Thermostable proteins designed by using phylogenetic trees

抄録

We have recently developed the way of designing substitutions that can improve thermostability of proteins. The method uses phylogenetic analysis of sequences of family enzymes. It is possible to infer ancestral residues possessed by Commonote, the common ancestor of all the living organisms. The ancestral residues are then introduced to the sequence of contemporary enzyme. The mutant enzymes were analyzed and compared with original enzymes. The results suggested that the ancestral residues tend to improve tharmostablity of proteins. In this report we discuss the results reported on the 3-isopropylmalate dehydrogenase and isocitrate dehydrogenase. The results suggest that the method is applicable to wider variety of proteins.