Abstract
Based on the findings during the course of studies on biosynthetic pathway and chemical synthesis of CoA, the author has been interested in elucidating the structural requirement of CoA for the coenzyme activity. Although the central role of the thiol group in an acyl-transfer system was already established, the function of the pantetheine and the nucleotide moieties of CoA has remained uncertain. The author focussed on the kinetic analysis of the effects of various CoA analogs on a CoA-dependent enzyme phosphotransacetylase. It was concluded that the nucleotide moiety of CoA is important for recognition of this coenzyme by phosphotransacetylase, while the pantetheine moiety may chiefly contribute to the binding strength of CoA with the enzyme.
