An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillus stearothermophilus

…, MA Luyten, H Wynn, LR Provencher…

Index: Bur; Luyten; Wynn; Provencher; Jones; Gold; Friesen; Clarke; Holbrook Canadian Journal of Chemistry, 1989 , vol. 67, # 6 p. 1065 - 1070

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Citation Number: 35

Abstract

The potential utility of the l-lactate dehydrogenase of Bacillus stearothermophilus (BSLDH) for stereospecific, preparative-scale reductions of α-keto acids to (S)-α-hydroxy acids of> 99% ee has been demonstrated. BSLDH is a stable, thermophilic, enzyme whose gene has been cloned into a high-expression vector to assure its plentiful supply. Its specificity for keto acid substrates possessing straight-and branched-chain alkyl, cyclopropyl, or phenyl ...

~78%

~85%

~86%

~91%

~10%

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