Sakurai M, Onodera K, Moriyama H, Matsumoto O, Tanaka N, Numata K, Imada K, Sato M, Katsube Y, Oshima T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa.
J Biochem. 1992 Aug;112(2):173-4. doi: 10.1093/oxfordjournals.jbchem.a123873.
A new type of chimeric 3-isopropylmalate dehydrogenase (2T2M6T) was produced by expressing the fused gene of Bacillus subtilis and Thermus thermophilus. The enzyme shows heat stability intermediate between those of the parents. The crystal of the enzyme belongs to the space group of P3(2)21, with cell dimensions of a = b = 78.9 A and c = 158.9 A. Two thermostable mutants of the chimeric enzyme were prepared by site-directed mutagenesis and then crystallized.
通过表达枯草芽孢杆菌和嗜热栖热菌的融合基因,产生了一种新型嵌合3-异丙基苹果酸脱氢酶(2T2M6T)。该酶的热稳定性介于亲本之间。该酶的晶体属于P3(2)21空间群,晶胞参数为a = b = 78.9 Å,c = 158.9 Å。通过定点诱变制备了该嵌合酶的两个热稳定突变体,然后使其结晶。