Design of Artificial Alcohol Oxidases: Alcohol Dehydrogenase-NADPH Oxidase Fusions for Continuous Oxidations.
Alcohol Dehydrogenase
/ chemistry
Alcohol Oxidoreductases
/ chemistry
Animals
Armoracia
/ enzymology
Benzyl Alcohols
/ chemistry
Biocatalysis
Cattle
Cyclohexanols
/ chemistry
Escherichia coli
/ genetics
Levilactobacillus brevis
/ enzymology
Micrococcus
/ enzymology
Multifunctional Enzymes
/ chemistry
NADPH Oxidases
/ chemistry
Oxidation-Reduction
Protein Engineering
Recombinant Fusion Proteins
/ chemistry
Thermoanaerobacter
/ enzymology
alcohol dehydrogenases
biocatalysis
enzyme engineering
fusion enzymes
oxidases
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
02 01 2019
02 01 2019
Historique:
received:
24
07
2018
pubmed:
6
9
2018
medline:
4
12
2019
entrez:
6
9
2018
Statut:
ppublish
Résumé
To expand the arsenal of industrially applicable oxidative enzymes, fusions of alcohol dehydrogenases with an NADPH-oxidase were designed. Three different alcohol dehydrogenases (LbADH, TbADH, ADHA) were expressed with a thermostable NADPH-oxidase fusion partner (PAMO C65D) and purified. The resulting bifunctional biocatalysts retained the catalytic properties of the individual enzymes, and acted essentially like alcohol oxidases: transforming alcohols to ketones by using dioxygen as mild oxidant, while merely requiring a catalytic amount of NADP
Identifiants
pubmed: 30184296
doi: 10.1002/cbic.201800421
pmc: PMC6899577
doi:
Substances chimiques
Benzyl Alcohols
0
Cyclohexanols
0
Multifunctional Enzymes
0
Recombinant Fusion Proteins
0
methylphenyl carbinol
E6O895DQ52
Alcohol Oxidoreductases
EC 1.1.-
Alcohol Dehydrogenase
EC 1.1.1.1
alcohol oxidase
EC 1.1.3.13
NADPH Oxidases
EC 1.6.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
51-56Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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