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Literature summary for 1.1.3.13 extracted from

  • Aalbers, F.S.; Fraaije, M.W.
    Design of artificial alcohol oxidases alcohol dehydrogenase-NADPH oxidase fusions for continuous oxidations (2019), ChemBioChem, 20, 51-56 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.13

Application

Application Comment Organism
synthesis expression of alcohol dehydrogenase with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D). The resulting bifunctional biocatalysts retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidases, while merely requiring a catalytic amount of NADP+ Levilactobacillus brevis
synthesis expression of alcohol dehydrogenase with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D). The resulting bifunctional biocatalysts retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidases, while merely requiring a catalytic amount of NADP+ Thermoanaerobacter brockii

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Levilactobacillus brevis
expression in Escherichia coli Thermoanaerobacter brockii

Protein Variants

Protein Variants Comment Organism
additional information alcohol dehydrogenase is expressed with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D) and purified. The resulting bifunctional biocatalyst retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidase, while merely requiring a catalytic amount of NADP+ Levilactobacillus brevis
additional information alcohol dehydrogenase is expressed with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D) and purified. The resulting bifunctional biocatalyst retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidase, while merely requiring a catalytic amount of NADP+ Thermoanaerobacter brockii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7
-
 Cyclohexanol wild-type, pH 7.5, 25°C Thermoanaerobacter brockii
5.8
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Thermoanaerobacter brockii
29
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Levilactobacillus brevis
31
-
 Cyclohexanol wild-type, pH 7.5, 25°C Levilactobacillus brevis

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis
-
-
-
Thermoanaerobacter brockii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclohexanol + O2
-
 Levilactobacillus brevis cyclohexanal + H2O2
-
 ?
cyclohexanol + O2
-
 Thermoanaerobacter brockii cyclohexanal + H2O2
-
 ?
rac-1-phenylethanol + O2
-
 Levilactobacillus brevis acetophenone + H2O2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Levilactobacillus brevis
2.2
-
 Cyclohexanol wild-type, pH 7.5, 25°C Levilactobacillus brevis
5.7
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Thermoanaerobacter brockii
8.3
-
 Cyclohexanol wild-type, pH 7.5, 25°C Thermoanaerobacter brockii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.069
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Levilactobacillus brevis
0.071
-
 Cyclohexanol wild-type, pH 7.5, 25°C Levilactobacillus brevis
0.98
-
 Cyclohexanol fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C Thermoanaerobacter brockii
2.2
-
 Cyclohexanol wild-type, pH 7.5, 25°C Thermoanaerobacter brockii