Article
Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus.
Protein engineering - 1 Jun 2002
Suzuki Toshiharu, Yasugi Masako, Arisaka Fumio, Oshima Tairo, Yamagishi Akihiko
Abstract excerpt
Random mutagenesis of Thermus thermophilus 3-isopropylmalate dehydrogenase revealed that a substitution of Val126Met in a hinge region caused a marked increase in specific activity, particularly at low temperatures, although the site is far from the binding residues for 3-isopropylmalate and NAD. To understand the molecular mechanism, residue 126 was substituted with one of eight other residues, Gly, Ala, Ser,...
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