Previously, we showed that mutants of Thermus thermophilus 3-isopropylmalate dehydrogenase (IPMDH) each containing a residue (ancestral residue) that had been predicted to exist in a postulated common ancestor protein often have greater thermal stabilities than does the contemporary wild-type enzyme. In this study, the combined effects of multiple ancestral residues were analyzed. Two mutants, containing multiple mutations, Sup3mut (Val181Thr/Pro324Thr/Ala335Glu) and Sup4mut (Leu134Asn/Val181Thr/Pro324Thr/Ala335Glu) were constructed and show greater thermal stabilities than the wild-type and single-point mutant IPMDHs do. Most of the mutants have similar or improved catalytic efficiencies at 70 degrees C when compared with the wild-type IPMDH. Study holds ProTherm entries: 22914, 22915, 22916, 22917 Extra Details: 0.5 mM EDTA was added in the experiment Ancestral residue; Protein stability; 3-Isopropylmalate dehydrogenase; Thermus thermophilus
ID: PVqRqV6H3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:54 p.m.
Version: 1
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