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Literature summary extracted from

  • Maruyama, R.; Nishizawa, M.; Itoi, Y.; Ito, S.; Inoue, M.
    The enzymes with benzil reductase activity conserved from bacteria to mammals (2002), J. Biotechnol., 94, 157-169.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.320 synthesis asymmetric reduction with Bacillus cereus benzil reductase can be utilized to produce important chiral compounds Bacillus cereus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.320 expression of GFP-tagged enzyme in Bacillus cereus strain IFO3563, subcloning in Escherichia coli Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.320 0.042
-
 1-phenyl-1,2-propanedione recombinant enzyme, pH 6.5, 37°C Bacillus cereus
1.1.1.320 0.768
-
 benzil recombinant enzyme, pH 6.5, 37°C Bacillus cereus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.320 (S)-benzoin + NADP+ Bacillus cereus stereospecific asymmetric reduction of benzil to (S)-benzoin benzil + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.320 Bacillus cereus
-
-
-
1.1.1.320 Bacillus cereus
-
 diverse strains, overview
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.320 recombinant enzyme from Escherichia coli strain DH5alpha by ammonium sulfate fractionation Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.320 (S)-benzoin + NADP+ stereospecific asymmetric reduction of benzil to (S)-benzoin Bacillus cereus benzil + NADPH + H+
-
 r
1.1.1.320 (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 Bacillus cereus benzil + NADPH + H+
-
 r
1.1.1.320 1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
 Bacillus cereus ? + NADP+
-
 ?
1.1.1.320 1-(4-methyl-phenyl)-2-phenyl-ethane-1,2-dione + NADPH + H+
-
 Bacillus cereus ? + NADP+
-
 ?
1.1.1.320 1-phenyl-1,2-propanedione + NADPH + H+
-
 Bacillus cereus ? + NADP+
-
 ?
1.1.1.320 2-hydroxy-1-phenyl-1-propanone + NADP+
-
 Bacillus cereus 1-phenylpropane-1,2-dione + NADPH + H+
-
 ?
1.1.1.320 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 Bacillus cereus ?
-
 ?
1.1.1.320 sec-phenethyl alcohol + NADP+
-
 Bacillus cereus 1-phenylethanone + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.320 benzil reductase
-
 Bacillus cereus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.320 37
-
 assay at Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.320 1.07
-
 benzil recombinant enzyme, pH 6.5, 37°C Bacillus cereus
1.1.1.320 2.75
-
 1-phenyl-1,2-propanedione recombinant enzyme, pH 6.5, 37°C Bacillus cereus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.320 6.5
-
 assay at, reduction reaction Bacillus cereus
1.1.1.320 10
-
 assay at, oxidation reaction Bacillus cereus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.320 NADP+
-
 Bacillus cereus
1.1.1.320 NADPH
-
 Bacillus cereus

General Information

EC Number General Information Comment Organism
1.1.1.320 evolution the enzyme is a member of the short-chain dehydrogenase/reductase, SDR, family Bacillus cereus
1.1.1.320 physiological function amino acid differences in the benzil reductase among Bacillus cereus strains Bacillus cereus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.320 1.4
-
 benzil recombinant enzyme, pH 6.5, 37°C Bacillus cereus
1.1.1.320 65.33
-
 1-phenyl-1,2-propanedione recombinant enzyme, pH 6.5, 37°C Bacillus cereus