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Previously we cloned and expressed gene of TvDAAO in E.coli cells. Crystals of mutant TvDAAO were prepared and structure was solved with resolution 1.8 Å. Analysis of the enzyme 3D structure revealed potential sites for directed mutagenesis to improve thermal stability and change substrate specificity. More than 20 mutant TvDAAOs were prepared and characterized. It was shown that amino acid substitutions resulted in significant change of thermal stability and provide mutant TvDAAO with different substrate specificity profile. Use for mutant TvDAAOs for fine organic synthesis as well in medicine diagnostics is discussed.