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Information on EC 1.1.1.320 - benzil reductase [(S)-benzoin forming]
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1.1.1.320 benzil reductase [(S)-benzoin forming]IUBMB Comments
The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency .
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Word Map
- 1.1.1.320
- reductases
-
pichia
- ketoreductase
- sepiapterin
-
stereoselective
- cereus
-
enantioselective
-
non-conventional
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
benzil reductase, kred1-pglu, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzil reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-benzoin + NADP+ = benzil + NADPH + H+
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SYSTEMATIC NAME
IUBMB Comments
(S)-benzoin:NADP+ oxidoreductase
The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency [2].
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CAS REGISTRY NUMBER
COMMENTARY
422524-67-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(2-fluorophenyl)ethanone + NADPH + H+
(1S)-1-(2-fluorophenyl)ethanol + NADP+
76% of the rate with 1-(4-nitrophenyl)ethanone, 97% yield, 94% enantiomeric excess
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-
?
1-(2-nitrophenyl)ethanone + NADPH + H+
(1S)-1-(2-nitrophenyl)ethanol + NADP+
53% of the rate with 1-(4-nitrophenyl)ethanone, 78% yield, 98% enantiomeric excess
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-
?
1-(3-fluorophenyl)ethanone + NADPH + H+
(1S)-1-(3-fluorophenyl)ethanol + NADP+
61% of the rate with 1-(4-nitrophenyl)ethanone, 85% yield, 98% enantiomeric excess
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-
?
1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
? + NADP+
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-
-
-
?
1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
? + NADP+
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-
-
?
1-(4-nitrophenyl)ethanone + NADPH + H+
(1S)-1-(4-nitrophenyl)ethanol + NADP+
100% yield, 98% enantiomeric excess
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-
?
1-(furan-2-yl)ethanone + NADPH + H+
(1S)-1-(furan-2-yl)ethanol + NADP+
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48% of the activity with benzil, 95% yield, 98% enantiomeric excess
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?
1-(pyridin-3-yl)ethanone + NADPH + H+
(S)-(1-pyridin-3yl)ethanol + NADP+
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58% of the activity with benzil, 95% yield, 98% enantiomeric excess
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?
1-(pyridin-3-yl)propan-1-one + NADPH + H+
(S)-1-(pyridin-3-yl)propanol + NADP+
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60% of the activity with benzil, 95% yield, 98% enantiomeric excess
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?
1-(thiophen-2-yl)ethanone + NADPH + H+
(1S)-1-(thiophen-2-yl)ethanol + NADP+
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51% of the activity with benzil, 95% yield, 98% enantiomeric excess
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?
2-acetylbenzonitrile + NADPH + H+
2-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
82% of the rate with 1-(4-nitrophenyl)ethanone, 98% yield, 98% enantiomeric excess
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-
?
2-hydroxy-1-phenyl-1-propanone + NADP+
1-phenylpropane-1,2-dione + NADPH + H+
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-
-
-
?
3-oxo-3-phenylpropanenitrile + NADPH + H+
(3S)-3-hydroxy-3-phenylpropanenitrile + NADP+
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55% of the activity with benzil, 95% yield, 95% enantiomeric excess
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?
4-acetylbenzonitrile + NADPH + H+
4-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
68% of the rate with 1-(4-nitrophenyl)ethanone, 70% yield, 97% enantiomeric excess
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-
?
benzophenone + NADPH + H+
diphenylmethanol + NADP+
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66% yield
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?
ethyl 2-oxo-2-phenylacetate + NADPH + H+
ethyl (2S)-hydroxy(phenyl)acetate + NADP+
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115% yield, 40% enantiomeric excess
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?
(S)-benzoin + NADP+
benzil + NADPH + H+
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stereospecific asymmetric reduction of benzil to (S)-benzoin
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r
(S)-benzoin + NADP+
benzil + NADPH + H+
stereospecific asymmetric reduction of benzil to (S)-benzoin
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r
(S)-benzoin + NADP+
benzil + NADPH + H+
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stereospecific asymmetric reduction of benzil to (S)-benzoin, recombinant Bacillus cereus benzil reductase produces optically pure (S)-benzoin with NADPH in vitro
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r
(S)-benzoin + NADP+
benzil + NADPH + H+
stereospecific asymmetric reduction of benzil to (S)-benzoin
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r
benzil + NADPH + H+
(S)-benzoin + NADP+
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98% enantiomeric excess
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?
additional information
?
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the enzyme is also active with 1,4-naphthoquinone, dichlone, and 4-phenylbenzaldehyde, substrate specificity, overview. 1-acenaphthenol is oxidized, although the kcat/Km ratio is low. No activity with progesterone, daunorubicin, and menaquinone. No or poor activity with benzyl phenyl ketone, benzophenone, dibenzoylmethane, chalcone, 1-phenyl-1,3-butanedione, diacetyl, 3,4-hexanedione, and acetophenone
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?
additional information
?
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for the enantioselective reduction of mono-substituted acetophenones, reaction rates of meta- and para-derivatives are consistent with the electronic effects described by delta-Hammett coefficients. Enantioselectivity is determined by an opposite orientation of the substrate in the binding pocket. Reduction of ortho-derivatives occurs only with substrates bearing substituents with low steric impact, and reactivity is controlled by stereoelectronic features
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?
additional information
?
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for the enantioselective reduction of mono-substituted acetophenones, reaction rates of meta- and para-derivatives are consistent with the electronic effects described by delta-Hammett coefficients. Enantioselectivity is determined by an opposite orientation of the substrate in the binding pocket. Reduction of ortho-derivatives occurs only with substrates bearing substituents with low steric impact, and reactivity is controlled by stereoelectronic features
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?
additional information
?
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the enzyme prefers space-demanding substrates, which are often converted with high stereoselectivity
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?
additional information
?
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the enzyme prefers space-demanding substrates, which are often converted with high stereoselectivity
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?
additional information
?
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the enzyme is preferentiallly active on aromatic 1,2-diketones. It catalyzes the stereoselective monoreduction and desymmerization of bulky dicarbonyls. Mechanism and in silico prediction of substrates reactivity, overview
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additional information
?
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the enzyme is preferentiallly active on aromatic 1,2-diketones. It catalyzes the stereoselective monoreduction and desymmerization of bulky dicarbonyls. Mechanism and in silico prediction of substrates reactivity, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-benzoin + NADP+
benzil + NADPH + H+
-
stereospecific asymmetric reduction of benzil to (S)-benzoin
-
-
r
(S)-benzoin + NADP+
benzil + NADPH + H+
stereospecific asymmetric reduction of benzil to (S)-benzoin
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-
r
(S)-benzoin + NADP+
benzil + NADPH + H+
stereospecific asymmetric reduction of benzil to (S)-benzoin
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-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
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amino acid differences in the benzil reductase among Bacillus cereus strains
evolution
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the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family
evolution
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the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family
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Show AA Sequence and Transmembrane Helices (358 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.
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme KRED1-Pglu, X-ray diffraction structure determination and analysis at 1.77 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain DH5alpha by ammonium sulfate fractionation
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GFP-tagged enzyme in Bacillus cereus strain IFO3563, subcloning in Escherichia coli
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gene yueD, Bacillus cereus library screening in Escherichia coli and cloning of the gene encoding the benzil reductase, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain DH5alpha
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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asymmetric reduction with Bacillus cereus benzil reductase can be utilized to produce important chiral compounds
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruyama, R.; Nishizawa, M.; Itoi, Y.; Ito, S.; Inoue, M.
Isolation and expression of a Bacillus cereus gene encoding benzil reductase
Biotechnol. Bioeng.
75
630-633
2001
Bacillus cereus (Q8RJB2), Bacillus cereus, Bacillus cereus Tim-r01 (Q8RJB2)
brenda
Maruyama, R.; Nishizawa, M.; Itoi, Y.; Ito, S.; Inoue, M.
The enzymes with benzil reductase activity conserved from bacteria to mammals
J. Biotechnol.
94
157-169
2002
Bacillus cereus
brenda
Contente, M.L.; Serra, I.; Brambilla, M.; Eberini, I.; Gianazza, E.; De Vitis, V.; Molinari, F.; Zambelli, P.; Romano, D.
Stereoselective reduction of aromatic ketones by a new ketoreductase from Pichia glucozyma
Appl. Microbiol. Biotechnol.
100
193-201
2016
Ogataea glucozyma (A0A0H4SN47), Ogataea glucozyma
brenda
Rabuffetti, M.; Cannazza, P.; Contente, M.; Pinto, A.; Romano, D.; Hoyos, P.; Alcantara, A.; Eberini, I.; Laurenzi, T.; Gourlay, L.; Di Pisa, F.; Molinari, F.
Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction
Bioorg. Chem.
108
104644
2021
Ogataea glucozyma (A0A0H4SN47), Ogataea glucozyma
brenda
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