Enzymatic synthesis of L-carnitine and related alcohols

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An NADPH-dependent aldehyde reductase of Sporobolomyces salmonicolor was purified and characterized. The enzyme was found to be useful for the asmmetric reduction of various prochiral carbonyl compounds. When a 4-halo-acetoacetic acid ester was substrate, the corresponding R-(-)-alcohol, R-(-)-4-halo-3-hydroxybutanoic acid was efficiently synthesized.Under the conditions of organic solvent-water two phase system containing the aldehyde reductase, glucose dehydrogenase as a NADPH regenerator, glucose and 4-chloro-3-oxo-butanoic acid ethyl ester, about 100 g/l of R-(-)-4-chloro-3 -hydrobutanoic acid was produced (90%ee, mol yeild ca 100%).The primary amino acid sequence of the aldehyde reductase was determined.