Kinetic and stereoelectronic effects of a fluorine substituent on the reaction catalysed by an NADPH-dependent cyclohex-1-enylcarbonyl CoA reductase

Abstract

The introduction of a fluorine atom at C-3 of cyclohex-1-enecarbonyl CoA has a dramatic effect on the processing of the fluorinated over the natural analogue by NADPH dependant cyclohex-1-enecarbonyl CoA reductase from Streptomyces collinus; the fluorinated analogue is processed with a five fold increase in V_max and kinetic isotope studies suggest that hydride delivery is only partially rate limiting in the latter case; the enzyme also shows a small kinetic preference for axial over equatorial fluorine at C-3 of 3-fluorocyclohex-1-encarbonyl CoA 4.