cover illustration The locations of the mutations inducing low-temperature activation of the hyperthermostable Sulfolobus tokodaii 3-isopropylmalate dehydrogenase and the homologous Thermus thermophilus enzyme. The low-temperature activated mutants were selected after random mutagenesis. The locations and properties of the mutations found for the selected mutants of S. tokodaii enzyme are compared with those of the homologous Thermus thermophilus enzyme. The mutations are distributed throughout their tertiary structures. These enzymes seemed to adapt to lower temperatures by different kinetic mechanisms. Therefore, there may be many ways to achieve low-temperature adaptation. For further details please see Sasaki et al., pp. 721-727.
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