EVIDENCE A FOR PROTOPHOSPHATASE CATALYSED CLEAVAGE OF ADENOSINE TRIPHOSPHATE BY A DISSOCIATIVE-TYPE MECHANISM WITHIN A RECEPTOR-SUBSTRATE COMPLEX

Article abstract of DOI:10.1016/S0040-4039(00)96208-7

Analogues of ATP and diadenosine 5',5''-P1,P4-tetraphosphate, Ap4A, have been used to explore the specificity and mechanism of the proto-ATPase activity of the macrocyclic polyamine <24>-N6O2 (1).The results show that (1) has exonuclease-like activity and support a mechanism that is dissociative in character within a pre-associative scheme resulting from receptor-substrate binding.