BRENDA - Enzyme Database show
show all sequences of 1.1.1.320

The enzymes with benzil reductase activity conserved from bacteria to mammals

Maruyama, R.; Nishizawa, M.; Itoi, Y.; Ito, S.; Inoue, M.; J. Biotechnol. 94, 157-169 (2002)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
asymmetric reduction with Bacillus cereus benzil reductase can be utilized to produce important chiral compounds
Bacillus cereus
Cloned(Commentary)
Commentary
Organism
expression of GFP-tagged enzyme in Bacillus cereus strain IFO3563, subcloning in Escherichia coli
Bacillus cereus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
0.768
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-benzoin + NADP+
Bacillus cereus
stereospecific asymmetric reduction of benzil to (S)-benzoin
benzil + NADPH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus cereus
-
; diverse strains, overview
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain DH5alpha by ammonium sulfate fractionation
Bacillus cereus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-benzoin + NADP+
stereospecific asymmetric reduction of benzil to (S)-benzoin
717892
Bacillus cereus
benzil + NADPH + H+
-
-
-
r
(S)-benzoin + NADP+
stereospecific asymmetric reduction of benzil to (S)-benzoin, recombinant Bacillus cereus benzil reductase produces optically pure (S)-benzoin with NADPH in vitro
717892
Bacillus cereus
benzil + NADPH + H+
-
-
-
r
1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
1-phenyl-1,2-propanedione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
2-hydroxy-1-phenyl-1-propanone + NADP+
-
717892
Bacillus cereus
1-phenylpropane-1,2-dione + NADPH + H+
-
-
-
?
additional information
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
717892
Bacillus cereus
?
-
-
-
-
sec-phenethyl alcohol + NADP+
-
717892
Bacillus cereus
1-phenylethanone + NADPH + H+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus cereus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.07
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
2.75
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
assay at, reduction reaction
Bacillus cereus
10
-
assay at, oxidation reaction
Bacillus cereus
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Bacillus cereus
NADPH
-
Bacillus cereus
Application (protein specific)
Application
Commentary
Organism
synthesis
asymmetric reduction with Bacillus cereus benzil reductase can be utilized to produce important chiral compounds
Bacillus cereus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of GFP-tagged enzyme in Bacillus cereus strain IFO3563, subcloning in Escherichia coli
Bacillus cereus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Bacillus cereus
NADPH
-
Bacillus cereus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
0.768
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-benzoin + NADP+
Bacillus cereus
stereospecific asymmetric reduction of benzil to (S)-benzoin
benzil + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain DH5alpha by ammonium sulfate fractionation
Bacillus cereus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-benzoin + NADP+
stereospecific asymmetric reduction of benzil to (S)-benzoin
717892
Bacillus cereus
benzil + NADPH + H+
-
-
-
r
(S)-benzoin + NADP+
stereospecific asymmetric reduction of benzil to (S)-benzoin, recombinant Bacillus cereus benzil reductase produces optically pure (S)-benzoin with NADPH in vitro
717892
Bacillus cereus
benzil + NADPH + H+
-
-
-
r
1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
1-phenyl-1,2-propanedione + NADPH + H+
-
717892
Bacillus cereus
? + NADP+
-
-
-
?
2-hydroxy-1-phenyl-1-propanone + NADP+
-
717892
Bacillus cereus
1-phenylpropane-1,2-dione + NADPH + H+
-
-
-
?
additional information
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
717892
Bacillus cereus
?
-
-
-
-
sec-phenethyl alcohol + NADP+
-
717892
Bacillus cereus
1-phenylethanone + NADPH + H+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus cereus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.07
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
2.75
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
assay at, reduction reaction
Bacillus cereus
10
-
assay at, oxidation reaction
Bacillus cereus
General Information
General Information
Commentary
Organism
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family
Bacillus cereus
physiological function
amino acid differences in the benzil reductase among Bacillus cereus strains
Bacillus cereus
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family
Bacillus cereus
physiological function
amino acid differences in the benzil reductase among Bacillus cereus strains
Bacillus cereus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.4
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
65.33
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.4
-
benzil
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
65.33
-
1-phenyl-1,2-propanedione
recombinant enzyme, pH 6.5, 37°C
Bacillus cereus
Other publictions for EC 1.1.1.320
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739919
Contente
Stereoselective reduction of a ...
Ogataea glucozyma
Appl. Microbiol. Biotechnol.
100
193-201
2016
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1
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3
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16
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1
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1
1
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16
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1
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1
1
1
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2
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1
1
717892
Maruyama
The enzymes with benzil reduct ...
Bacillus cereus
J. Biotechnol.
94
157-169
2002
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1
1
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2
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1
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6
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1
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8
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1
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2
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2
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1
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8
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1
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2
2
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2
2
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2
2
717406
Maruyama
Isolation and expression of a ...
Bacillus cereus, Bacillus cereus Tim-r01
Biotechnol. Bioeng.
75
630-633
2001
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