期刊
MOLECULES
卷 22, 期 12, 页码 -出版社
MDPI
DOI: 10.3390/molecules22122205
关键词
biocatalysis; alcohol oxidation; aldehyde oxidation; flavoprotein oxidase; protein design
资金
- Austrian Science Fund (FWF) within the DK Molecular Enzymology [W901]
- Austrian BMWFW
- BMVIT
- SFG
- Standortagentur Tirol
- Government of Lower Austria
- ZIT through the Austrian FFG-COMET-Funding Program
The oxidation of alcohols to the corresponding carbonyl or carboxyl compounds represents a convenient strategy for the selective introduction of electrophilic carbon centres into carbohydrate-based starting materials. The O-2-dependent oxidation of prim-alcohols by flavin-containing alcohol oxidases often yields mixtures of aldehyde and carboxylic acid, which is due to over-oxidation of the aldehyde hydrate intermediate. In order to directly convert alcohols into carboxylic acids, rational engineering of 5-(hydroxymethyl)furfural oxidase was performed. In an attempt to improve the binding of the aldehyde hydrate in the active site to boost aldehyde-oxidase activity, two active-site residues were exchanged for hydrogen-bond-donating and -accepting amino acids. Enhanced over-oxidation was demonstrated and Michaelis-Menten kinetics were performed to corroborate these findings.
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