An evaluation of the substrate specificity, and of its modification by site-directed mutagenesis, of the cloned L-lactate dehydrogenase from Bacillus stearothermophilus

MA Luyten, D Bur, H Wynn, W Parris…

文献索引：Luyten, Marcel A.; Bur, Daniel; Wynn, Hla; Parris, Wendy; Glod, Marvin; et al. Journal of the American Chemical Society, 1989 , vol. 111, # 17 p. 6800 - 6804

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被引用次数: 29

摘要

Abstract: The L-lactate dehydrogenase of Bacillus stearothermophilus (BSLDH) is a stable, thermophilic oxidoreductase. It has been selected as a model of enzymes with considerable future promise in asymmetric synthesis in that it has been cloned to ensure a plentiful and inexpensive supply and because of the potential for tailoring its specificity to accept unnatural substrate structures via the site-directed mutagenesis techniques of molecular ...