Effects of Gln102Arg and Cys97Gly mutations on the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus
…, MA Luyten, W Parris, M Gold, CM Kay…
文献索引：Kallwass, Helmut K. W.; Luyten, Marcel A.; Parris, Wendy; Gold, Marvin; Kay, Cyril M.; Bryan Jones Journal of the American Chemical Society, 1992 , vol. 114, # 12 p. 4551 - 4557
Abstract: The L-lactate dehydrogenase of Bacillus stearothermophilus (BSLDH) is a thermostable enzyme with considerable potential for applications in asymmetric synthesis. An understanding of the factors controlling its structural specificity and stereospecificity is therefore of interest. In this paper the effects of Gln102-Arg and Cys97-Gly mutations have been evaluated. In a survey of thirteen 2-keto acids, the Q102R mutation was found to ...
