Stereochemistry of Horse Liver Alcohol Dehydrogenase Mediated Oxidoreduction of 2-Brendanone Type Cage-Shaped Tricyclic Ketones and the Related Stereoisomeric Alcohols

Article abstract of DOI:10.1021/jo00171a036

For elucidation of the origin of the inertness exhibited by 2-twist-brendanone type ketones 1 toward microbial and HLADH-catalyzed reductions, the stereochemistry of the oxidoreduction of 2-brendanone type ketones 5 and the related alcohols 14 was studied by preparative-scale incubation experiments.Oxidoreduction of 2-brendanone type substrates 5 and 14 by the HLADH-NAD(+) system was found to proceed with much higher rates than those of the 2-twist-brendanone type substrates 1 and 10.The steric courses found in these enzymatic processes were compared with those of microbial processes.