title: Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis.
abstract: Pyruvate decarboxylases (E.C. 4.1.1.1) 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.
authors.affiliation: Institut für Enzymtechnologie, Heinrich-Heine Universität Düsseldorf, im Forschungszentrum Jülich.
authors.forename: M
authors.initials: M
authors.lastname: Pohl
mesh_terms: D000595:Amino Acid Sequence; D001711:Biotransformation; D017076:Computer-Aided Design; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011767:Pyruvate Decarboxylase / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment
chemical_list: D007527:Isoenzymes; D011767:Pyruvate Decarboxylase