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Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis.

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  • 1Institut für Enzymtechnologie, Heinrich-Heine Universität Düsseldorf, im Forschungszentrum Jülich.


Pyruvate decarboxylases (E.C. from various organisms have been studied for many years, mainly with respect to the mechanism of the non-oxidative decarboxylation reaction. Although the C-C-bond-forming properties of these enzymes are known and have been applied for many years in biotransformations for the synthesis of chiral alpha-hydroxy ketones, only little is known about the factors influencing the carboligase side-reaction. The present review surveys recent efforts in the study of site-directed mutagenesis on PDCs, which are discussed against a background of the structural and kinetical investigations. It also includes recent studies on tailoring the PDCs of Zymomonas mobilis for the syntheses of (R)-phenylacetyl carbinol (PAC), a pre-step in the synthesis of L-ephedrine, by protein design techniques.

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