Identification of Candida tenuis xylose reductase as highly selective biocatalyst for the synthesis of aromatic alpha-hydroxy esters and improvement of its efficiency by protein engineering.
Wild-type Candida tenuis xylose reductase and two Trp-23 mutants thereof catalyze NADH-dependent reduction of a homologous series of aromatic alpha-keto esters with absolute pseudo re-face stereoselectivity and broad tolerance for the substituent on the aromatic ring, producing the corresponding R-alcohols in high yield.
Kratzer
Regina
R
Research Centre Applied Biocatalysis, Petersgasse 14, A-8010 Graz, Austria c/o Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, A-8010 Graz, Austria.
Nidetzky
Bernd
B
D000449:Aldehyde Reductase / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D018360:Crystallography, X-Ray; D004952:Esters / Q000138:chemical synthesis* / Q000737:chemistry; D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009243:NAD / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D015202:Protein Engineering; D013379:Substrate Specificity; D014994:Xylose / Q000737:chemistry / Q000378:metabolism*
D004952:Esters; D009243:NAD; D014994:Xylose; D000449:Aldehyde Reductase