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Protein Engineering vol. 8 no. 1 pp. 39-43, 1995
© 1995 Oxford University Press

RESEARCH-ARTICLE

Thermal stability of chimeric isopropylmalate dehydrogenase genes constructed from a thermophile and a mesophile

Koichi Numata1, Masashi Muro, Nobuko Akutsu, Yoshiaki Nosoh2, Akihiko Yamagishi and Tairo Oshima3

Department of Life Science, Tokyo Institute of Technology Nagatsuta, Yokohama 227, Japan

3To whom correspondence should be addressed

Chimeric isopropylmalate dehydrogenases were constructed by connecting the genes isolated from an extreme thermophile, Thermus thermophilus, and a mesophile, Bacillus subtilis. These genes were expressed in Escherichia coli. The enzymes were purified and analysed. Enzymes of T.thermophilus and B.subtilis and chimeric enzymes showed similar enzymological characteristics except for thermal stability. The stability of each enzyme was approximately proportional to the content of the amino acid sequence from the TJhermophilus enzyme. The results suggested that amino acid residues contributing the thermal stability distribute themselves, in general, evenly at least in the N-terminal half of the amino acid sequence of T.thermophilus isopropylmalate dehydrogenase.

Keywords: Bacillus subtilis/hybrid enzyme/isopropylmalate dehydrogenase/leuB/Thermus thermophilus

Received August 29, 1994; revised September 1, 1994; accepted September 5, 1994.


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