Conversion of the dimeric D‐amino acid oxidase from Rhodotorula gracilis to a monomeric form. A rational mutagenesis approach

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Abstract
The relevance of the dimeric state for the structure/function relationships of Rhodotorula gracilis D‐amino acid oxidase (RgDAAO) holoenzyme has been investigated by rational mutagenesis. Deletion of 14 amino acids in a surface loop (connecting β‐strands 12 and 13) transforms RgDAAO from a dimeric protein into a stable monomer. The mutant enzyme is still catalytically competent and retains its binding with the FAD coenzyme. Dimerization has been used by this flavoenzyme in evolution to achieve maximal activity, a tighter interaction between the protein moiety and the coenzyme, and higher thermal stability.