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Literature summary for 1.1.1.1 extracted from

  • Shah, S.; Agera, R.; Sharma, P.; Sunder, A.; Bajwa, H.; James, H.; Gaikaiwari, R.; Wangikar, P.
    Development of biotransformation process for asymmetric reduction with novel anti-Prelog NADH-dependent alcohol dehydrogenases (2018), Process Biochem., 70, 71-78 .
No PubMed abstract available
Search for more literature for 1.1.1.1

Application

Application Comment Organism
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Acetobacter aceti catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Acetobacter aceti
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Aminobacter aminovorans slightly catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Aminobacter aminovorans
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Gluconobacter diazotrophicus slightly catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Gluconacetobacter diazotrophicus
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Komagataeibacter medellinensis catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Komagataeibacter medellinensis
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenase. The enzyme from Komagataeibacter xylinus catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Komagataeibacter xylinus
synthesis development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. The enzyme from Acetobacter senegalensis catalyzes the formation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), a key chiral intermediate in the synthesis of HMG-CoA reductase inhibitors (cholesterol lowering drugs like lipitor), slagenins B, slagenins C, and 1,4-dihydropyridine type beta-blockers Acetobacter senegalensis

Cloned(Commentary)

Cloned (Comment) Organism
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Acetobacter aceti
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Gluconacetobacter diazotrophicus
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Komagataeibacter medellinensis
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Aminobacter aminovorans
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Acetobacter senegalensis
recombinant soluble enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Komagataeibacter xylinus

Protein Variants

Protein Variants Comment Organism
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE) Gluconacetobacter diazotrophicus
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE) Komagataeibacter medellinensis
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE) Aminobacter aminovorans
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE) Acetobacter senegalensis
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), process optimization, overview Acetobacter aceti
additional information biotransformation studies with the recombinant enzyme expressed in Escherichia coli strain BL21(DE3) cells using the cell culture. Asymmetric biotransformation of (S)-ethyl-4-chloro-3-hydroxybutanoate ((S)-CHBE), process optimization, overview Komagataeibacter xylinus

Organism

Organism UniProt Comment Textmining
Acetobacter aceti
-
-
-
Acetobacter senegalensis A0A0U5FNC1
-
-
Aminobacter aminovorans A0A380WRS7
-
-
Gluconacetobacter diazotrophicus
-
-
-
Komagataeibacter medellinensis G2I689
-
-
Komagataeibacter medellinensis NBRC 3288 G2I689
-
-
Komagataeibacter xylinus A0A3T0KHC6
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Aminobacter aminovorans
5.7
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Gluconacetobacter diazotrophicus
6.3
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Acetobacter senegalensis
9.9
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Komagataeibacter medellinensis
11.4
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Komagataeibacter xylinus
66
-
 recombinant enzyme, crude Escherichia coli cell extract, substrate ethyl 4-chloro-3-oxobutanoate, pH 7.0, 30°C Acetobacter aceti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-pentanone + NADH + H+
-
 Acetobacter aceti 2-pentanol + NAD+
-
 ?
2-pentanone + NADH + H+
-
 Gluconacetobacter diazotrophicus 2-pentanol + NAD+
-
 ?
2-pentanone + NADH + H+
-
 Komagataeibacter medellinensis 2-pentanol + NAD+
-
 ?
2-pentanone + NADH + H+
-
 Acetobacter senegalensis 2-pentanol + NAD+
-
 ?
2-pentanone + NADH + H+
-
 Komagataeibacter xylinus 2-pentanol + NAD+
-
 ?
2-pentanone + NADH + H+
-
 Komagataeibacter medellinensis NBRC 3288 2-pentanol + NAD+
-
 ?
4-bromoacetophenone + NADH + H+
-
 Acetobacter aceti 1-(4-bromophenyl)ethanol + NAD+
-
 ?
4-bromoacetophenone + NADH + H+
-
 Gluconacetobacter diazotrophicus 1-(4-bromophenyl)ethanol + NAD+
-
 ?
4-bromoacetophenone + NADH + H+
-
 Komagataeibacter medellinensis 1-(4-bromophenyl)ethanol + NAD+
-
 ?
4-bromoacetophenone + NADH + H+
-
 Acetobacter senegalensis 1-(4-bromophenyl)ethanol + NAD+
-
 ?
4-bromoacetophenone + NADH + H+
-
 Komagataeibacter xylinus 1-(4-bromophenyl)ethanol + NAD+
-
 ?
4-chloroacetophenone + NADH + H+
-
 Acetobacter aceti 1-(4-chlorophenyl)ethanol + NAD+
-
 ?
4-chloroacetophenone + NADH + H+
-
 Gluconacetobacter diazotrophicus 1-(4-chlorophenyl)ethanol + NAD+
-
 ?
4-chloroacetophenone + NADH + H+
-
 Komagataeibacter medellinensis 1-(4-chlorophenyl)ethanol + NAD+
-
 ?
4-chloroacetophenone + NADH + H+
-
 Acetobacter senegalensis 1-(4-chlorophenyl)ethanol + NAD+
-
 ?
4-chloroacetophenone + NADH + H+
-
 Komagataeibacter xylinus 1-(4-chlorophenyl)ethanol + NAD+
-
 ?
4-fluoroacetophenone + NADH + H+
-
 Acetobacter aceti 1-(4-fluorophenyl)ethanol + NAD+
-
 ?
4-fluoroacetophenone + NADH + H+
-
 Gluconacetobacter diazotrophicus 1-(4-fluorophenyl)ethanol + NAD+
-
 ?
4-fluoroacetophenone + NADH + H+
-
 Komagataeibacter medellinensis 1-(4-fluorophenyl)ethanol + NAD+
-
 ?
4-fluoroacetophenone + NADH + H+
-
 Acetobacter senegalensis 1-(4-fluorophenyl)ethanol + NAD+
-
 ?
4-fluoroacetophenone + NADH + H+
-
 Komagataeibacter xylinus 1-(4-fluorophenyl)ethanol + NAD+
-
 ?
acetone + NADH + H+
-
 Acetobacter aceti propan-2-ol + NAD+
-
 ?
acetone + NADH + H+
-
 Gluconacetobacter diazotrophicus propan-2-ol + NAD+
-
 ?
acetone + NADH + H+
-
 Komagataeibacter medellinensis propan-2-ol + NAD+
-
 ?
acetone + NADH + H+
-
 Acetobacter senegalensis propan-2-ol + NAD+
-
 ?
acetone + NADH + H+
-
 Komagataeibacter xylinus propan-2-ol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Acetobacter aceti 1-phenylethanol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Gluconacetobacter diazotrophicus 1-phenylethanol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Komagataeibacter medellinensis 1-phenylethanol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Acetobacter senegalensis 1-phenylethanol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Komagataeibacter xylinus 1-phenylethanol + NAD+
-
 ?
acetophenone + NADH + H+
-
 Komagataeibacter medellinensis NBRC 3288 1-phenylethanol + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Acetobacter aceti ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Gluconacetobacter diazotrophicus ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter medellinensis ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Aminobacter aminovorans ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Acetobacter senegalensis ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter xylinus ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter medellinensis NBRC 3288 ethyl 3-hydroxybutanoate + NAD+
-
 ?
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase Gluconacetobacter diazotrophicus (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase Komagataeibacter medellinensis (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase Aminobacter aminovorans (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase Acetobacter senegalensis (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase Komagataeibacter xylinus (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
ethyl 4-chloro-3-oxobutanoate + NADH + H+ COBE, ADH performs a enantioselective reduction, reacting as an anti-Prelog reductase. An enantiomeric excess of 99% is achieved in the process Acetobacter aceti (S)-ethyl-4-chloro-3-hydroxybutanoate + NAD+
-
 r
methyl 3-oxobutanoate + NADH + H+
-
 Acetobacter aceti methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Gluconacetobacter diazotrophicus methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter medellinensis methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Aminobacter aminovorans methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Acetobacter senegalensis methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter xylinus methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 3-oxobutanoate + NADH + H+
-
 Komagataeibacter medellinensis NBRC 3288 methyl 3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Acetobacter aceti methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Gluconacetobacter diazotrophicus methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Komagataeibacter medellinensis methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Aminobacter aminovorans methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Acetobacter senegalensis methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
methyl 4-chloro-3-oxobutanoate + NADH + H+
-
 Komagataeibacter xylinus methyl 4-chloro-3-hydroxybutanoate + NAD+
-
 ?
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Gluconacetobacter diazotrophicus ?
-
-
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Komagataeibacter medellinensis ?
-
-
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Aminobacter aminovorans ?
-
-
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Acetobacter senegalensis ?
-
-
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Komagataeibacter xylinus ?
-
-
additional information the NADH-dependent alcohol dehydrogenases from Acetobacter aceti with anti-Prelog stereoselectivity exhibits high specific activity on beta-ketoesters, such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. Development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Acetobacter aceti ?
-
-
additional information development of biotransformation process for asymmetric reduction with anti-Prelog NADH-dependent alcohol dehydrogenases. Product identification using gas chromatography Komagataeibacter medellinensis NBRC 3288 ?
-
-

Synonyms

Synonyms Comment Organism
ADH
-
 Acetobacter aceti
ADH
-
 Gluconacetobacter diazotrophicus
ADH
-
 Komagataeibacter medellinensis
ADH
-
 Aminobacter aminovorans
ADH
-
 Acetobacter senegalensis
ADH
-
 Komagataeibacter xylinus
anti-Prelog reductase
-
 Acetobacter aceti
anti-Prelog reductase
-
 Gluconacetobacter diazotrophicus
anti-Prelog reductase
-
 Komagataeibacter medellinensis
anti-Prelog reductase
-
 Aminobacter aminovorans
anti-Prelog reductase
-
 Acetobacter senegalensis
anti-Prelog reductase
-
 Komagataeibacter xylinus
NADH-dependent alcohol dehydrogenase
-
 Acetobacter aceti
NADH-dependent alcohol dehydrogenase
-
 Gluconacetobacter diazotrophicus
NADH-dependent alcohol dehydrogenase
-
 Komagataeibacter medellinensis
NADH-dependent alcohol dehydrogenase
-
 Aminobacter aminovorans
NADH-dependent alcohol dehydrogenase
-
 Acetobacter senegalensis
NADH-dependent alcohol dehydrogenase
-
 Komagataeibacter xylinus
NADH-dependent anti-Prelog specific ADH
-
 Acetobacter aceti
NADH-dependent anti-Prelog specific ADH
-
 Gluconacetobacter diazotrophicus
NADH-dependent anti-Prelog specific ADH
-
 Komagataeibacter medellinensis
NADH-dependent anti-Prelog specific ADH
-
 Aminobacter aminovorans
NADH-dependent anti-Prelog specific ADH
-
 Acetobacter senegalensis
NADH-dependent anti-Prelog specific ADH
-
 Komagataeibacter xylinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Gluconacetobacter diazotrophicus
30
-
 assay at Komagataeibacter medellinensis
30
-
 assay at Aminobacter aminovorans
30
-
 assay at Acetobacter senegalensis
30
-
 assay at Komagataeibacter xylinus
45
-
-
 Acetobacter aceti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Acetobacter aceti
7
-
 assay at Gluconacetobacter diazotrophicus
7
-
 assay at Komagataeibacter medellinensis
7
-
 assay at Aminobacter aminovorans
7
-
 assay at Acetobacter senegalensis
7
-
 assay at Komagataeibacter xylinus

Cofactor

Cofactor Comment Organism Structure
additional information the activity with NADPH is only 4% compared to that achieved with NADH Acetobacter aceti
NAD+
-
 Acetobacter aceti
NAD+
-
 Gluconacetobacter diazotrophicus
NAD+
-
 Komagataeibacter medellinensis
NAD+
-
 Aminobacter aminovorans
NAD+
-
 Acetobacter senegalensis
NAD+
-
 Komagataeibacter xylinus
NADH a NADH-dependent alcohol dehydrogenase Acetobacter aceti
NADH a NADH-dependent alcohol dehydrogenase Gluconacetobacter diazotrophicus
NADH a NADH-dependent alcohol dehydrogenase Komagataeibacter medellinensis
NADH a NADH-dependent alcohol dehydrogenase Aminobacter aminovorans
NADH a NADH-dependent alcohol dehydrogenase Acetobacter senegalensis
NADH a NADH-dependent alcohol dehydrogenase Komagataeibacter xylinus

General Information

General Information Comment Organism
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Acetobacter aceti
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Gluconacetobacter diazotrophicus
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Komagataeibacter medellinensis
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Acetobacter senegalensis
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Komagataeibacter xylinus
evolution anti-Prelog NADH-dependent alcohol dehydrogenase enzymes are analysed for their specificity and activity on carbonyl substrates from different classes such as beta-ketoesters, aromatic ketones and aliphatic ketones. Acetobacter aceti ADH is highly active on beta-ketoesters such as methyl or ethyl 3-oxobutanoate, with maximum specific activity (66 U/mg) on ethyl 4-chloro-3-oxobutanoate. While the Acetobacter aceti, Aminobacter aminovorans, and Gluconacetobacter diazotrophicus ADH enzymes are more specific for beta-ketoesters, the enzymes from Acetobacter senegalensis, Komagataeibacter xylinus, and Komagataeibacter medellinensis exhibit a broader substrate spectrum with moderate to high preference for acetophenone and its derivatives as well. ADH activity is favoured by the presence of electron-withdrawing halogen substituents F and Cl at para-position on the benzene ring of acetophenone, all the enzymes display significantly reduced activity with 4-bromoacetophenone and exhibit poor activity on the aliphatic substrate pentanone Aminobacter aminovorans