ArticleChembiochem : a European journal of chemical biology2019
Design of Artificial Alcohol Oxidases: Alcohol Dehydrogenase-NADPH Oxidase Fusions for Continuous Oxidations.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Regeneration of cofactor NAD(P)Frontiers in bioengineering and biotechnology · 2025Review
- Biocatalysis enables the scalable conversion of biobased furans into various furfurylamines.Nature communications · 2024Article
- Constructing an artificial short route for cell-free biosynthesis of the phenethylisoquinoline scaffold.Synthetic and systems biotechnology · 2023Article
- Artificial Fusions between P450 BM3 and an Alcohol Dehydrogenase for Efficient (+)-Nootkatone Production.Chembiochem : a European journal of chemical biology · 2022Article
- Modular Assembly of Phosphite Dehydrogenase and Phenylacetone Monooxygenase for Tuning Cofactor Regeneration.Biomolecules · 2021Article
- Efficient whole-cell oxidation of α,β-unsaturated alcohols to α,β-unsaturated aldehydes through the cascade biocatalysis of alcohol dehydrogenase, NADPH oxidase and hemoglobin.Microbial cell factories · 2021Article
- Engineering natural and noncanonical nicotinamide cofactor-dependent enzymes: design principles and technology development.Current opinion in biotechnology · 2020Review
- High-Throughput Fluorescence Assay for Ketone Detection and Its Applications in Enzyme Mining and Protein Engineering.ACS omega · 2020Article
- Design of Artificial Alcohol Oxidases: Alcohol Dehydrogenase-NADPH Oxidase Fusions for Continuous Oxidations.Chembiochem : a European journal of chemical biology · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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