-benzoxazolyl)acetophenone + NADPH
?
-
Substrates: -
Products: -
Products: -
?
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone + NADPH + H+
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
phenyl-4-pyridylmethanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
S-(-)-phenylpyridin-4-yl-methynol + NADP+
-
Substrates: stereoselective reduction
Products: -
Products: -
?
4-bromoacetophenone + NADPH + H+
(1S)-1-(4-bromophenyl)ethanol + (1R)-1-(4-bromophenyl)ethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 42% enantiomeric excess, mutant Q245H, (S)-configuration with 92%, mutant Q245P, with 98%, mutant Q245L, with 97% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 42% enantiomeric excess, mutant Q245H, (S)-configuration with 92%, mutant Q245P, with 98%, mutant Q245L, with 97% enantiomeric excess, respectively
?
4-bromobenzaldehyde + NADPH + H+
4-bromobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-carboxybenzaldehyde + NADPH
4-carboxybenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: reduction of 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate by transformants in an aqueous mono-phase system for 18 h, gives a molar yield of 94% and an optical purity of the (S)-isomer of more than 99% enantiomeric excess
Products: -
Products: -
?
4-chloroacetophenone + NADPH + H+
(1S)-1-(4-chlorophenyl)ethanol + (1R)-1-(4-chlorophenyl)ethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 14% enantiomeric excess, mutant Q245H, (S)-configuration with 90%, mutant Q245P, with 96%, mutant Q245L, with 96% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 14% enantiomeric excess, mutant Q245H, (S)-configuration with 90%, mutant Q245P, with 96%, mutant Q245L, with 96% enantiomeric excess, respectively
?
4-chlorobenzaldehyde + NADPH + H+
4-chlorobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-cyanobenzaldehyde + NADPH + H+
4-cyanobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-hexanoylpyridine + NADPH
1-(pyridin-4-yloxy)hexan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzaldehyde + NADPH + H+
4-hydroxybenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-methoxyacetophenone + NADPH
(1S)-1-(4-methoxyphenyl)ethanol + (1R)-1-(4-methoxyphenyl)ethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 57% enantiomeric excess, mutant Q245H, (S)-configuration with 79%, mutant Q245P, with 98%, mutant Q245L, with 96% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 57% enantiomeric excess, mutant Q245H, (S)-configuration with 79%, mutant Q245P, with 98%, mutant Q245L, with 96% enantiomeric excess, respectively
?
4-methoxybenzaldehyde + NADPH + H+
4-methoxybenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-methylacetophenone + NADPH + H+
(1S)-1-(4-methylphenyl)ethanol + (1R)-1-(4-methylphenyl)ethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 59% enantiomeric excess, mutant Q245H, (S)-configuration with 95%, mutant Q245P, with 96%, mutant Q245L, with 95% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 59% enantiomeric excess, mutant Q245H, (S)-configuration with 95%, mutant Q245P, with 96%, mutant Q245L, with 95% enantiomeric excess, respectively
?
4-methylbenzaldehyde + NADPH + H+
4-methylbenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-methylnitrosamino-1-(3-pyridyl)-1-butanone + NADPH + H+
4-methylnitrosamino-1-(3-pyridyl)-1-butanol + NADP+
-
Substrates: i.e. NNK, genotoxic compound from tobacco smoke, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184
Products: -
Products: -
r
4-nitroacetophenone + NADPH
1-(4-nitrophenyl)ethanol + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
4-oxo-2-nonenal + NADPH + H+
? + NADP+
-
Substrates: 9% of the activity with 9,10-phenanthrenequinone
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + 4-hydroxynon-2-enal + 1-hydroxynon-2-en-4-one + NADP+
-
Substrates: molecular modeling of substrate binding in the active site
Products: product identification, 4-hydroxynon-2-enal is the major product
Products: product identification, 4-hydroxynon-2-enal is the major product
?
4-pregnen-3,20-dione + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
ir
4-tert-butylacetophenone + NADPH + H+
(1S)-1-(4-tert-butylphenyl)ethanol + (1R)-1-(4-tert-butylphenyl)ethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 31% enantiomeric excess, mutant Q245H, (S)-configuration with 96%, mutant Q245P, with 99%, mutant Q245L, with 99% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 31% enantiomeric excess, mutant Q245H, (S)-configuration with 96%, mutant Q245P, with 99%, mutant Q245L, with 99% enantiomeric excess, respectively
?
5alpha-androstane-3alpha,17beta-diol + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
r
5alpha-dihydrotestosterone + NADPH
?
-
Substrates: only enzyme form CR1
Products: -
Products: -
?
5beta-dihydrotestosterone + NADPH
?
-
Substrates: only enzyme form CR1
Products: -
Products: -
?
5beta-pregnan-3beta-ol-20-one + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
r
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+
Substrates: selective substrate of human carbonyl reductase 1
Products: -
Products: -
?
9,10-phenanthroline + NADPH + H+
?
-
Substrates: stereoselective reduction
Products: -
Products: -
?
9-cis-retinal + NADPH
9-cis-retinol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
9-cis-retinal + NADPH + H+
9-cis-retinol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetophenone + NADH + H+
(R)-1-phenylethan-1-ol + NAD+
Substrates: -
Products: -
Products: -
?
acetophenone + NADPH + H+
(1S)-1-phenylethanol + (1R)-1-phenylethanol + NADP+
-
Substrates: -
Products: wild-type, (R)-configuration of product with 42% enantiomeric excess, mutant Q245H, (S)-configuration with 78%, mutant Q245P, with 64%, mutant Q245L, with 82% enantiomeric excess, respectively
Products: wild-type, (R)-configuration of product with 42% enantiomeric excess, mutant Q245H, (S)-configuration with 78%, mutant Q245P, with 64%, mutant Q245L, with 82% enantiomeric excess, respectively
?
all-trans retinal + NADPH + H+
all-trans retinol + NADP+
-
Substrates: -
Products: -
Products: -
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH
-
Substrates: -
Products: -
Products: -
r
alpha-acetoxyacetophenone + NADPH + H+
?
-
Substrates: -
Products: -
Products: -
?
alpha-bromoacetophenone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
alpha-chloroacetophenone + NADPH + H+
? + NADP+
-
Substrates: 40.6% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADPH
benzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
benzoylformic acid ethyl ester + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
r
bupropion + NADPH + H+
erythrohydrobupropion + NADP+
-
Substrates: -
Products: in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
Products: in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
?
bupropion + NADPH + H+
threohydrobupropion + NADP+
-
Substrates: -
Products: in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
Products: in liver cytosol, antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion
?
butyrophenone + NADPH + H+
(1S)-1-phenylbutan-1-ol + NADP+
-
Substrates: -
Products: over 90% chiral purity of the alcohol product
Products: over 90% chiral purity of the alcohol product
?
chloromethyl 3-oxobutyrate + NADPH + H+
chloromethyl (S)-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 97% purity of the S-enantiomer
Products: 97% purity of the S-enantiomer
?
cinnamaldehyde + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
cycloheptanone + NADPH + H+
cycloheptanol + NADP+
-
Substrates: -
Products: -
Products: -
?
cyclohex-2-en-1-ol + NADPH
cyclohex-2-en-1-one + NADP+
-
Substrates: -
Products: -
Products: -
?
cyclohexanol + NADP+
cyclohexanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cyclopentanol + NADP+
cyclopentanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cyclopentanone + NADPH
cyclopentanol + NADP+
-
Substrates: low activity
Products: -
Products: -
?
D-xylose + NADPH
? + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: very low activity
Products: -
Products: -
ir
DELTA4-androstan-17beta-ol-3-one + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
r
dihydroxyacetone + NADPH + H+
glycerol + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-chloro-3-oxobutanoate + NADPH + H+
(S)-ethyl 2-chloro-3-hydroxybutanoate + NADP+
Substrates: 135.7% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
ethyl 2-chloro-3-oxobutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-chloro-3-oxobutanoate + NADPH + H+
ethyl 2-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 2-chloro-3-oxobutanoate + NADPH + H+
ethyl-2-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 2-methyl-3-oxobutanoate + NADPH + H+
ethyl 3-hydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-3-phenylpropanoate + NADPH + H+
ethyl 2-hydroxy-3-phenylpropanoate + NADP+
Substrates: 128% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutanoate + NADPH + H+
ethyl (2S)-2-hydroxy-4-phenylbutanoate + NADP+
Substrates: 576% of the activity with 2-chloroacetophenone
Products: 100% conversion, 85.7% enantiomeric excess
Products: 100% conversion, 85.7% enantiomeric excess
?
ethyl 2-oxobutanoate + NADPH + H+
ethyl 2-hydroxybutanoate + NADP+
-
Substrates: 16% activity compared to ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
r
ethyl 2-oxophenylacetate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxopropanoate + NADPH + H+
ethyl 2-hydroxypropanoate + NADP+
Substrates: 41% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
ethyl 3,3-dimethyl-2-oxobutanoate + NADPH + H+
ethyl 3,3-dimethyl-2-hydroxybutanoate + NADP+
-
Substrates: reduction of the sterically bulky ketone to the corresponding alcohol with excellent optical purity
Products: -
Products: -
?
ethyl 3,3-dimethyl-2-oxobutyrate + NADPH + H+
(S)-ethyl 3,3-dimethyl-2-hydroxybutyrate + NADP+
-
Substrates: stereoselective reaction
Products: over 90% chiral purity of the alcohol product
Products: over 90% chiral purity of the alcohol product
?
ethyl 3-methyl-2-oxobutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 3-methyl-2-oxobutanoate + NADPH + H+
ethyl (2R)-2-hydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: 95% conversion, 98.3% enantiomeric excess
Products: 95% conversion, 98.3% enantiomeric excess
?
ethyl 3-oxo-3-phenylpropionate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 3-oxobutanoate + NADPH
ethyl 3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 3-oxobutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 3-oxobutanoate + NADPH + H+
ethyl 3-hydroxybutanoate + NADP+
Substrates: 25.2% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
ethyl 3-oxobutyrate + NADPH + H+
ethyl (R,S)-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 61% S-enantiomer
Products: 61% S-enantiomer
?
ethyl 3-oxopentanoate + NADPH + H+
ethyl (R,S)-3-hydroxypentanoate + NADP+
-
Substrates: -
Products: 61% S-enantiomer
Products: 61% S-enantiomer
?
ethyl 3-oxopentanoate + NADPH + H+
ethyl (S)-3-hydroxypentanoate + NADP+
-
Substrates: -
Products: 99% conversion, 99% enantiomeric excess
Products: 99% conversion, 99% enantiomeric excess
?
ethyl 4,4,4-trifluoro-3-oxobutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4,4,4-trifluoro-3-oxobutanoate + NADPH + H+
ethyl (3R)-4,4,4-trifluoro-3-hydroxybutanoate + NADP+
Substrates: 74% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
ethyl 4,4,4-trifluoro-3-oxobutanoate + NADPH + H+
ethyl (3S)-4,4,4-trifluoro-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 90% purity of the S-enantiomer
Products: 90% purity of the S-enantiomer
?
ethyl 4,4-dimethyl-3-oxopentanoate + NADPH + H+
ethyl 4,4-dimethyl-3-hydroxypentanoate + NADP+
-
Substrates: reduction of the sterically bulky ketone to the corresponding alcohol with excellent optical purity
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (R)-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: 99% conversion, 92% enantiomeric excess
Products: 99% conversion, 92% enantiomeric excess
Products: 99% conversion, 92% enantiomeric excess
?
ethyl 4-chloroacetoacetate + NADPH + H+
? + NADP+
-
Substrates: 76.9% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
ethyl 5-oxohexanoate + NADPH
ethyl-5-hydroxyhexanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl benzoylformate + NADPH + H+
? + NADP+
-
Substrates: 90.8% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
ethyl pyruvate + NADPH + H+
ethyl (2S)-2-hydroxypropanoate + NADP+
Substrates: 7821% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
ethyl pyruvate + NADPH + H+
ethyl lactate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl-2-oxo-2-phenylacetate + NADH + H+
(RS)-ethyl-2-hydroxy-2-phenylacetate + NAD+
Substrates: 86% conversion
Products: -
Products: -
?
ethyl-2-oxo-2-phenylacetate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
ethyl-2-oxo-2-phenylacetate + NADPH + H+
(RS)-ethyl-2-hydroxy-2-phenylacetate + NADP+
Substrates: 100% conversion, 70% S-enantiomeric excess
Products: -
Products: -
?
ethyl-2-oxo-2-phenylacetate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl-4,4,4-trifloro-3-oxo-butanoate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
ethyl-4,4,4-trifloro-3-oxo-butanoate + NADPH + H+
(R)-ethyl-4,4,4-trifluoro-3-hydroxybutanoate + NADP+
ethyl-4,4,4-trifloro-3-oxo-butanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethylpyruvate + NADPH
? + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: low activity
Products: -
Products: -
ir
furfural + NADPH + H+
furfuryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
glutaraldehyde + NADPH
? + NADP+
-
Substrates: low activity
Products: -
Products: -
?
glutathione-4-oxononanal + NADPH + H+
glutathione-4-hydroxynonanal + NADP+
-
Substrates: conjugate, molecular modeling of substrate binding in the active site
Products: -
Products: -
?
heptanal + NADPH + H+
heptan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
hexaphenone + NADPH
1-phenylhexan-1-ol + NADP+
-
Substrates: native and recombinant enzymes
Products: -
Products: -
?
hydroxyacetone + NADPH
? + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: low activity
Products: -
Products: -
ir
hydroxyacetophenone + NAD+
(R)-1-phenyl-1,2-ethanediol + NADH + H+
Substrates: -
Products: -
Products: -
?
isoamyl pyruvate + NADPH + H+
isoamyl lactate + NADP+
Substrates: -
Products: -
Products: -
?
isopropyl 3-oxobutyrate + NADPH + H+
isopropyl (S)-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 99% purity of the S-enantiomer
Products: 99% purity of the S-enantiomer
?
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
ketopantoyl lactone + NADPH
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
methyl 2-chloro-3-oxobutanoate + NADPH + H+
(S)-methyl 2-chloro-3-hydroxybutanoate + NADP+
methyl 2-oxo-4-phenylbutanoate + NADPH + H+
methyl (R)-2-hydroxy-4-phenylbutanoate + NADP+
methyl 2-oxopropanoate + NADPH + H+
methyl (2S)-2-hydroxypropanoate + NADP+
Substrates: -
Products: 67% conversion, 99.9% enantiomeric excess
Products: 67% conversion, 99.9% enantiomeric excess
?
methyl 4-chloro-3-oxobutanoate + NADPH + H+
(S)-methyl 4-chloro-3-hydroxybutanoate + NADP+
Substrates: 25.4% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
methyl 4-chloro-3-oxobutanoate + NADPH + H+
methyl 4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: 9% activity compared to ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
r
methyl 4-chloroacetoacetate + NADPH
methyl (S)-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: highly enantioselective reduction
Products: -
Products: -
ir
methyl benzoylformate + NADPH + H+
? + NADP+
-
Substrates: 79.4% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
methyl glyoxal + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
methyl pyruvate + NADPH
methyl lactate + NADP+
-
Substrates: -
Products: -
Products: -
?
methyl-2-oxobutanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
methyl-2-oxopropanoate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
methylglyoxal + NADPH
? + NADP+
-
Substrates: very low activity
Products: -
Products: -
ir
N,N-dimethyl-3-keto-2-thienyl-propanamine + NADPH
(S)-N,N-dimethyl-3-keto-2-thienyl-propanamine + NADP+
-
Substrates: -
Products: key intermediate in synthesis of (S)-duloxetine
Products: key intermediate in synthesis of (S)-duloxetine
?
N,N-dimethyl-3-keto-3-(2-thienyl)-1-keto propanamine + NADPH + H+
(S)-3-(dimethylamino)-1-(2-thienyl)-1-propanol + NADP+
-
Substrates: mutant enzyme A89N/F154Y with yield of 91.2% and S-enantiomeric excess of 99.9%
Products: -
Products: -
?
n-hexylaldehyde + NADPH
n-hexanol + NADP+
-
Substrates: low activity
Products: -
Products: -
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
nonanophenone + NADPH
1-phenylnonan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
octanal + NADPH + H+
octan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
octyl 4-chloro-3-oxobutanoate + NADPH
octyl 4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
octyl 4-chloro-3-oxobutanoate + NADPH
octyl-4-chloro-3-hydroxybutanoate + NADP+
Candida macedoniensis
-
Substrates: -
Products: -
Products: -
?
oracin + NADPH + H+
11-dihydrooracin + NADP+
Substrates: -
Products: -
Products: -
?
p-anisaldehyde + NADPH + H+
p-anisalcohol + NADP+
Substrates: -
Products: -
Products: -
?
phenyl 3-oxobutyrate + NADPH + H+
phenyl (S,R)-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 56% S-enantiomer
Products: 56% S-enantiomer
?
phenyl cyclopropyl ketone + NADPH + H+
?
-
Substrates: -
Products: -
Products: -
?
phenylglyoxal + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
polyketid + NADPH
?
-
Substrates: enzyme acts on the nascent polyketid chain from polyketid synthase reaction and reduces the carbonyl group at C-9
Products: -
Products: -
?
propionaldehyde + NADPH
propanol + NADP+
-
Substrates: low activity
Products: -
Products: -
?
prostaglandin A1 + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
prostaglandin A2 + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
prostaglandin D2 + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
prostaglandin F2alpha + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
pyridin-4-carboxyaldehyde + NADPH
pyridin-4-ylmethanol + NADP+
-
Substrates: artificial substrate
Products: -
Products: -
?
pyridine-3-aldehyde + NADPH
pyridin-3-ylbutanol + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
t-butyl 6-cyano-(5R)-hydroxy-3-oxohexanoate + NADPH + H+
t-butyl 6-cyano-(3R,5R)-dihydroxyhexanoate + NADP+
tert-butyl 3-oxobutyrate + NADPH + H+
tert-butyl (S)-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: 99% purity of the S-enantiomer
Products: 99% purity of the S-enantiomer
?
trans-4-phenyl-3-buten-2-one + NADPH
trans-4-phenyl-3-buten-2-ol + NADP+
-
Substrates: also reacts with NADH, produces only R-enatiomer
Products: -
Products: -
?
valeraldehyde + NADPH + H+
pentan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
(R)-2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(R)-2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
1,4-naphthoquinone + NADPH + H+
? + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanol + NADP+
F1N8Y3
Substrates: i.e. mequindox, synthetic quinoxaline derivative, inhibitory to several Gram-positive and Gram-negative bactria
Products: -
Products: -
?
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-1,4-dioxidoquinoxalin-2-yl)ethanol + NADP+
Substrates: i.e. mequindox, synthetic quinoxaline derivative, inhibitory to several Gram-positive and Gram-negative bacteria
Products: -
Products: -
?
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanol + NADP+
F1N8Y3
Substrates: -
Products: -
Products: -
?
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanone + NADPH + H+
1-(3-methyl-4-oxidoquinoxalin-2-yl)ethanol + NADP+
Substrates: -
Products: -
Products: -
?
1-(4-chlorophenyl)ethan-1-one + NADPH + H+
1-(4-chlorophenyl)ethan-1-ol + NADP+
-
Substrates: 41% conversion after 24 h, 99% S-enantiomeric excess
Products: -
Products: -
?
1-(4-chlorophenyl)ethan-1-one + NADPH + H+
1-(4-chlorophenyl)ethan-1-ol + NADP+
-
Substrates: 41% conversion after 24 h, 99% S-enantiomeric excess
Products: -
Products: -
?
1-acetonaphtone + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADPH + H+
(R)-1-phenyl-2-hydroxy-1-propanone + NADP+
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADPH + H+
(R)-1-phenyl-2-hydroxy-1-propanone + NADP+
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADPH + H+
(S)-1-phenyl-2-hydroxy-1-propanone + NADP+
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADPH + H+
(S)-1-phenyl-2-hydroxy-1-propanone + NADP+
Substrates: -
Products: -
Products: -
?
1-phenylethan-1-one + NADPH + H+
1-phenylethan-1-ol + NADP+
-
Substrates: 75% conversion after 24 h, 99% S-enantiomeric excess
Products: -
Products: -
?
1-phenylethan-1-one + NADPH + H+
1-phenylethan-1-ol + NADP+
-
Substrates: 75% conversion after 24 h, 99% S-enantiomeric excess
Products: -
Products: -
?
1-phenylisatin + NADPH
? + NADP+
-
Substrates: high activity, recombinant enzyme
Products: -
Products: -
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
2,2,2-trifluoro-1-phenylethan-1-one + NADPH + H+
2,2,2-trifluoro-1-phenylethan-1-ol + NADP+
-
Substrates: 99.6% conversion after 24 h, 91.5% R-enantiomeric excess
Products: -
Products: -
?
2,2,2-trifluoro-1-phenylethan-1-one + NADPH + H+
2,2,2-trifluoro-1-phenylethan-1-ol + NADP+
-
Substrates: 99.6% conversion after 24 h, 91.5% R-enantiomeric excess
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
-
Substrates: 126.2% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Substrates: the preferred substrate is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
Products: -
Products: -
r
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Substrates: best substrate, 462% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Substrates: the preferred substrate is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
Products: -
Products: -
r
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Substrates: best substrate, 462% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: the preferred substrate is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
Products: -
Products: -
r
2,2,2-trifluoroacetophenone + NADPH + H+
(1S)-2,2,2-trifluoro-1-phenylethanol + NADP+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: best substrate, 462% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADPH + H+
(R)-2,2,2-trifluoro-1-phenylethanol + NADP+
Substrates: 140% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
2,2,2-trifluoroacetophenone + NADPH + H+
(R)-2,2,2-trifluoro-1-phenylethanol + NADP+
Bacillus sp. (in: firmicutes) ECU0013
Substrates: 140% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
2,3-butanedione + NADPH
? + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: -
Products: -
Products: -
ir
2,3-butanedione + NADPH
? + NADP+
-
Substrates: low activity
Products: -
Products: -
ir
2,3-butanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-butanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-butanedione + NADPH + H+
? + NADP+
Substrates: 35.2% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
2,3-heptandione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-hexandione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-hexanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-hexanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-hexanedione + NADPH + H+
? + NADP+
Substrates: 17.3% of the activity with dihydroxyacetone
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
(R)-2-hydroxy-pentane-3-one + NADP+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
(R)-2-hydroxy-pentane-3-one + NADP+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
(S)-2-hydroxy-pentane-3-one + NADP+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
(S)-2-hydroxy-pentane-3-one + NADP+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
? + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: low activity
Products: -
Products: -
ir
2,3-pentanedione + NADPH + H+
? + NADP+
Substrates: 58.6% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
2,4-dichlorobenzaldehyde + NADPH + H+
2,4-dichlorobenzyl alcohol + NADP+
Substrates: lowest activity
Products: -
Products: -
?
2,4-dichlorobenzaldehyde + NADPH + H+
2,4-dichlorobenzyl alcohol + NADP+
Substrates: lowest activity
Products: -
Products: -
?
2,5-diketo-D-gluconate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,5-diketo-D-gluconate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-butanol + NADP+
2-butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-butanone + NADPH
2-butanol + NADP+
-
Substrates: low activity
Products: -
Products: -
?
2-chloro-1-(3,4-dichlorophenyl)ethan-1-one + NADPH + H+
2-chloro-1-(3,4-dichlorophenyl)ethan-1-ol + NADP+
-
Substrates: 41% conversion after 24 h, 99% R-enantiomeric excess
Products: -
Products: -
?
2-chloro-1-(3,4-dichlorophenyl)ethan-1-one + NADPH + H+
2-chloro-1-(3,4-dichlorophenyl)ethan-1-ol + NADP+
-
Substrates: 41% conversion after 24 h, 99% R-enantiomeric excess
Products: -
Products: -
?
2-chloroacetophenone + NADPH + H+
(R)-2-chloro-1-phenylethanol + NADP+
Substrates: -
Products: 74.5% conversion, 99% enantiomeric excess
Products: 74.5% conversion, 99% enantiomeric excess
?
2-chloroacetophenone + NADPH + H+
(R)-2-chloro-1-phenylethanol + NADP+
Bacillus sp. (in: firmicutes) ECU0013
Substrates: -
Products: 74.5% conversion, 99% enantiomeric excess
Products: 74.5% conversion, 99% enantiomeric excess
?
2-chloroacetophenone + NADPH + H+
(RS)-2-chloro-1-phenylethan-1-ol + NADP+
Substrates: 100% conversion
Products: -
Products: -
?
2-chloroacetophenone + NADPH + H+
(RS)-2-chloro-1-phenylethan-1-ol + NADP+
Substrates: 100% conversion
Products: -
Products: -
?
2-chlorobenzaldehyde + NADPH + H+
2-chlorobenzyl alcohol + NADP+
Candida macedoniensis
-
Substrates: -
Products: -
Products: -
?
2-chlorobenzaldehyde + NADPH + H+
2-chlorobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
-
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
Starmerella magnoliae AKU4643
-
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADPH + H+
(R)-1-phenyl-1,2-ethanediol + NADP+
Substrates: -
Products: product of mutant enzyme S67D/H68D, 95.4% purity
Products: product of mutant enzyme S67D/H68D, 95.4% purity
?
2-hydroxyacetophenone + NADPH + H+
(R)-1-phenyl-1,2-ethanediol + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADPH + H+
(RS)-1-phenyl-1,2-ethanediol + NADP+
Substrates: 100% conversion, more than 99% S-enantiomeric excess
Products: -
Products: -
?
2-hydroxyacetophenone + NADPH + H+
(RS)-1-phenyl-1,2-ethanediol + NADP+
Substrates: 100% conversion, more than 99% S-enantiomeric excess
Products: -
Products: -
?
2-hydroxyacetophenone + NADPH + H+
(S)-1-phenyl-1,2-ethanediol + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxyacetophenone + NADPH + H+
(S)-1-phenyl-1,2-ethanediol + NADP+
Substrates: -
Products: product of wild-type enzyme, 96.2% purity
Products: product of wild-type enzyme, 96.2% purity
?
2-hydroxyacetophenone + NADPH + H+
(S)-1-phenyl-1,2-ethanediol + NADP+
Substrates: -
Products: -
Products: -
?
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
Candida macedoniensis
-
Substrates: -
Products: -
Products: -
?
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2-octanone + NADPH + H+
? + NADP+
-
Substrates: 64.6% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
2-octanone + NADPH + H+
? + NADP+
-
Substrates: 64.6% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
2-oxo-2-phenylacetaldehyde + NADPH + H+
(S)-1-phenylethane-1,2-diol + NADP+
Substrates: 11% conversion, more than 99% S-enantiomeric excess
Products: -
Products: -
?
2-oxo-2-phenylacetaldehyde + NADPH + H+
(S)-1-phenylethane-1,2-diol + NADP+
Substrates: 11% conversion, more than 99% S-enantiomeric excess
Products: -
Products: -
?
2-oxo-4-phenylbutanoate + NADPH + H+
(R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: 77.1% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
2-oxo-4-phenylbutanoate + NADPH + H+
(R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: 77.1% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
2-pentanol + NADP+
2-pentanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-pentanol + NADP+
2-pentanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-propanol + NADP+
propanone + NADPH + H+
-
Substrates: -
Products: 2-propanone i.e. acetone
Products: 2-propanone i.e. acetone
r
2-propanol + NADP+
propanone + NADPH + H+
-
Substrates: -
Products: 2-propanone i.e. acetone
Products: 2-propanone i.e. acetone
r
3,4-hexandione + NADPH + H+
? + NADP+
Substrates: low activity
Products: -
Products: -
?
3,4-hexandione + NADPH + H+
? + NADP+
Substrates: low activity
Products: -
Products: -
?
3-benzoylpyridine + NADPH
(S)-alpha-phenyl-3-pyridylmethanol + NADP+
-
Substrates: highly stereoselective reaction, native and recombinant enzymes
Products: -
Products: -
?
3-benzoylpyridine + NADPH
(S)-alpha-phenyl-3-pyridylmethanol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
3-bromoacetophenone + NADPH + H+
1-(3-bromophenyl)ethanol + NADP+
-
Substrates: 61% conversion after 24 h
Products: -
Products: -
?
3-bromoacetophenone + NADPH + H+
1-(3-bromophenyl)ethanol + NADP+
-
Substrates: 61% conversion after 24 h
Products: -
Products: -
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
-
Substrates: -
Products: -
Products: -
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
Substrates: -
Products: -
Products: -
?
3-glutathionyl-4-hydroxynonanal + NADPH + H+
3-glutathionyl-1,4-dihydroxynonane + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzaldehyde + NADPH + H+
3-hydroxybenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxybenzaldehyde + NADPH + H+
3-hydroxybenzyl alcohol + NADP+
Substrates: 7.1% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
4'-chloroacetophenone + NADPH + H+
(S)-1-(4-chlorophenyl)ethanol + NADP+
Substrates: 64% of the activity with 2-chloroacetophenone
Products: 49.6% conversion, 99% enantiomeric excess
Products: 49.6% conversion, 99% enantiomeric excess
?
4'-chloroacetophenone + NADPH + H+
(S)-1-(4-chlorophenyl)ethanol + NADP+
Bacillus sp. (in: firmicutes) ECU0013
Substrates: 64% of the activity with 2-chloroacetophenone
Products: 49.6% conversion, 99% enantiomeric excess
Products: 49.6% conversion, 99% enantiomeric excess
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
ir
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: highly stereoselective reaction, native and recombinant enzymes
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-alpha-phenyl-4-pyridylmethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-phenyl(pyridin-4-yl)methanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-phenyl(pyridin-4-yl)methanol + NADP+
Substrates: -
Products: -
Products: -
?
4-benzoylpyridine + NADPH + H+
(S)-phenyl(pyridin-4-yl)methanol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-bromobenzaldehyde + NADPH + H+
(4-bromophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-bromobenzaldehyde + NADPH + H+
(4-bromophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-chlorobenzaldehyde + NADPH + H+
(4-chlorophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-chlorobenzaldehyde + NADPH + H+
(4-chlorophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-fluorobenzaldehyde + NADPH + H+
(4-fluorophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-fluorobenzaldehyde + NADPH + H+
(4-fluorophenyl)methanol + NADP+
-
Substrates: 99% conversion
Products: -
Products: -
?
4-hexanoylpyridine + NADPH + H+
1-(pyridin-4-yloxy)hexan-1-ol + NADP+
-
Substrates: native and recombinant enzymes
Products: -
Products: -
?
4-hexanoylpyridine + NADPH + H+
1-(pyridin-4-yloxy)hexan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
4-nitroacetophenone + NADPH
?
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: artificial substrate
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzylalcohol + NADP+
-
Substrates: native and recombinant enzymes
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
1-hydroxynon-2-en-4-one + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
1-hydroxynon-2-en-4-one + NADP+
-
Substrates: -
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-hydroxynon-2-enal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-hydroxynon-2-enal + NADP+
-
Substrates: -
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
5alpha-androstan-17beta-ol-3-one + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
ir
5alpha-androstane-17beta-ol-3-one + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
5alpha-androstane-17beta-ol-3-one + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
5alpha-androstane-17beta-ol-3-one + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3,17-dione + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
ir
5alpha-androstane-3,17-dione + NADPH
?
-
Substrates: only enzyme forms CR2, CR8
Products: -
Products: -
?
5alpha-androstane-3,17-dione + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3,17-dione + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
5beta-androstan-17beta-ol-3-one + NADPH
?
-
Substrates: only enzyme forms CR2, CR8
Products: -
Products: -
?
5beta-androstane-3,17-dione + NADPH
?
-
Substrates: isozymes CHCR1-3
Products: -
Products: -
ir
5beta-androstane-3,17-dione + NADPH
?
-
Substrates: only enzyme form CR1
Products: -
Products: -
?
5beta-pregnan-3alpha-ol-20-one + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
r
9,10-phenanthrenequinone + NADPH
? + NADP+
-
Substrates: artificial substrate
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH
? + NADP+
-
Substrates: best substrate, recombinant enzyme
Products: -
Products: -
r
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
acetone + NADPH + H+
propan-2-ol + NADP+
-
Substrates: 20.2% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
acetone + NADPH + H+
propan-2-ol + NADP+
-
Substrates: 20.2% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
acetophenone + NADPH + H+
(1S)-1-phenylethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetophenone + NADPH + H+
(1S)-1-phenylethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetophenone + NADPH + H+
(R)-1-phenylethan-1-ol + NADP+
Substrates: 88.5% conversion, 35% R-enantiomeric excess
Products: -
Products: -
?
acetophenone + NADPH + H+
(R)-1-phenylethan-1-ol + NADP+
Substrates: 88.5% conversion, 35% R-enantiomeric excess
Products: -
Products: -
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
Substrates: -
Products: -
Products: -
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: highest activity
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: highest activity
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: 43% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
-
Substrates: -
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
Substrates: -
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
J9P7P2
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: -
Products: -
Products: -
?
diacetyl + NADPH + H+
(3S)-acetoin + NADP+
-
Substrates: -
Products: no synthesis of (2S,3S)-2,3-butanediol
Products: no synthesis of (2S,3S)-2,3-butanediol
?
diacetyl + NADPH + H+
(3S)-acetoin + NADP+
-
Substrates: -
Products: no synthesis of (2S,3S)-2,3-butanediol
Products: no synthesis of (2S,3S)-2,3-butanediol
?
diacetyl + NADPH + H+
acetoin + NADP+
-
Substrates: -
Products: -
Products: -
?
dihydroxyacetone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: CBR1 is a predominant hepatic doxorubicin reductase
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: -
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: -
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-methylacetoacetate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-methylacetoacetate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-methylacetoacetate + NADPH + H+
? + NADP+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-3-phenylpyruvate + NADPH + H+
ethyl 2-hydroxy-3-phenylpyruvate + NADP+
-
Substrates: 97.7% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
ethyl 2-oxo-3-phenylpyruvate + NADPH + H+
ethyl 2-hydroxy-3-phenylpyruvate + NADP+
-
Substrates: 97.7% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutanoate + NADPH + H+
ethyl (R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutanoate + NADPH + H+
ethyl (R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutyrate + NADPH + H+
? + NADP+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutyrate + NADPH + H+
ethyl 2-hydroxy-4-phenylbutyrate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 2-oxo-4-phenylbutyrate + NADPH + H+
ethyl 2-hydroxy-4-phenylbutyrate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 3-oxobutanoate + NADPH + H+
ethyl (3S)-3-hydroxybutanoate + NADP+
Substrates: 145% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
ethyl 3-oxobutanoate + NADPH + H+
ethyl (3S)-3-hydroxybutanoate + NADP+
Bacillus sp. (in: firmicutes) ECU0013
Substrates: 145% of the activity with 2-chloroacetophenone
Products: 100% conversion, 99% enantiomeric excess
Products: 100% conversion, 99% enantiomeric excess
?
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+
-
Substrates: stereospecific reaction, formation of a hydrophobic channel induced by NADPH binding, structure overview
Products: optically pure (S)-enantiomer
Products: optically pure (S)-enantiomer
?
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+
-
Substrates: stereospecific reaction
Products: optically pure (S)-enantiomer
Products: optically pure (S)-enantiomer
?
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+
Starmerella magnoliae AKU4643
-
Substrates: stereospecific reaction
Products: optically pure (S)-enantiomer
Products: optically pure (S)-enantiomer
?
ethyl 4-chloro-3-oxobutanoate + NADPH
ethyl-4-chloro-3-hydroxybutanoate + NADP+
Candida macedoniensis
-
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH
ethyl-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH
ethyl-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: only produces S-enantiomer
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
(S)-ethyl 4-chloro-3-hydroxybutanoate + NADP+
Cylindrocarpon sclerotigenum
-
Substrates: highly stereoselective reduction
Products: -
Products: -
ir
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
(S)-ethyl 4-chloro-3-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (3R)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: 8776% of the activity with 2-chloroacetophenone
Products: 100% conversion, 62% enantiomeric excess
Products: 100% conversion, 62% enantiomeric excess
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (3R)-4-chloro-3-hydroxybutanoate + NADP+
Bacillus sp. (in: firmicutes) ECU0013
Substrates: 8776% of the activity with 2-chloroacetophenone
Products: 100% conversion, 62% enantiomeric excess
Products: 100% conversion, 62% enantiomeric excess
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (3S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (3S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: enantioselectivity shows a strong dependence on temperature. Under optimal conditions of -3°C, (S)-4-chloro-3-hydroxybutanoate in 98% enantiomeric excess is produced
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: the enantioselectivity of NcCR for the reduction of ethyl 4-chloro-3-oxobutanoate shows a strong dependence on temperature. The enantiomeric excess is substantially increased by decreasing the temperature from 40°C (78.8%) to -3°C (98.0%)
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Starmerella magnoliae AKU4643
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl 4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl 4-chloro-3-hydroxybutanoate + NADP+
Substrates: 384% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: enantioselective reduction
Products: -
Products: -
ir
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: highly enantioselective reduction
Products: -
Products: -
ir
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl S-4-chloro-3-hydroxybutyrate + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl S-4-chloro-3-hydroxybutyrate + NADP+
-
Substrates: 100% activity
Products: -
Products: -
?
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl S-4-chloro-3-hydroxybutyrate + NADP+
-
Substrates: 100% activity
Products: -
Products: -
?
ethyl acetoacetate + NADPH + H+
ethyl S-3-hydroxybutyrate + NADP+
-
Substrates: 23.7% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
ethyl acetoacetate + NADPH + H+
ethyl S-3-hydroxybutyrate + NADP+
-
Substrates: 23.7% activity compared to ethyl 4-chloroacetoacetate
Products: -
Products: -
?
ethyl pyruvate + NADPH + H+
ethyl 2-hydroxypropanoic acid + NADP+
-
Substrates: -
Products: -
Products: -
?
ethyl pyruvate + NADPH + H+
ethyl 2-hydroxypropanoic acid + NADP+
-
Substrates: 24% activity compared to ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
r
ethyl-2-oxo-4-phenylbutanoate + NADH + H+
(RS)-ethyl-2-hydroxy-4-phenylbutanoate + NAD+
Substrates: 84% conversion
Products: -
Products: -
?
ethyl-2-oxo-4-phenylbutanoate + NADH + H+
(RS)-ethyl-2-hydroxy-4-phenylbutanoate + NAD+
Substrates: 84% conversion
Products: -
Products: -
?
ethyl-2-oxo-4-phenylbutanoate + NADPH + H+
(R)-ethyl-2-hydroxy-4-phenylbutanoate + NADP+
Substrates: 92% conversion, more than 99% R-enantiomeric excess
Products: -
Products: -
?
ethyl-2-oxo-4-phenylbutanoate + NADPH + H+
(R)-ethyl-2-hydroxy-4-phenylbutanoate + NADP+
Substrates: 92% conversion, more than 99% R-enantiomeric excess
Products: -
Products: -
?
ethyl-2-oxo-4-phenylbutanoate + NADPH + H+
(RS)-ethyl-2-hydroxy-4-phenylbutanoate + NADP+
Substrates: 98% conversion, 70% S-enantiomeric excess
Products: -
Products: -
?
ethyl-2-oxo-4-phenylbutanoate + NADPH + H+
(RS)-ethyl-2-hydroxy-4-phenylbutanoate + NADP+
Substrates: 98% conversion, 70% S-enantiomeric excess
Products: -
Products: -
?
ethyl-4,4,4-trifloro-3-oxo-butanoate + NADPH + H+
(R)-ethyl-4,4,4-trifluoro-3-hydroxybutanoate + NADP+
Substrates: 15% conversion, 69% R-enantiomeric excess
Products: -
Products: -
?
ethyl-4,4,4-trifloro-3-oxo-butanoate + NADPH + H+
(R)-ethyl-4,4,4-trifluoro-3-hydroxybutanoate + NADP+
Substrates: 15% conversion, 69% R-enantiomeric excess
Products: -
Products: -
?
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
Substrates: -
Products: -
Products: -
?
heptanophenone + NADPH
1-phenylheptan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
heptanophenone + NADPH
1-phenylheptan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
hexanal + NADPH + H+
hexan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
hexanal + NADPH + H+
hexan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
hexanal + NADPH + H+
hexan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
hexanophenone + NADPH
1-phenylhexan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
hexanophenone + NADPH
1-phenylhexan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
hydroxyacetone + NADPH + H+
glycerol + NADP+
Substrates: -
Products: -
Products: -
?
hydroxyacetone + NADPH + H+
glycerol + NADP+
Substrates: -
Products: -
Products: -
?
isatin + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
isatin + NADPH + H+
3-hydroxy-2-oxoindole + NADP+
Substrates: -
Products: -
Products: -
?
isatin + NADPH + H+
3-hydroxy-2-oxoindole + NADP+
Substrates: -
Products: -
Products: -
?
isatin + NADPH + H+
3-hydroxy-2-oxoindole + NADP+
Substrates: -
Products: -
Products: -
?
isatin + NADPH + H+
3-hydroxy-2-oxoindole + NADP+
Substrates: 17.7% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
menadione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
menadione + NADPH
? + NADP+
-
Substrates: artificial substrate
Products: -
Products: -
?
menadione + NADPH
? + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
menadione + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
menadione + NADPH + H+
?
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
menadione + NADPH + H+
? + NADP+
-
Substrates: 48% of the activity with 9,10-phenanthrenequinone
Products: -
Products: -
?
methyl 2-chloro-3-oxobutanoate + NADPH + H+
(S)-methyl 2-chloro-3-hydroxybutanoate + NADP+
Substrates: 25.1% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
methyl 2-chloro-3-oxobutanoate + NADPH + H+
(S)-methyl 2-chloro-3-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
methyl 2-oxo-3-phenylpropanoate + NADPH + H+
methyl 2-hydroxy-3-phenylpropanoate + NADP+
-
Substrates: 86.3% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
methyl 2-oxo-3-phenylpropanoate + NADPH + H+
methyl 2-hydroxy-3-phenylpropanoate + NADP+
-
Substrates: 86.3% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
methyl 2-oxo-4-phenylbutanoate + NADPH + H+
methyl (R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: 88.5% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
methyl 2-oxo-4-phenylbutanoate + NADPH + H+
methyl (R)-2-hydroxy-4-phenylbutanoate + NADP+
-
Substrates: 88.5% of the activity with ethyl 2-oxo-4-phenylbutanoate
Products: -
Products: -
?
methylglyoxal + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
methylglyoxal + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
mitroxantrone + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
mitroxantrone + NADPH + H+
?
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
n-butyrophenone + NADPH
1-phenylbutan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
n-butyrophenone + NADPH
1-phenylbutan-1-ol + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
n-butyrophenone + NADPH
1-phenylbutan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
naphthazarin + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
naphthazarin + NADPH + H+
?
Substrates: an anthracyclin, formation of a 13-hydroxy-anthracyclin
Products: -
Products: -
?
oracin + NADPH + H+
dihydrooracin + NADP+
-
Substrates: 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
Products: -
Products: -
r
oracin + NADPH + H+
dihydrooracin + NADP+
-
Substrates: 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
Products: -
Products: -
r
pentanal + NADPH + H+
pentan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
pentanal + NADPH + H+
pentan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
phenylglyoxal + 2 NADPH + 2 H+
(R)-1-phenyl-1,2-ethanediol + 2 NADP+
-
Substrates: -
Products: 99% yield and 99% enantiomeric excess, by coupling with D-glucose dehydrogenase for the regeneration of cofactor NADPH
Products: 99% yield and 99% enantiomeric excess, by coupling with D-glucose dehydrogenase for the regeneration of cofactor NADPH
?
phenylglyoxal + 2 NADPH + 2 H+
(R)-1-phenyl-1,2-ethanediol + 2 NADP+
-
Substrates: -
Products: 99% yield and 99% enantiomeric excess, by coupling with D-glucose dehydrogenase for the regeneration of cofactor NADPH
Products: 99% yield and 99% enantiomeric excess, by coupling with D-glucose dehydrogenase for the regeneration of cofactor NADPH
?
propanal + NADPH + H+
propan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
propanal + NADPH + H+
propan-1-ol + NADP+
Substrates: -
Products: -
Products: -
?
propanal + NADPH + H+
propan-1-ol + NADP+
Substrates: 54% of the activity with ethyl 2-methyl-3-oxobutanoate
Products: -
Products: -
?
propiophenone + NADPH
1-phenylpropan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
propiophenone + NADPH
1-phenylpropan-1-ol + NADP+
-
Substrates: native and recombinant enzymes, low activity
Products: -
Products: -
?
propiophenone + NADPH
1-phenylpropan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
prostaglandin A1-GSH + NADPH
?
-
Substrates: only enzyme forms T3, V1, V2
Products: -
Products: -
?
prostaglandin B2 + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
prostaglandin E2 + NADPH
?
-
Substrates: isozymes CHCR1 and 2, no activity with isozyme CHCR3
Products: -
Products: -
r
prostaglandin E2 + NADPH
?
-
Substrates: only enzyme forms CR2, CR8
Products: -
Products: -
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
r
pyridine-4-aldehyde + NADPH + H+
pyridin-4-ylmethanol + NADP+
-
Substrates: -
Products: -
Products: -
?
pyridine-4-aldehyde + NADPH + H+
pyridin-4-ylmethanol + NADP+
-
Substrates: native and recombinant enzymes
Products: -
Products: -
?
pyridine-4-aldehyde + NADPH + H+
pyridin-4-ylmethanol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
S-nitrosoglutathione + NADPH + H+
? + NADP+
Substrates: 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
Products: -
Products: -
?
S-nitrosoglutathione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
t-butyl 6-cyano-(5R)-hydroxy-3-oxohexanoate + NADPH + H+
t-butyl 6-cyano-(3R,5R)-dihydroxyhexanoate + NADP+
-
Substrates: high stereoselectivity, 94% conversion in 4 h
Products: -
Products: -
?
t-butyl 6-cyano-(5R)-hydroxy-3-oxohexanoate + NADPH + H+
t-butyl 6-cyano-(3R,5R)-dihydroxyhexanoate + NADP+
[Candida] boidinii CGMCC 9446
-
Substrates: high stereoselectivity, 94% conversion in 4 h
Products: -
Products: -
?
valerophenone + NADPH
1-phenylpentan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
valerophenone + NADPH
1-phenylpentan-1-ol + NADP+
-
Substrates: native and recombinant enzymes
Products: -
Products: -
?
valerophenone + NADPH
1-phenylpentan-1-ol + NADP+
-
Substrates: recombinant enzyme
Products: -
Products: -
?
additional information
?
-
Candida macedoniensis
-
Substrates: very low activity with NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADPH can only partially replace NADH as coenzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: uses only S-enantiomers of methyl-3-hydroxybutanoate, 2-butanol, phenylethanol
Products: -
Products: -
?
additional information
?
-
Substrates: the reduction of aldehydes is cofactor (NADPH) specific unlike the alpha-ketoesters which show dual specificity i.e. both NADH and NADPH
Products: -
Products: -
?
additional information
?
-
Substrates: no reaction with 2-chloroacetophenone plus NADH or 2-hydroxyacetophenone plus NADH
Products: -
Products: -
?
additional information
?
-
Substrates: the reduction of aldehydes is cofactor (NADPH) specific unlike the alpha-ketoesters which show dual specificity i.e. both NADH and NADPH
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH also acts as cofactor
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH also acts as cofactor
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH also acts as cofactor
Products: -
Products: -
?
additional information
?
-
-
Substrates: ordered bi bi mechanism
Products: -
Products: -
?
additional information
?
-
-
Substrates: low reverse direction only detected with cyclohexanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity of various enzyme forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificities of the 3 isozymes, overview, no activity with 5alpha-androstan-3beta-ol-17-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 5alpha-androstane-3alpha-ol-17-one
Products: -
Products: -
?
additional information
?
-
Cylindrocarpon sclerotigenum
-
Substrates: enzyme shows highly restricted substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: stereospecific enzyme, substrate binding mechanism, active site cleft
Products: -
Products: -
?
additional information
?
-
-
Substrates: sniffer prevents age-dependent and oxidative stress-induced neurodegeneration in Drosophila melanogaster, formation of 4-hydroxyalkenals due to lipoprotein oxidation, and is shown to drive macrophage uptake and sub-intimal accumulation of oxidized lipids and lesion progression
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH only acts as cofactor for enzyme form CR1
Products: -
Products: -
?
additional information
?
-
Substrates: reduction of alpha-diketones is regio- and stereospecific producing the corresponding 2R-hydroxy-ketone
Products: -
Products: -
?
additional information
?
-
Substrates: reduction of alpha-diketones is regio- and stereospecific producing the corresponding 2R-hydroxy-ketone
Products: -
Products: -
?
additional information
?
-
Substrates: reduction of alpha-diketones is regio- and stereospecific producing the corresponding 2S-hydroxy-ketone
Products: -
Products: -
?
additional information
?
-
Substrates: reduction of alpha-diketones is regio- and stereospecific producing the corresponding 2S-hydroxy-ketone
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 1-hydroxynon-2-en-4-one and 4-hydroxynon-2-enal
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme metabolizes prostaglandins, steroids, quinines, and anthracycline antibiotics, enzyme expression is inversely associated with tumor progression and angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is active with steroids and prostaglandins
Products: -
Products: -
?
additional information
?
-
Substrates: no doxorubicin or menadione reduction is catalyzed by CBR3
Products: -
Products: -
?
additional information
?
-
-
Substrates: no doxorubicin or menadione reduction is catalyzed by CBR3
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 5alpha-androstane-3alpha-ol-17-one
Products: -
Products: -
?
additional information
?
-
Substrates: inactive towards menadione
Products: -
Products: -
?
additional information
?
-
Substrates: inactive towards menadione
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is a reductase no dehydrogenase, no activity with phenylglyoxal, 2,4-pentanedione, ethyl 3-oxobutanoate, or methyl 3-oxobutanoate, no activity with nitrobenzaldehydes, xylose, isatin, acetone, acetophenone, propionaldehyde, and pyridine 3-aldehyde, enzyme might be an alpha-subunit of the fatty acid synthase due to amino acid sequence identity, but does not show fatty acid synthase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: asymmetric reduction, anti- and syndiastereoselective reactions, overview, identification of products
Products: -
Products: -
?
additional information
?
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward 5-hydroxymethylfurfural, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward 5-hydroxymethylfurfural, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: strong activities are observed toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward 5-hydroxymethylfurfural, propionaldehyde, D-alanine, L-alanine,D-lactate, L-lactate or pyruvate. Enzyme does not exhibit NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is able to reduce both aldehydes and ketones
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is able to reduce both aldehydes and ketones
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyses the oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction. No primary alcohols are oxidized. 1,3-Butandiol, glycerol, methanol, ethanol, 1,2-ethandiol, 1-propanol, 1-amino-2-propanol, 1-butanol, 1-pentanol, 1-hexanol and benzylalcohol are not oxidized nor are the respective aldehydes or ketones reduced
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH also acts as cofactor
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme exhibits a restricted substrate spectrum towards various ketones, and the highest activity is observed with dihydroxyacetone, while hydroxyacetone is reduced with only 0.2% of the activity achieved with dihydroxyacetone, among aliphatic and aromatic ketones and aldehydes. The enzyme proves to be very selective in the reduction of different alpha- and beta-keto esters. Several compounds are converted to the corresponding hydroxy ester in high enantiomeric excess at high conversion rates. Diketones are also accepted by the enzyme. Highest activities are obtained with alpha,beta-diketones carrying the two ketogroups near the end of the aliphatic chain. No or poor activity with 2,5-hexandione, 2-cyclohexen-1-one, cyclohexanone, 2-methylcyclohexanone, 2-pentanone, 4-phenyl-2-butanone, cyclopropyl methyl ketone, trans-3-nonen-2-one, 2-butanone, 2-methyl-2-cyclopenten-1-one, and beta-ionone. The enantioselectivity of the enzyme reaction is highly increased at lower temperatures, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme exhibits a restricted substrate spectrum towards various ketones, and the highest activity is observed with dihydroxyacetone, while hydroxyacetone is reduced with only 0.2% of the activity achieved with dihydroxyacetone, among aliphatic and aromatic ketones and aldehydes. The enzyme proves to be very selective in the reduction of different alpha- and beta-keto esters. Several compounds are converted to the corresponding hydroxy ester in high enantiomeric excess at high conversion rates. Diketones are also accepted by the enzyme. Highest activities are obtained with alpha,beta-diketones carrying the two ketogroups near the end of the aliphatic chain. No or poor activity with 2,5-hexandione, 2-cyclohexen-1-one, cyclohexanone, 2-methylcyclohexanone, 2-pentanone, 4-phenyl-2-butanone, cyclopropyl methyl ketone, trans-3-nonen-2-one, 2-butanone, 2-methyl-2-cyclopenten-1-one, and beta-ionone. The enantioselectivity of the enzyme reaction is highly increased at lower temperatures, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity of various enzyme forms
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 5alpha-androstane-3alpha-ol-17-one
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 5beta-pregnan-3alpha-ol-20-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is highly stereospecific, broad range substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: high enantioselectivity and broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no activity for methyl-3-oxobutanoate and simple ketones and aldehydes such as benzaldehyde and acrolein. No substrate: pyridine-4-aldehyde, ethyl 4,4,4-trifluoro-3-oxobutanoate, pyridine-3-aldehyde or p-nitrobenzaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme performs enantioselective reductions of sterically bulky aryl alkyl ketones, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: reduces ethyl 4-chloro-3-oxobutanoate selectively to S-product
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, detailed overview, the enzyme shows anti-Prelog enantioselectivity, the enzyme catalyzes the reduction of a series of ketones, alpha- and beta-ketoesters, synthesis of several chiral alcohol intermediates of pharmaceutical importance
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes pro-S stereoselective hydrogen transfer from NADPH
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, no activity with 3-nitroacetophenone and 4-acetylpyridine, catalytic activity of the recombinant enzyme is similar to the native enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyses the NADPH-linked reduction of a variety of carbonyl compounds to their secondary alcohols
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme exhibits broad substrate specificity towards various keto esters, ketones and aldehydes, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme exhibits broad substrate specificity towards various keto esters, ketones and aldehydes, detailed overview
Products: -
Products: -
?
additional information
?
-
Substrates: gene contains the conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
Products: -
Products: -
?
additional information
?
-
-
Substrates: gene contains the conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme exhibits broad substrate specificity towards various keto esters, ketones and aldehydes, detailed overview
Products: -
Products: -
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: the recombinant enzyme exhibits broad substrate specificity towards various keto esters, ketones and aldehydes, detailed overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-3-[5-(4-fluorophenyl)-1,5-dioxopentyl]-4-phenyl-2-oxazolidinone + NADPH + H+
(4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one + NADP+
-
Substrates: 99.1% conversion
Products: -
Products: -
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
4-benzoylpyridine + NADPH + H+
S-(-)-phenylpyridin-4-yl-methynol + NADP+
-
Substrates: stereoselective reduction
Products: -
Products: -
?
4-methylnitrosamino-1-(3-pyridyl)-1-butanone + NADPH + H+
4-methylnitrosamino-1-(3-pyridyl)-1-butanol + NADP+
-
Substrates: i.e. NNK, genotoxic compound from tobacco smoke, isozyme 11beta-HSD1, carbonyl reductase activity, EC 1.1.1.184
Products: -
Products: -
r
4-oxonon-2-enal + NADPH + H+
1-hydroxynon-2-en-4-one + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-hydroxynon-2-enal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
4-oxonon-2-enal + NADPH + H+
4-oxononanal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
all-trans retinal + NADPH + H+
all-trans retinol + NADP+
-
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
doxorubicin + NADPH + H+
doxorubicinol + NADP+
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
ethyl 4-chloroacetoacetate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
-
Substrates: enantioselective reduction
Products: -
Products: -
ir
glutathione-4-oxonon-2-enal + NADPH + H+
glutathione-4-hydroxynon-2-enal + NADP+
-
Substrates: metabolic inactivation of the lipid peroxidation product, pathway overview
Products: -
Products: -
?
menadione + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
mitroxantrone + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
N,N-dimethyl-3-keto-3-(2-thienyl)-1-keto propanamine + NADPH + H+
(S)-3-(dimethylamino)-1-(2-thienyl)-1-propanol + NADP+
-
Substrates: mutant enzyme A89N/F154Y with yield of 91.2% and S-enantiomeric excess of 99.9%
Products: -
Products: -
?
naphthazarin + NADPH + H+
?
Substrates: reduction of the anthracycline C13 carbonyl results in a 13-hydroxy metabolite that elicits potent cardiotoxic effects while possessing significantly reduced anticancer properties
Products: -
Products: -
?
oracin + NADPH + H+
dihydrooracin + NADP+
-
Substrates: 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
Products: -
Products: -
r
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
13,14-dihydro-15-ketoprostaglandin F2alpha + NADPH
13,14-dihydroprostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
-
Substrates: -
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
Substrates: -
Products: -
Products: -
?
cortisol + NADPH + H+
20beta-dihydrocortisol + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
ethyl 4-chloro-3-oxobutanoate + NADPH + H+
ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+
Starmerella magnoliae AKU4643
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin E2 + NADPH
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: sniffer prevents age-dependent and oxidative stress-induced neurodegeneration in Drosophila melanogaster, formation of 4-hydroxyalkenals due to lipoprotein oxidation, and is shown to drive macrophage uptake and sub-intimal accumulation of oxidized lipids and lesion progression
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme metabolizes prostaglandins, steroids, quinines, and anthracycline antibiotics, enzyme expression is inversely associated with tumor progression and angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
the wild-type exhibits coenzyme specificity for NADPH over NADH, whereas NADH has stronger inducing ability than NADPH for the S67D/H68D mutant
NADH
-
mutant enzyme with inverted cofactor specificity, strictly specific for
NADPH
-
pro-4S hydrogen atom of the nicotinamide ring of NADPH is transferred to the substrate
NADPH
-
pro-4S hydrogen atom of the nicotinamide ring of NADPH is transferred to the substrate
NADPH
Cylindrocarpon sclerotigenum
-
dependent on, no reverse reaction with NADP+ as cofactor
NADPH
-
catalytically important arginine and lysine residues are located in the enzymes' cofactor binding site and interact with the 2'-phosphate group of the cofactor
NADPH
-
dependent on, structure of the NADPH-binding domain and interaction between the enzyme and NADPH, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Fe2+
KCl
-
optimal activity is observed in the presence of 500 mM NaCl or KCl
Mn2+
NaCl
-
optimal activity is observed in the presence of 500 mM NaCl or KCl
Ni2+
Zinc
Zn2+
additional information
Zn2+
contains two different Zn atoms viz. catalytic Zn and the structural Zn
additional information
-
enzyme is not affected by Mg2+, Ca2+ and Cu2+ at 1 mM
additional information
the enzyme activity is metal-ion-independent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
2,3,4-trinitrobenzenesulfonate sodium
-
acts on a catalytic lysine located at the cofactor binding site, rapid inactivation of the liver enzyme, kinetics, NADP+, 2'-AMP, 2',5'-ADP, and 2'-phospho-5'-ADP-ribose partly protect, but 4-acetylpyridine, 5'-AMP, 5'-ADP, NMN and NAD+ do not
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
-
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
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
butyrophenone
-
inhibitory potency in decreasing order: hexanophenone, valerophenone, heptanophenone, butyrophenone, propiophenone
glycyrrhetinic acid
-
inhibits both 11beta-hydroxysteroid dehydrogenase and carbonyl reductase activities of the enzyme potently
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
EDTA
addition of EDTA to the enzyme solution in a 1:3 enzyme: EDTA mole ratio, results in a drop of the specific activity of the enzyme immediately by 30%
NADP+
NADPH-linked reductase activities of CHCRs are partly inhibited by 2 mM NADP+; NADPH-linked reductase activities of CHCRs are partly inhibited by 2 mM NADP+; NADPH-linked reductase activities of CHCRs are partly inhibited by 2 mM NADP+
Phenylglyoxal
-
acts on a catalytic arginine located at the cofactor binding site, rapid inactivation of the liver enzyme, kinetics, NADP+, 2'-AMP, 2',5'-ADP, and 2'-phospho-5'-ADP-ribose partly protect, but 4-acetylpyridine, 5'-AMP, 5'-ADP, NMN and NAD+ do not
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
additional information
Cylindrocarpon sclerotigenum
-
no inhibition by diphenylhydantoin, N-ethylmaleimide, p-chloromercuribenzoate, PMSF, Mg2+, and Zn2+
-
additional information
not inhibitory: up to 1.0 mM Zn2+, Mg2+, Mn2+, Fe2+, or EDTA
-
additional information
not inhibitory: up to 1.0 mM Zn2+, Mg2+, Mn2+, Fe2+, or EDTA
-
additional information
-
no inhibition by 5 mM 2,2'-dipyridyl, EDTA does not inhibit up to 5 mM
-
additional information
-
protective effects of cofactor derivatives against inactivation by phenylglyoxal and 2,3,4-trinitrobenzenesulfonate sodium, overview
-
additional information
-
not affected by EDTA and 1,10-phenanthroline at 1 mM
-
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
-
additional information
the nonionic surfactants Tween 80 and Triton X-100 have only weak impacts on the enzyme activity
-
additional information
-
the nonionic surfactants Tween 80 and Triton X-100 have only weak impacts on the enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-propanol
-
increases conversion, giving the conversion of 90% compared to 9% in control at a substrate concentration of 70 mM in 1 h. Operational stability increases at higher temperatures with the addition of 2-propanol in the reaction mixture with good conversion (90%) and enantiomeric excess (more than 99%) at 45°C and 50°C. It may be used as a co-substrate for the bioreduction reaction, which may help in widening its applicability in terms of substrate tolerance, reduced time of conversion, increased conversion rate and thermostability
fatty acids
-
with carbon chain length greater than nine at pH 7.0 activate, e.g. arachidonic acid
hexane
-
activity retention is highest in the presence of hexane, reaction shows maximum conversion and enantiomeric excess of 96 and more than 99%, respectively in 15%, v/v hexane with 2-propanol as the cosubstrate
additional information
-
for free cells, activity retention is low in ethanol, butanol and benzyl alcohol
-
additional information
-
CR expression is upregulated in brains suffering from Alzheimers disease
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Injuries
Carbonyl Reductase 1 Attenuates Ischemic Brain Injury by Reducing Oxidative Stress and Neuroinflammation.
Breast Neoplasms
Inhibition of Carbonyl Reductase 1 Safely Improves the Efficacy of Doxorubicin in Breast Cancer Treatment.
Breast Neoplasms
The role of cytochromes p450 and aldo-keto reductases in prognosis of breast carcinoma patients.
Carcinoma
Carbonyl reductase 1 is a new target to improve the effect of radiotherapy on head and neck squamous cell carcinoma.
Carcinoma
Decreased carbonyl reductase 1 expression promotes tumor growth via epithelial mesenchymal transition in uterine cervical squamous cell carcinomas.
Carcinoma
Inhibition of Carbonyl Reductase 1 Enhances Metastasis of Head and Neck Squamous Cell Carcinoma through ?-catenin-Mediated Epithelial-Mesenchymal Transition.
Carcinoma
Low carbonyl reductase 1 expression is associated with poor prognosis in patients with oral squamous cell carcinoma.
Carcinoma, Hepatocellular
Carbonyl reductase 1 as a novel target of (-)-epigallocatechin gallate against hepatocellular carcinoma.
Carcinoma, Hepatocellular
Human carbonyl reductase 1 upregulated by hypoxia renders resistance to apoptosis in hepatocellular carcinoma cells.
Carcinoma, Hepatocellular
The epigallocatechin gallate derivative Y6 reduces the cardiotoxicity and enhances the efficacy of daunorubicin against human hepatocellular carcinoma by inhibiting carbonyl reductase 1 expression.
Carcinoma, Squamous Cell
Carbonyl reductase 1 is a new target to improve the effect of radiotherapy on head and neck squamous cell carcinoma.
Carcinoma, Squamous Cell
Decreased carbonyl reductase 1 expression promotes tumor growth via epithelial mesenchymal transition in uterine cervical squamous cell carcinomas.
Carcinoma, Squamous Cell
Inhibition of Carbonyl Reductase 1 Enhances Metastasis of Head and Neck Squamous Cell Carcinoma through ?-catenin-Mediated Epithelial-Mesenchymal Transition.
Cardiotoxicity
Carbonyl reductase 1 as a novel target of (-)-epigallocatechin gallate against hepatocellular carcinoma.
Cardiotoxicity
DNA sequence variants in the carbonyl reductase 1 (cbr1) gene in seven breeds of Canis lupus familiaris.
Cardiotoxicity
EXPRESSION OF THE ANTHRACYCLINE METABOLIZING ENZYME CARBONYL REDUCTASE 1 (CBR1) IN HEARTS FROM DONORS WITH DOWN SYNDROME.
Cardiotoxicity
Inhibition of Carbonyl Reductase 1 Safely Improves the Efficacy of Doxorubicin in Breast Cancer Treatment.
Cardiotoxicity
Inhibitory Effect of Fruit Juices on the Doxorubicin Metabolizing Activity of Carbonyl Reductase 1.
Cardiotoxicity
Protection from doxorubicin-induced cardiac toxicity in mice with a null allele of carbonyl reductase 1.
Cardiotoxicity
Synthesis of 8-hydroxy-2-iminochromene derivatives as selective and potent inhibitors of human carbonyl reductase 1.
Cardiotoxicity
The epigallocatechin gallate derivative Y6 reduces the cardiotoxicity and enhances the efficacy of daunorubicin against human hepatocellular carcinoma by inhibiting carbonyl reductase 1 expression.
Dehydration
An unusual dehydratase acting on glycerate and a ketoreducatse stereoselectively reducing ?-ketone in polyketide starter unit biosynthesis.
Dehydration
Inhibition of mammalian fatty acid synthetase activity by NADP involves decreased mobility of the 4'-phosphopantetheine prosthetic group.
Dehydration
Reconstitution of a Type II Polyketide Synthase that Catalyzes Polyene Formation.
Dehydration
Stereospecificity of the dehydratase domain of the erythromycin polyketide synthase.
Diabetes Mellitus, Type 2
Genetic variation in the carbonyl reductase 3 gene confers risk of type 2 diabetes and insulin resistance: a potential regulator of adipogenesis.
Down Syndrome
EXPRESSION OF THE ANTHRACYCLINE METABOLIZING ENZYME CARBONYL REDUCTASE 1 (CBR1) IN HEARTS FROM DONORS WITH DOWN SYNDROME.
Drug Resistant Epilepsy
CB1 and CB2 cannabinoid receptor expression during development and in epileptogenic developmental pathologies.
Gastrointestinal Neoplasms
Up-Regulation of Carbonyl Reductase 1 Renders Development of Doxorubicin Resistance in Human Gastrointestinal Cancers.
Heart Failure
Genetic polymorphisms in the carbonyl reductase 3 gene CBR3 and the NAD(P)H:quinone oxidoreductase 1 gene NQO1 in patients who developed anthracycline-related congestive heart failure after childhood cancer.
Insulin Resistance
Genetic variation in the carbonyl reductase 3 gene confers risk of type 2 diabetes and insulin resistance: a potential regulator of adipogenesis.
Keloid
Upregulation of the NNP-1 (novel nuclear protein-1, D21S2056E) gene in keloid tissue determined by cDNA microarray and in situ hybridization.
Kidney Failure, Chronic
Downregulation of Hepatic Carbonyl Reductase Type 1 in End-Stage Renal Disease.
Leiomyosarcoma
Overexpression of carbonyl reductase 1 inhibits malignant behaviors and epithelial mesenchymal transition by suppressing TGF-? signaling in uterine leiomyosarcoma cells.
Leukemia
Carbonyl Reductase 1 Offers a Novel Therapeutic Target to Enhance Leukemia Treatment by Arsenic Trioxide.
Leukemia
Correction: Carbonyl Reductase 1 Offers a Novel Therapeutic Target to Enhance Leukemia Treatment by Arsenic Trioxide.
Leukemia, Myeloid, Acute
Carbonyl reductase 1 expression influences daunorubicin metabolism in acute myeloid leukemia.
Liver Diseases
Identification and Analysis of the Tegument Protein and Excretory-Secretory Products of the Carcinogenic Liver Fluke Clonorchis sinensis.
Lung Neoplasms
Cinnamic acid derivatives as chemosensitising agents against DOX-treated lung cancer cells - Involvement of carbonyl reductase 1.
Lung Neoplasms
Induction of carbonyl reductase 1 (CBR1) expression in human lung tissues and lung cancer cells by the cigarette smoke constituent benzo[a]pyrene.
Malformations of Cortical Development
CB1 and CB2 cannabinoid receptor expression during development and in epileptogenic developmental pathologies.
Neoplasm Metastasis
Bcl-x(L)-mediated changes in metabolic pathways of breast cancer cells: from survival in the blood stream to organ-specific metastasis.
Neoplasm Metastasis
Inhibition of Carbonyl Reductase 1 Enhances Metastasis of Head and Neck Squamous Cell Carcinoma through ?-catenin-Mediated Epithelial-Mesenchymal Transition.
Neoplasm Metastasis
Inhibitory effect of carbonyl reductase 1 against peritoneal progression of ovarian cancer: evaluation by ex vivo 3D-human peritoneal model.
Neoplasms
Antioxidants: friends or foe in prevention or treatment of cancer: the debate of the century.
Neoplasms
Carbonyl Reductase 3 (CBR3) Mediates 9-cis-Retinoic Acid-Induced Cytostatis and is a Potential Prognostic Marker for Oral Malignancy.
Neoplasms
Decreased carbonyl reductase 1 expression promotes tumor growth via epithelial mesenchymal transition in uterine cervical squamous cell carcinomas.
Neoplasms
Decreased expression of carbonyl reductase 1 promotes ovarian cancer growth and proliferation.
Neoplasms
Genetic polymorphisms in the carbonyl reductase 3 gene CBR3 and the NAD(P)H:quinone oxidoreductase 1 gene NQO1 in patients who developed anthracycline-related congestive heart failure after childhood cancer.
Neoplasms
Identification and Analysis of the Tegument Protein and Excretory-Secretory Products of the Carcinogenic Liver Fluke Clonorchis sinensis.
Neoplasms
Inhibition of Carbonyl Reductase 1 Enhances Metastasis of Head and Neck Squamous Cell Carcinoma through ?-catenin-Mediated Epithelial-Mesenchymal Transition.
Neoplasms
Inhibitory effect of carbonyl reductase 1 on ovarian cancer growth via tumor necrosis factor receptor signaling.
Neoplasms
Overexpression of carbonyl reductase 1 inhibits malignant behaviors and epithelial mesenchymal transition by suppressing TGF-? signaling in uterine leiomyosarcoma cells.
Neoplasms
Regulation of Human Carbonyl Reductase 3 (CBR3; SDR21C2) Expression by Nrf2 in Cultured Cancer Cells.
Neoplasms
The role of cytochromes p450 and aldo-keto reductases in prognosis of breast carcinoma patients.
Neuroinflammatory Diseases
Carbonyl Reductase 1 Attenuates Ischemic Brain Injury by Reducing Oxidative Stress and Neuroinflammation.
Obesity
Carbonyl reductase 1 amplifies glucocorticoid action in adipose tissue and impairs glucose tolerance in lean mice.
Obesity
Carbonyl reductase 1 catalyzes 20?-reduction of glucocorticoids, modulating receptor activation and metabolic complications of obesity.
Ovarian Neoplasms
Decreased expression of carbonyl reductase 1 promotes ovarian cancer growth and proliferation.
Ovarian Neoplasms
Gene therapy for ovarian cancer using carbonyl reductase 1 DNA with a polyamidoamine dendrimer in mouse models.
Ovarian Neoplasms
Inhibitory effect of carbonyl reductase 1 against peritoneal progression of ovarian cancer: evaluation by ex vivo 3D-human peritoneal model.
Ovarian Neoplasms
Inhibitory effect of carbonyl reductase 1 on ovarian cancer growth via tumor necrosis factor receptor signaling.
Prostatic Neoplasms
Synergistic anticancer activity of doxorubicin and piperlongumine on DU-145 prostate cancer cells - The involvement of carbonyl reductase 1 inhibition.
Reperfusion Injury
Upregulation of Carbonyl Reductase 1 by Nrf2 as a Potential Therapeutic Intervention for Ischemia/ Reperfusion Injury during Liver Transplantation.
Squamous Cell Carcinoma of Head and Neck
Carbonyl reductase 1 is a new target to improve the effect of radiotherapy on head and neck squamous cell carcinoma.
Squamous Cell Carcinoma of Head and Neck
Inhibition of Carbonyl Reductase 1 Enhances Metastasis of Head and Neck Squamous Cell Carcinoma through ?-catenin-Mediated Epithelial-Mesenchymal Transition.
Squamous Cell Carcinoma of Head and Neck
Low carbonyl reductase 1 expression is associated with poor prognosis in patients with oral squamous cell carcinoma.
Tuberculosis
Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.
Tuberous Sclerosis
CB1 and CB2 cannabinoid receptor expression during development and in epileptogenic developmental pathologies.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.59
2-hydroxyacetophenone
wild-type, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
0.63
2-hydroxyacetophenone
mutant DELTA31, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
0.68
2-hydroxyacetophenone
mutant S172T, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
0.71
2-hydroxyacetophenone
mutant V270D, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
0.76
2-hydroxyacetophenone
mutant S67D/H68D, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
7.89
2-hydroxyacetophenone
wild-type, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
8.03
2-hydroxyacetophenone
mutant DELTA31, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
8.45
2-hydroxyacetophenone
mutant V270D, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
8.67
2-hydroxyacetophenone
mutant S172T, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
10.27
2-hydroxyacetophenone
mutant S67D/H68D, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
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
0.043
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.386
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.435
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.12
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.338
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.354
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.64
4-nitrobenzaldehyde
-
recombinant protein purified from E. coli
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
0.0128
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
0.0393
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
0.0026
ethyl 4-chloro-3-oxobutanoate
-
pH 6.5, 30°C, recombinant mutant S1M4
0.003
ethyl 4-chloro-3-oxobutanoate
-
pH 6.5, 30°C, recombinant wild-type enzyme
0.0039
ethyl 4-chloro-3-oxobutanoate
-
pH 6.5, 30°C, recombinant mutant S1M1
0.00183
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.0026
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
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
0.078
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
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
0.3
NADH
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.43
NADH
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
8.03
NADH
deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C
0.00214
NADPH
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.0022
NADPH
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.0218
NADPH
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.63
NADPH
deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C
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
0.832
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
-
additional information
additional information
-
pharmacokinetics of acetohexamide in male Wistar-Imamichi, showing very low enzyme amount, and Sprague-Dawley rats, overview
-
additional information
additional information
-
reaction and cofactor binding kinetics of wild-type and mutant enzymes, thermodynamics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.2
ethyl 2-oxo-4-phenylbutyrate
pH 9.0, 70°C, recombinant enzyme
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
1.13
2-hydroxyacetophenone
mutant S172T, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.21
2-hydroxyacetophenone
mutant S67D/H68D, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.22
2-hydroxyacetophenone
mutant V270D, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.24
2-hydroxyacetophenone
mutant DELTA31, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.26
2-hydroxyacetophenone
mutant S67D/H68D, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.32
2-hydroxyacetophenone
wild-type, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.34
2-hydroxyacetophenone
mutant V270D, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.36
2-hydroxyacetophenone
mutant S172T, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.39
2-hydroxyacetophenone
mutant DELTA31, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
1.48
2-hydroxyacetophenone
wild-type, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)
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
0.053
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°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
1.03
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
1.967
4-benzoylpyridine
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.0283
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.3
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
1.087
4-nitrobenzaldehyde
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 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
0.5167
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
0.583
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
1.225
isatin
at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C
1.24
NADH
deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C
1.39
NADPH
deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1.72
S-nitrosoglutathione
mutant D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, pH 7.4, temperature not specified in the publication
2.5
S-nitrosoglutathione
mutant C227S, 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
93.45
S-nitrosoglutathione
wild-type, pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0105
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
0.05
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.00021
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
0.0036
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
0.034
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.011
0.02
0.025
0.03
with cinnamaldehyde and NADH as substrates, at pH 7.0 and 30°C
0.073
-
substrate 1-phenylethanonee, pH 6.5, temperature not specified in the publication
0.074
-
substrate 1-(4-chlorophenyl)ethanone, pH 6.5, temperature not specified in the publication
0.12
-
recombinant enzyme, substrate trifluoromethyl 3-oxobutyrate
0.45
with 4-hydroxybenzaldehyde and NADPH as substrates, at pH 7.0 and 30°C
0.47
with 2-chlorobenzaldehyde and NADPH as substrates, at pH 7.0 and 30°C
0.522
-
substrate ethyl 3-oxopentanoate, pH 6.5, temperature not specified in the publication
0.58
0.62
with 2-oxo-2-phenylacetic acid and NADPH as substrates, at pH 7.0 and 30°C
0.64
with ethyl-2-oxo-2-phenylacetate and NADH as substrates, at pH 7.0 and 30°C
0.85
with ethyl-2-oxo-2-phenylacetate and NADPH as substrates, at pH 7.0 and 30°C
1.2
1.63
with 2-oxo-2-phenylacetaldehyde and NADPH as substrates, at pH 7.0 and 30°C
10.9
-
substrate 4-bromobenzaldehyde, pH 6.5, temperature not specified in the publication
1502
-
substrate ethyl 4-chloro-3-oxobutanoate, pH 6.5, temperature not specified in the publication
19.69
with 4-methoxybenzaldehyde as substrate, at pH 7.5 and 30°C
2.1
3.5
purified recombinant enzyme, substrate 3,4-hexandione, pH 7.0, 30°C
3.8
with 2,4-dichlorobenzaldehyde as substrate, at pH 7.5 and 30°C
33.96
4.14
with 3-hydroxybenzaldehyde and NADPH as substrates, at pH 7.0 and 30°C
468
6.3
-
substrate 4-chlorobenzaldehyde, pH 6.5, temperature not specified in the publication
7
-
substrate 4-fluorobenzaldehyde, pH 6.5, temperature not specified in the publication
7.9
8.33
with cinnamaldehyde and NADPH as substrates, at pH 7.0 and 30°C
80
purified recombinant enzyme, substrate 2,3-hexandione, pH 7.0, 30°C
89
purified recombinant enzyme, substrate 2,3-heptandione, pH 7.0, 30°C
additional information
0.01
with ethyl-4,4,4-trifloro-3-oxo-butanoate and NADPH as substrates, at pH 7.0 and 30°C
0.01
with acetophenone and NADH as substrates, at pH 7.0 and 30°C
0.01
with acetophenone and NADPH as substrates, at pH 7.0 and 30°C
0.02
with 2-oxo-2-phenylacetaldehyde and NADH as substrates, at pH 7.0 and 30°C
0.02
with ethyl-4,4,4-trifloro-3-oxo-butanoate and NADH as substrates, at pH 7.0 and 30°C
0.58
with benzaldehyde and NADH as substrates, at pH 7.0 and 30°C
33.96
with benzaldehyde and NADPH as substrates, at pH 7.0 and 30°C
468
purified recombinant enzyme, substrate dihydroxyacetone, pH 7.0, 30°C
additional information
-
quantitative enzyme expression analysis in 59 samples of non-small-cell lung cancer, overview
additional information
-
plasma clearance of acetohexamide in male Wistar-Imamichi, showing very low enzyme amount, and Sprague-Dawley rats, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5.3
-
4-nitroacetophenone, pyridine 4-aldehyde, 5beta-dihydrotestosterone, enzyme CR2
5 - 6
5.5
6.5
additional information
-
enzyme activation by arachidonic acid shifts pH-optimum from 5.8 to 6.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6 - 8
-
more than 50% activity between pH 6.0 and 8.0. The activity decreases rapidly when pH is below 6.0 or above 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
60
additional information
additional information
the enantioselectivity of the enzyme reaction is highly increased at lower temperatures, overview
additional information
-
the enantioselectivity of the enzyme reaction is highly increased at lower temperatures, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
-
the activity increases as temperature increases from 10 to 35°C. However, the activity decreases rapidly when temperature is above 35°C. The enzyme shows more than 60% activity between 30 and 45°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Starmerella magnoliae AKU4643
-
-
-
brenda
isoform Cbr3, comparison with prostaglandin 9-ketoreductase Cbr1
SwissProt
brenda
male Wistar-Imamichi, showing very low enzyme amount, and Sprague-Dawley rats
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GM10853, GM10845, GM10857, GM10858, GM10860, GM17240, GM16654, GM16688, and GM16689
brenda
-
enzyme expression analysis, 59 different samples
brenda
additional information
-
strong expression of isozyme CHCR1, weaker expression of isozyme CHCR2, no expression of isozyme CHCR3
brenda
-
strong expression of all 3 isozyme in descending order CHCR1, CHCR2, CHCR3
brenda
high expression of CHCR1 at both the mRNA and protein levels
brenda
high expression of CHCR2 at both the mRNA and protein levels
brenda
-
major form of soluble NADPH-dependent all-trans-retinal dehydrogenase in liver
brenda
-
moderate expression of all 3 isozyme in descending order CHCR1, CHCR2, CHCR3
brenda
black and white donors, show similar CBR1 mRNA and protein levels. CBR1 1096G-A polymorphism is common in samples from white donors
brenda
-
ciliated cells, nonciliated bronchiolar cells, Type II alveolar pneumocytes, epithelial cells of the ducts of the bronchial gland
brenda
high expression of CHCR1 at both the mRNA and protein levels
brenda
high expression of CHCR2 at both the mRNA and protein levels
brenda
additional information
CHCR1 is absent from uterus and ovary. CHCR1 shows a sex-dependent expression at the protein level
brenda
additional information
CHCR1 is absent from uterus and ovary. CHCR1 shows a sex-dependent expression at the protein level
brenda
additional information
CHCR1 is absent from uterus and ovary. CHCR1 shows a sex-dependent expression at the protein level
brenda
additional information
-
CHCR1 is absent from uterus and ovary. CHCR1 shows a sex-dependent expression at the protein level
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
sequence contains peroxisomal targeting signal Ser-His-Leu
brenda
C-terminal peroxisomal targeting sequence 1 of each subunit is involved in intersubunit interactions and buried in the interior of the tetrameric enzyme
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
pharmacological inhibition of carbonyl reductase 1 in diet-induced obesity in mice results in more marked glucose intolerance with evidence for enhanced hepatic glucocorticoid receptor signaling
metabolism
physiological function
CBR1 is upregulated at the transcript level during cell differentiation. CBR1 expression is increased during skeletal muscle regeneration in tibialis anterior muscle after injury induced by cardiotoxin. Intracellular reactice levels and lipid peroxidation are increased incells transfected with CBR1 siRNA
additional information
evolution
the enzyme belongs to the aldo-keto reductase (AKR) superfamily of NAD(P)(H)-dependent oxidoreductases
evolution
the enzyme is a member of the aldo-keto-reductase family (AKR)
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) family
evolution
Starmerella magnoliae AKU4643
-
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) family
-
evolution
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the enzyme belongs to the aldo-keto reductase (AKR) superfamily of NAD(P)(H)-dependent oxidoreductases
-
evolution
-
the enzyme belongs to the aldo-keto reductase (AKR) superfamily of NAD(P)(H)-dependent oxidoreductases
-
evolution
-
the enzyme is a member of the aldo-keto-reductase family (AKR)
-
metabolism
-
carbonyl reductase 1 generating 20beta-dihydrocortisol is a pathway modulating glucocorticoid receptor activation and providing enzymatic protection against excessive GR activation in obesity
metabolism
carbonyl reductase 1 generating 20beta-dihydrocortisol is a pathway modulating glucocorticoid receptor activation and providing enzymatic protection against excessive GR activation in obesity
metabolism
carbonyl reductase 1 generating 20beta-dihydrocortisol is a pathway modulating glucocorticoid receptor activation and providing enzymatic protection against excessive GR activation in obesity
additional information
conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
additional information
-
conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
-
additional information
-
conserved catalytic tetrad D-Y-K-H (Asp53, Tyr58, Lys84, and His117) and putative cofactor binding sites at Asp53, Ser147, Asn148, Gln169, Glu249, and Asn254
-
Show AA Sequence and Transmembrane Helices (2294 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
23000
24000
27000
30000
31000
31590
32000
34000
35000
40000
additional information
110000
analytical ultracentrifugation analysis, mutant S67D/H68D and wild-type
31000
-
x * 31000, isozyme CHCR1, SDS-PAGE, x * 32000, isozyme CHCR2, SDS-PAGE, x * 34000, isozyme CHCR3, SDS-PAGE
32000
-
x * 31000, isozyme CHCR1, SDS-PAGE, x * 32000, isozyme CHCR2, SDS-PAGE, x * 34000, isozyme CHCR3, SDS-PAGE
34000
-
x * 31000, isozyme CHCR1, SDS-PAGE, x * 32000, isozyme CHCR2, SDS-PAGE, x * 34000, isozyme CHCR3, SDS-PAGE
additional information
-
the enzyme forms aggregates of high molecular weight above the size exclusion limit of native PAGE of 1300 kDa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homotetramer
monomer
oligomer
tetramer
additional information
?
-
x * 31000, isozyme CHCR1, SDS-PAGE, x * 32000, isozyme CHCR2, SDS-PAGE, x * 34000, isozyme CHCR3, SDS-PAGE
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
x * 32000, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
-
ribbon diagram of tertiary structure, diagrams of additional members of SDR family
tetramer
-
in presence of NADPH, in absence of cofactor the enzyme forms mixtures of dimer, monomer, and tetramer, SDS-PAGE and native PAGE
additional information
-
enzyme from human liver indistinguishable from enzyme from brain
additional information
molecular modeling and generation of a three-dimensional structural model
additional information
-
SSCR has two domains, an NADPH-binding domain and a substrate-binding domain, structure overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional strcuture determined by molecular replacement at a resolution of 2.09 A, in the presence of NADPH. Extensive formation of the intrasubunit ion pair networks, and the presence of the strong intersubunit interaction, is likely responsible for thermostability
apo-enzyme, diffraction to 2.7 A. Enzyme forms a homotetramer with broken 2-2-2 symmetry. In the apo-form, the entrance of the NADPH pocket is blocked by a surface loop
by the hanging-drop vapor diffusion method, to 2.7 A resolution, crystal form belongs to space group P212121 with cell dimensions of a=104.7 A, b=142.8 A, and c=151.8 A. It forms a homotetramer with a broken 2-2-2 symmetry. SCR contains an extended N-terminal peptide (i.e., residues 1-25) and a short helix (residues 26-30) projecting out from the core domain that may stabilize the oligomer. In the apo-SCR structure, the entrance of the NADPH pocket is blocked by a surface loop
homology modeling of native enzyme, enzyme lacking the extra loop domain, and exchange of the extra loop domain for the short extra loop of 3alpha/20beta-hydroxysteroid dehydrogenase
-
purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml water with 0.003 ml protein solution and 0.003 ml reservoir solution giving 18% w/v PEG 4000, 0.15 M sodium acetate, 75 mM Tris, pH 8.5, severeal days at 4°C, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular modeling
-
molecular replacement, to 1.98 A resolution in presence of NADPH and ethylene glycol
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
computational model of docking of 4¢-methoxyacetophenone to the Q245H mutant
-
purified recombinant free wild-type or selenomethionine-labeled enzyme and in complex with NADPH, vapour disffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, against a reservoir solution containing 32% w/v PEG 2000 monomethyl ether, 100 mM ammonium sulfate, and 0.2 M sodium acetate, pH 5.0, with or without 4 mM NADPH, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, structure modeling
-
purified detagged recombinant enzyme, sitting-drop vapour-diffusion method, protein solution is supplemented with 5 mM beta-NADPH, crystallization from 31% v/v PEG 400, 0.2 M Li2SO4, 0.08 M sodium potassium tartrate tetrahydrate, 0.1 M sodium cacodylate, pH 6.5, at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.90 A resolution
5 mg/ml recombinant enzyme in 25 mM phosphate buffer, pH 8.0, with 10% glycerol, and 5 mM NADP+, hanging drop vapour diffusion method, against well solution containing 4.0-4.4 M sodium formate and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
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
-
in complex with cofactor NADP+ and with NADP+ and substrate ethyl 2-oxo-4-phenylbutyrate, to 1.7 and 2.0 A resolution, respectively. Both crystals belong to space group P3121, with similar unit-cell parameters
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G135A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
G180A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
I190A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
M186A
-
the mutant shows increased activity with 3-bromoacetophenone as compared to the wild type enzyme
Q187A
-
the mutant shows increased activity with 3-bromoacetophenone as compared to the wild type enzyme
V181A
-
the mutant shows strongly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
W144A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
Y141A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
G135A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
G180A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
V181A
-
the mutant shows strongly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
W144A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
Y141A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
DELTA31
deletion of the N-terminal 31 residues, kinetic parameters KM and kcat are essentially the same as those of the wild-type. It forms a tetramer in solution, which is similar to the wild-type but is less stable. Melting temperature is 48°C, which is lower than that of the wild-type (52°C)
H68D/P69D
produces (R)-enantiomer with low optical purity and yield
S172A
S172T
S67D/H68D
S67D/P69D
produces (R)-enantiomer with low optical purity and yield
V270D
Y187A
Y187F
W230P
-
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
Y172A
Km value for 9,10-phenanthrenequinone (model substrate) is 12.5 times higher than that for the wild-type enzyme
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
V166A
-
the mutant has increased activity with 2,2,2-trifluoroacetophenone compared to the wild type enzyme
W230P
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
A89N/F154Y
-
Vmax and kcat values of the mutant enzyme are enhanced by 2.08 and 3.86fold, respectively, while the Km value decreases by 2.36fold compared to the wild type enzyme
Q245H
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
Q245L
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
Q245P
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
S41A/S42A/S43Q/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M1 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
S41A/S42A/S43R/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M4 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
S41A/S42A/S43Q/W63I/Y64D/N65I/S66N
Starmerella magnoliae AKU4643
-
site-sirected mutagenesis, mutant S1M1 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
-
S41A/S42A/S43R/W63I/Y64D/N65I/S66N
Starmerella magnoliae AKU4643
-
site-sirected mutagenesis, mutant S1M4 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
-
additional information
S172A
site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity
S172A
melting temperature is 46°C, which is lower than that of the wild-type (52°C). Shows no activity
S172T
site-directed mutagenesis, decrease of melting temperature compared to wild-type. Catalytic activity similar to wild-type
S172T
melting temperature is 48°C, which is lower than that of the wild-type (52°C). Activity is essentially the same as the wild-type
S67D/H68D
site-directed mutagenesis, about 10fold increase and 20fold decrease for NADH and NADPH kcat/KM-value, respectively
S67D/H68D
produces (R)-1-phenyl-1,2-ethanediol with high optical purity of 95.4% and a yield of 83.1% in the NADH-linked reaction. It results in a nearly 10fold increase and a 20fold decrease in the kcat/Km value when NADH and NADPH are used as the cofactors, respectively, but maintaining a kcat value essentially the same with respect to wild-type. The mutant has a stronger preference for NADH and weaker binding for NADPH. It exhibits a secondary structure and melting temperature similar to the wild-type form. NADH provides maximal protection against thermal and urea denaturation for S67D/H68D, in contrast to the effective protection by NADP(H) for the wild-type enzyme. Thus, the double point mutation S67D/H68D successfully converts the coenzyme specificity of SCR from NADP(H) to NAD(H) as well as the product enantioselectivity without disturbing enzyme stability
S67D/H68D
double-point mutation inside the coenzyme-binding pocket results in a nearly 10fold increase and a 20fold decrease in the kcat/KM value when NADH and NADPH are used as cofactors, respectively, with kcat remaining essentially the same. Shows similar thermal stability to wild-type
V270D
site-directed mutagenesis, catalytic acitivity similar to wild-type, mutant forms a dimer
V270D
renders the SCR as a homodimer, rather than a tetramer, without affecting the enzymatic activity. Melting temperature is 45°C, which is lower than that of the wild-type (52°C)
Y187A
site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity
Y187A
melting temperature is 45°C, which is lower than that of the wild-type (52°C). Shows no activity
Y187F
site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity
Y187F
melting temperature is 46°C, which is lower than that of the wild-type (52°C). Shows no activity
P230W
-
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
P230W
active towards isatin and 9,10-phenanthrenequinone as the wild-type
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
site-directed mutagenesis, deletion of the N-terminal 31 residues, catalytic parameters similar to wild-type, decrase in melting temperature
additional information
codon variants DELTA24 (truncation of disorder sequence of 4-27 bp at the 5'-terminus), aRCR (its nine out of 11 rare codons are adapted according to the codon bias in Escherichia coli), and mRCR (its disorder sequence of 4-27 bp at the 5'-terminus is truncated and nine out of 11 rare codons are adapted) are expressed at higher levels than the wild-type. Mutant mRCR presents highest enzyme activity. When compared with wild-type, mRCR shows an increase of 35.6% in the total activity of cell-free extracts
additional information
-
codon variants DELTA24 (truncation of disorder sequence of 4-27 bp at the 5'-terminus), aRCR (its nine out of 11 rare codons are adapted according to the codon bias in Escherichia coli), and mRCR (its disorder sequence of 4-27 bp at the 5'-terminus is truncated and nine out of 11 rare codons are adapted) are expressed at higher levels than the wild-type. Mutant mRCR presents highest enzyme activity. When compared with wild-type, mRCR shows an increase of 35.6% in the total activity of cell-free extracts
additional information
-
removal of the extra-loop domain in 3alpha/hydroxysteroid dehydrogenase/carbonyl reductase may lead to the formation of an enzymatically active homotetramer
additional information
-
gene sniffer mutants are highly sensitive to hyperoxia-induced oxidative stress, mutations in the gene lead to a reduced life span, age-related neurodegeneration, and motoric dysfunctions that deteriorate with age, analysis of the central nervous system in sniffer mutants reveals signifcant cortex and neutrophil vacuolization and apoptosis in the brain, overexpression confers neuronal protection against oxygen-induced apoptosis, increases resistance of flies to experimental normobaric hyperoxia, and improves general locomotor fitness, overview
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
additional information
-
design and construction of mutant enzymes, e.g. S1M1 and S1M4, with inverted cofactor specificity using computer-aided methods, in silico screening, three-dimensional structure modeling, and site-sirected mutagenesis, mutant screening, overview, the mutant enzyme utilizes NADH, but not NADPH as cofactor
additional information
Starmerella magnoliae AKU4643
-
design and construction of mutant enzymes, e.g. S1M1 and S1M4, with inverted cofactor specificity using computer-aided methods, in silico screening, three-dimensional structure modeling, and site-sirected mutagenesis, mutant screening, overview, the mutant enzyme utilizes NADH, but not NADPH as cofactor
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
4°C, maintains more than 80% of maximum activity for 48 h
5.5 - 7.5
-
the enzyme is highly stable in acidic environment and more than 80% of the activity is maintained when exposed to pH 5.5-7.5 for 60 min at 25°C
9
-
the enzyme keeps more than 70% of its peak activity after incubation in Tris-HCl buffer at pH 9.0 for 40 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25 - 55
-
the enzyme has half-lives of 18.57, 12.99, 0.76 and 0.06 h at 25, 35, 45 and 55°C respectively
35 - 55
-
about 60% of enzymatic activity is maintained after 30 min of incubation at 35°C. However, the activity is completely lost after incubation at 55°C for 30 min
40 - 50
-
when incubated at 40°C and 50°C for 2 h, the enzyme maintains residual enzyme activity of more than 70%
45
46
48
melting temperature, mutant S172T and N-terminal deletion mutant lacking 31 amino acids
50
85
additional information
-
activation by arachidonic acid leads to a decrease in thermal stability
85
the purified recombinant enzyme retains 63% of its maximal activity after 15 h at 85°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
an ammonium sulfate precipitate (3 M, pH 7) of the enzyme loses its activity completely within a few days
-
compared to activity in acetate and Tris-HCl, carbonyl reductase shows higher activity using potassium phosphate as buffer at pH 5.5 or pH 7
minor loss of activity in 50 mM phosphate buffer is observed during purification and storage at 4°C without additional precautions
-
no conditions to stabilize the enzyme by freezing at -20°C are found. Addition of 1-10% bovine serum albumin, 20-50% glycerol, 20% 1,2-ethanediol or 0.1% Triton X-100 to the enzyme solution in 40 mM phosphate or 40 mM Tris-HC1 pH 7 before freezing for 1 day or longer has no stabilizing effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
acetonitrile
DMSO
Ethanol
Methanol
2-propanol
concentrations up to 10% v/v slightly increase the enzyme activity to 112%
2-propanol
-
concentrations up to 10% v/v slightly increase the enzyme activity to 112%
-
2-propanol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
concentrations up to 10% v/v slightly increase the enzyme activity to 112%
-
acetonitrile
concentrations up to 10% v/v slightly increase the enzyme activity to 108%
acetonitrile
-
concentrations up to 10% v/v slightly increase the enzyme activity to 108%
-
acetonitrile
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
concentrations up to 10% v/v slightly increase the enzyme activity to 108%
-
DMSO
concentrations up to 10% v/v slightly decrease the enzyme activity
DMSO
-
concentrations up to 10% v/v slightly decrease the enzyme activity
-
DMSO
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
concentrations up to 10% v/v slightly decrease the enzyme activity
-
Ethanol
concentrations up to 10% v/v slightly increase the enzyme activity to 109%
Ethanol
-
concentrations up to 10% v/v slightly increase the enzyme activity to 109%
-
Ethanol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
concentrations up to 10% v/v slightly increase the enzyme activity to 109%
-
Methanol
concentrations up to 10% v/v slightly decrease the enzyme activity
Methanol
-
concentrations up to 10% v/v slightly decrease the enzyme activity
-
Methanol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
concentrations up to 10% v/v slightly decrease the enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.02 mg/ml protein concentration, 0.15 M KCl, stable for at least several days, 90% loss of activity after 2 weeks
-
4°C, pH 7, protein concentration above 1.5 mg/ml, strictly anaerobic conditions in 50 mM phosphate, stable for up to 1 year without significant loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
380fold to homogeneity by protamine precipitation, solubilization, ammonium sulfate fractionation, solubilization with 0.5 M NaCl, ultrafiltration, butyl-resin chromatography, and gel filtration
-
by affinity chromatography on a Ni2+ column and by gel filtration
by metal-chelating affinity column chromatography and gel filtration
by Ni2+ chelating affinity column chromatography
by sequential column chromatographies involving DEAE ion exchange, phenyl resin, and hydroxylapatite chromatography
Cylindrocarpon sclerotigenum
-
by several chromatographic steps, i.e. Q-Sepharose, FPLC, Phenyl Sepharose, HiTrap Blue, Red Sepharose, and gel filtration, and native PAGE
-
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
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) partially by ammonium sulfate fractionation
-
recombinant His-tagged enzyme 17.8fold from Escherichia coli strain BL21(DE3) by affinity chromatography
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged isozymes CHCR1-3 from Escherichia coli strain BL21(DE3)
-
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity and anion exchange chromatography, cleavage of the tag by thrombin protease, and gel filtration
recombinant protein
recombinant wild-type and mutant enzymes from Escherichia coli strain HB101 by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, to homogeneity
-
recombinant wild-type enzyme from Escherichia coli strain JM109 and recombinant selenomethionine-CR from Escherichia coli strain B834, by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, and gel filtration
-
wild-type and mutant enzymes purified to homogeneity by Ni-affinity chromatography
by affinity chromatography on a Ni2+ column and by gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
co-expressed with glucose dehydrogenase from Exiguobacterium sibiricum in Escherichia coli BL21 (DE3) cells
-
co-expressed with glucose dehydrogenase from Thermus acidophilum in Escherichia coli BL21(DE3) cells
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)
expression of His6-tagged enzyme in Escherichia coli strain Rosetta (DE3)
expression of isozymes CHCR1-3 as His-tagged proteins in Escherichia coli strain BL21(DE3)
-
expression of the heart enzyme in Escherichia coli BL21(DE3), assembly to tetrameric form
-
expression of wild-type and mutant enzymes in Escherichia coli strain HB101
-
expression of wild-type enzyme in Escherichia coli strain JM109, and of selenomethionine-CR in Escherichia coli strain B834
-
from a liver cDNA library, overexpression in Escherichia coli as His-tagged enzyme
-
functional overexpression as His-tagged protein in Escherichia coli BL21(DE3)
-
gene Gre2, high level expression in Escherichia coli strain BL21(DE3)
-
gene nccr, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
gene Tm1743, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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)
-
mutant enzyme V166A is co-expressed with alcohol dehydrogenase from Thermoanaerobacter ethanolicus in Rhodococcus opacus strain B-4
-
overview
pET28a-CHCR-transformed Escherichia coli BL21(DE3)pLys cells
quantitative enzyme expression analysis in 59 samples of non-small-cell lung cancer, overview
-
SCR overexpressed from pETSCR plasmid in Escherichia coli BL21 (DE3) as His6-tagged proteins
sniffer gene, expression as His-tagged enzyme from Escherichia coli strain M15
-
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
wild-type and mutant enzymes inserted into vector pQE30a and expressed in Escherichia coli BL21 (AITM) cells
wild-type and mutants expressed in Escherichia coli strain BL21(DE3) as His6-tagged proteins
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
-
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
-
wild-type and mutant cloned into the pET-28a vector and expressed in Escherichia coli, BL21(DE3) pLysE cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CBR1 is upregulated at the transcript level during cell differentiation. CBR1 expression is increased during skeletal muscle regeneration in tibialis anterior muscle after injury induced by cardiotoxin. The transcriptional upregulation of CBR1 is controlled by nuclear factor erythroid 2-related factor 2 (Nrf2), and Nrf2 knockdown with specific siRNA inhibits muscle differentiation
the enzyme is up-regulated in adipose tissue in obesity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
expression of CBR mRNA is a significant prognostic factor in nonsmall-cell lung cancer and is inversely associated with tumor progression and angiogenesis
drug development
food industry
mequindox, inhibitor of several Gram-positive and Gram-negative bacteria, is reduced by carbonyl reductase CBR1
industry
medicine
synthesis
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
industry
modification of coenzyme specificity and alteration of product enantioselectivity in SDRs by using the protein engineering approach, which will have valuable industrial applications
industry
improved (R)-1-phenyl-1,2-ethanediol production by a codon optimized R-specific carbonyl reductase whose coding gene rcr is engineered by truncating its disorder sequence of 4-27 bp at 5'-terminus and adaption of codon usage bias in Escherichia coli. It will provide a new method to establish an effective expression system for improving chiral alcohol productivity by codon optimization
industry
enzyme has a promising future for industrial application
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
medicine
-
antidepressant bupropion is reduced to erythrohydrobupropion and threohydrobupropion in liver. Menadione and 18beta-glycyrrhetinic acid are inhibitory
synthesis
-
enzyme is useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compouds
synthesis
Cylindrocarpon sclerotigenum
-
enzyme might be useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compounds
synthesis
the enzyme is useful for stereoselective enzymatic synthesis of chiral alcohols and chiral alcohol intermediates of pharmaceutical importance
synthesis
-
production of Geotrichum candidum carbonyl reductase in a laboratory scale stirred tank bioreactor, optimization of conditions. At controlled pH value of 5.5 the specific enzyme activity is highest with 306 U/mg. Optimization of glucose concentration yields 21 g/l cell mass with 9770 U enzyme activity/g glucose
synthesis
-
production of carbonyl reductase by Candida viswanathii in 6.6 l fermentor, using controlled pH value at 8.0, aeration rate 1 vvm and an agitation speed of 250 rpm at 25°C. Use of enzyme for preparative scale reduction of N,N-dimethyl-3-keto-2-thienyl-propanamine to (S)-N,N-dimethyl-3-keto-2-thienyl-propanamine
synthesis
-
synthesis of (R)-beta-hydroxynitriles with good optical purity by use of recombinant carbonyl reductase and further conversion to (R)-beta-hydroxy carboxylic acids via a nitrilase-catalyzed hydrolysis
synthesis
enzyme product ethyl (S)-4-chloro-3-hydroxybutanoate is a chiral compound valuable as a building block for pharmaceuticals
synthesis
-
synthesis of (3S)-acetoin in a coupled system consisting of glucose dehydrogenase from Bacillus subtilis 168 and the NADPH-dependent carbonyl reductase. Under the optimal conditions, 12.2 g/l (3S)-acetoin is produced from 14.3 g/l diacetyl in 75 min
synthesis
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
synthesis
-
coexpression with glucose dehydrogenase from Bacillus subtilis for NADPH regeneration in Escherichia coli and optimization of linker peptides used for the fusion expression of carbonyl reductase and glucose dehydrogenase. Up to 297.3 g/L (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol with enantiopurity >99.9% ee is produced via reduction of 1.2 M of substrate with a 96.7% yield and productivity of 29.7 g/(L h)
synthesis
in situ expression in Candida leads to over fourfold higher activity for conversion of racemic (R,S)-1-phenyl-1,2-ethanediol to 2-hydroxyacetophenone, while maintaining the activity for catalyzing 2-hydroxyacetophenone to (S)-1-phenyl-1,2-ethanediol. A recombinant Candida parapsilosis converts racemic (R,S)-1-phenyl-1,2-ethanediol to its (S)-isomer with an optical purity of 98.8% and a yield of 48.4%. The biotransformation duration is reduced from 48 to 13 h
synthesis
Starmerella magnoliae AKU4643
-
enzyme product ethyl (S)-4-chloro-3-hydroxybutanoate is a chiral compound valuable as a building block for pharmaceuticals
-
synthesis
Geotrichum candidum NCIM 980
-
production of Geotrichum candidum carbonyl reductase in a laboratory scale stirred tank bioreactor, optimization of conditions. At controlled pH value of 5.5 the specific enzyme activity is highest with 306 U/mg. Optimization of glucose concentration yields 21 g/l cell mass with 9770 U enzyme activity/g glucose
-
synthesis
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
-
synthesis
-
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
-
synthesis
-
synthesis of (3S)-acetoin in a coupled system consisting of glucose dehydrogenase from Bacillus subtilis 168 and the NADPH-dependent carbonyl reductase. Under the optimal conditions, 12.2 g/l (3S)-acetoin is produced from 14.3 g/l diacetyl in 75 min
-
EXTERNAL LINKS (specific for EC-Number 1.1.1.184)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
