Journal
FEBS LETTERS
Volume 580, Issue 16, Pages 3867-3871Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.06.012
Keywords
ancestral residue; protein stability; 3-isopropylmalate dehydrogenase; Thermus thermophilus
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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 (Leul34Asn/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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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