期刊
ACS CATALYSIS
卷 5, 期 3, 页码 1833-1839出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.5b00031
关键词
5-hydroxymethylfurfural oxidase; enzyme; 2,5-furandicarboxylic acid; biocatalysis; protein engineering; crystal structure
资金
- Dutch Ministry of Economic Affairs, Agriculture, and Innovation (ELI)
- BioStruct-X program [5275, 7551]
5-Hydroxymethylfurfural oxidase (HMFO) is a flavin-dependent enzyme that catalyzes the oxidation of many aldehydes, primary alcohols, and thiols. The three-step conversion of S-hydroxymethylfurfural to 2,5-furandicarboxylic acid is relevant for the industrial production of biobased polymers. The remarkable wide substrate scope of HMFO contrasts with the enzyme's precision in positioning the substrate to perform catalysis. We have solved the crystal structure of HMFO at 1.6 angstrom resolution, which guided mutagenesis experiments to probe the role of the active-site residues in catalysis. Mutations targeting two active-site residues generated engineered forms of HMFO with promising catalytic features, namely enantioselective activities on secondary alcohols and improved 2,5-furandicarboxylic acid yields.
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