Stereospecificity of hydride transfer for the catalytically recycled NAD+ in CDP-D-glucose 4,6-dehydratase

Article abstract of DOI:10.1016/S0040-4020(98)01005-9

CDP-D-glucose 4,6-dehydratase (E(od)), found in the biosynthetic pathway of 3,6-dideoxysugars, contains a tightly bound MAD⁺ that is recycled during catalysis. The stereochemical preference of the hydride transfer to and from the coenzyme in E(od) was determined to be pro-S by analyzing the NAD⁺ produced when the apoenzyme was incubated with stereospecifically labeled NADH and its product, CDP-6-deoxy-D-glycero-L-threo-4-hexulose.