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Literature summary for 1.1.1.B4 extracted from

  • Zhou, S.; Zhang, S.C.; Lai, D.Y.; Zhang, S.L.; Chen, Z.M.
    Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans (2013), Biotechnol. Lett., 35, 359-365.
    View publication on PubMed

Application

Application Comment Organism
synthesis ethyl benzoylformate is asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95% conversion and in an enantiomeric excess of 99.9% Carboxydothermus hydrogenoformans

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Carboxydothermus hydrogenoformans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3
-
ethyl 2-oxopropanoate pH 6.5, 50°C Carboxydothermus hydrogenoformans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
x * 30000, SDS-PAGE and calculated Carboxydothermus hydrogenoformans

Organic Solvent Stability

Organic Solvent Comment Organism
Acetone 10% v/v, 30% residual activity Carboxydothermus hydrogenoformans
DMSO 10% v/v, 50% residual activity Carboxydothermus hydrogenoformans
Ethanol 10% v/v, 50% residual activity Carboxydothermus hydrogenoformans
tetrahydrofuran 10% v/v, 25% residual activity Carboxydothermus hydrogenoformans

Organism

Organism UniProt Comment Textmining
Carboxydothermus hydrogenoformans Q3ACV3
-
-
Carboxydothermus hydrogenoformans DSM 6008 Q3ACV3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylpentan-2-one + NADH + H+ 46% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans 4-methylpentan-2-ol + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
4-methylpentan-2-one + NADH + H+ 46% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans DSM 6008 4-methylpentan-2-ol + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
cycloheptanone + NADH + H+ 69% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans cycloheptanol + NAD+
-
?
cycloheptanone + NADH + H+ 69% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans DSM 6008 cycloheptanol + NAD+
-
?
ethyl 2-oxo-3-phenylpropanoate + NADH + H+ 48% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl 2-hydroxy-3-phenylpropanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl 2-oxo-4-phenylbutanoate + NADH + H+ 135% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl 2-hydroxy-4-phenylbutanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl 2-oxopropanoate + NADH + H+
-
Carboxydothermus hydrogenoformans ethyl 2-hydroxypropanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl 3-oxohexanoate + NADH + H+ 105% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl 3-hydroxyhexanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl 4-chloro-3-oxobutanoate + NADH + H+ 129% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl 4-chloro-3-hydroxybutanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl 4-chloro-3-oxobutanoate + NADH + H+ 129% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans DSM 6008 ethyl 4-chloro-3-hydroxybutanoate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
ethyl benzoylformate + NADH + H+ 270% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl (R)-mandelate + NAD+ 95% conversion with 99.9% enantiomeric excess ?
ethyl benzoylformate + NADH + H+ 270% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans DSM 6008 ethyl (R)-mandelate + NAD+ 95% conversion with 99.9% enantiomeric excess ?
ethyl oxo(phenyl)acetate + NADH + H+ 270% of the activity with ethyl 2-oxopropanoate Carboxydothermus hydrogenoformans ethyl hydroxy(phenyl)acetate + NAD+ chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate ?
additional information enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters Carboxydothermus hydrogenoformans ?
-
?
additional information enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters Carboxydothermus hydrogenoformans DSM 6008 ?
-
?

Subunits

Subunits Comment Organism
? x * 30000, SDS-PAGE and calculated Carboxydothermus hydrogenoformans

Synonyms

Synonyms Comment Organism
CHY1186
-
Carboxydothermus hydrogenoformans
SDR
-
Carboxydothermus hydrogenoformans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
Carboxydothermus hydrogenoformans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.97
-
ethyl 2-oxopropanoate pH 6.5, 50°C Carboxydothermus hydrogenoformans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Carboxydothermus hydrogenoformans

Cofactor

Cofactor Comment Organism Structure
NADH preferred over NADPH Carboxydothermus hydrogenoformans
NADPH about 10% of the activity with NADH Carboxydothermus hydrogenoformans