Facile synthesis of chiral 2-hydroxy acids catalyzed by a stable duck epsilon-crystallin with endogenous L-lactate dehydrogenase activity.
Duck epsilon-crystallin, an abundant structural protein in lenses of some avian species, was shown to possess a genuine and stable L-lactate dehydrogenase (L-LDH; EC 1.1.1.27) activity suitable for the application to enzyme technology as a catalyst for the synthesis of chiral alpha-hydroxy acids. Two pharmaceutically important intermediates, 2-hydroxy acids (S)-2-hydroxybutanoic acid (S)-2-hydroxypentanoic acid have been synthesized in high yields and optical purity utilizing an in situ NADH regeneration system of duck epsilon-crystallin coupled with formate/formate dehydrogenase. This enzyme system is also shown to offer some advantages over the conventional L-LDH sources from several mammalian species.
Wu
C Y
CY
Institute of Biochemical Sciences, National Taiwan University, Taipei.
Chen
S T
ST
Chiou
S H
SH
Wang
K T
KT
D000818:Animals; D003459:Crystallins / Q000378:metabolism*; D004372:Ducks; D004795:Enzyme Stability; D006885:Hydroxybutyrates / Q000138:chemical synthesis*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D010421:Pentanoic Acids / Q000138:chemical synthesis*
D003459:Crystallins; D006885:Hydroxybutyrates; D010421:Pentanoic Acids; C074189:2-hydroxypentanoic acid; D007770:L-Lactate Dehydrogenase; C031570:2-hydroxybutyric acid