Chiral switch of enzymatic ketone reduction by addition of gamma-cyclodextrin.
We report a chiral switch in the configuration of 1-(p-methoxyphenyl)-propan-2-ol, synthesized in aqueous media by ketoreductase in the presence of high concentration of gamma-CD. NMR, ECD and fluorescence spectrometry were used in the effort to explain this unexpected effect. A comparison has been made between the catalytic activity of the enzyme and alpha-helix content in the conformation and it has been observed that enzyme is most active at the maximum alpha-helix content. The beta-sheet content and random coil conformation in the enzyme were found to be dependent on cyclodextrin concentration.
Petkova
Galina A
GA
Department of Analytical Chemistry, Institute of Chemical Technology Prague, Technicka 5, 166 28 Prague 6-Dejvice, Czech Republic.
Král
Vladimír
V
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D002942:Circular Dichroism; D007659:Ketones / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism; D046950:Thermoanaerobacterium / Q000201:enzymology; D047408:gamma-Cyclodextrins / Q000737:chemistry*
D007659:Ketones; D047408:gamma-Cyclodextrins; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C023792:gamma-cyclodextrin