Recombinant D-amino Acid Oxidase with Improved Properties

Abstract:

D-amino acid oxidase from Trigonopsis variabilis (TvDAAO) was overproduced in E. coli cells and properties of the recombinant enzyme were studied. Single point mutants of the enzyme with 2.4-fold higher thermal stability or changed spectra of substrate specificity compared to wild-type enzyme were prepared. It was shown that mutant TvDAAO has higher catalytic efficiency in cephalosporin C oxidation in comparison with wild-type enzyme. One mutant of recombinant TvDAAO was crystallized and its structure was solved with resolution 2.8 ?.