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Literature summary for 1.1.1.320 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

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

Cloned(Commentary)

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

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-
Bacillus cereus
-
diverse strains, overview
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
benzil reductase
-
Bacillus cereus

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment 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 Comment Organism
6.5
-
assay at, reduction reaction Bacillus cereus
10
-
assay at, oxidation reaction Bacillus cereus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Bacillus cereus
NADPH
-
Bacillus cereus

General Information

General Information Comment 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 Comment 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