D-mandelate dehydrogenase

Enzyme-catalyzed syntheses of enantiomeric pure hydroxy acids use lactate dehydrogenases (LDH E.C. 1.1.1.27) or hydroxyisocaproate dehydrogenases (HicDH). Both kinds of enzymes are available as D- or L-specific catalysts. L-specific [5, 6] LDHs as well as D-specific [7-10] LDHs favorably catalyze the reduction of pyruvate, HicDHs (and mandelate dehydrogenase, too) convert keto acids with longer aliphatic or aromatic side chains. These enzymes can be isolated from Lactobacillus strains [11-14]. 

Tsou, A.Y., S.C. Ransom, J.A. Gerlt, D.D. Buechter, P.C. Babbitt, and G.L. Kenyon. 1990. Mandelate pathway of Pseudomonas putida sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry 29 9856-9862. 

Scheme 8.16 Formal Mitsunobu reaction by combining an alcohol dehydrogenase (here mandelate dehydrogenase, D-MDH) with an amino acid dehydrogenase (here l-AADH).

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