Enhanced activity of 3'-pyrophospho coenzyme A

3'-Super(pyro)phospho CoA synthesized by enzymic transfer of 5'-beta, alpha-pyrophosphoryl group from dATP to dephospho CoA at adenosine 3'-OH site catalysed by Streptomyces morookaensis ATP nucleotide pyrophosphokinase (EC 2.7.6.4). CoApp was found to be about twice more active than normal CoA as a cofactor of phospho-transacetylases from C. kluyveri, L. mesenteroides and E. coli. Acetyl CoApp was found to be about six times more active than normal acetyl CoA as an allosteric effector with E. coli phosphoenolpyruvate carboxylase. Significance of these findings was discussed.