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Information on EC 1.1.1.320 - benzil reductase [(S)-benzoin forming] and Organism(s) Bacillus cereus and UniProt Accession Q8RJB2

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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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This record set is specific for:
Bacillus cereus
UNIPROT: Q8RJB2
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Word Map
The taxonomic range for the selected organisms is: Bacillus cereus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
benzil reductase, kred1-pglu, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
benzil reductase
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
422524-67-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-benzoin + NADP+
benzil + NADPH + H+
show the reaction diagram
stereospecific asymmetric reduction of benzil to (S)-benzoin
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-
r
(S)-benzoin + NADP+
benzil + NADPH + H+
show the reaction diagram
1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
1-phenyl-1,2-propanedione + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
2-hydroxy-1-phenyl-1-propanone + NADP+
1-phenylpropane-1,2-dione + NADPH + H+
show the reaction diagram
-
-
-
-
?
sec-phenethyl alcohol + NADP+
1-phenylethanone + NADPH + H+
show the reaction diagram
-
-
-
-
?
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-benzoin + NADP+
benzil + NADPH + H+
show the reaction diagram
stereospecific asymmetric reduction of benzil to (S)-benzoin
-
-
r
(S)-benzoin + NADP+
benzil + NADPH + H+
show the reaction diagram
-
stereospecific asymmetric reduction of benzil to (S)-benzoin
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042
1-phenyl-1,2-propanedione
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recombinant enzyme, pH 6.5, 37°C
0.768
benzil
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recombinant enzyme, pH 6.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.75
1-phenyl-1,2-propanedione
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recombinant enzyme, pH 6.5, 37°C
1.07
benzil
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recombinant enzyme, pH 6.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65.33
1-phenyl-1,2-propanedione
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recombinant enzyme, pH 6.5, 37°C
1.4
benzil
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recombinant enzyme, pH 6.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
assay at, oxidation reaction
6.5
-
assay at, reduction reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
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amino acid differences in the benzil reductase among Bacillus cereus strains
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BZRD_BACCE
249
0
27960
Swiss-Prot
-
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
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
expression of GFP-tagged enzyme in Bacillus cereus strain IFO3563, subcloning in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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asymmetric reduction with Bacillus cereus benzil reductase can be utilized to produce important chiral compounds
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team