Production of D-pantothenate with Microbial Enzymes

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New NADPH-dependent carbonyl reductases which catalyzes stereospecific reductions of carbonyl compounds have been purified from various microorganisms and characterixed. The enzyme "polyketone reductase" from Candida parapsilosis specifically catalyzes reduction of various prochiral diketones, yielding the corresponding (R) - hydroxyketones. Aldehyde reductase from Sporobolomyces salmonicolor and carbonyl reductase from Candida macedoniensis catalyze stereospecific reduction of various aliphatic and aromatic ketones and aldehydes. Ketopantoic acid reductase from Pseudomonas maltophilia and an FMN-dependent alcohol dehydrogenase from Nocardia asteroides, catalyze reduction of ketopantoic acid to D-pantoic acid and oxidation of L-pantoyl lactone to ketopantoyl lactone, respectively. These enzymes were successfully applied to the synthesis of chiral intermediates for the syntesis of D-pantothenate.