Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.

Abstract

Formyltetrahydrofolate synthetase from Clostridium cylindrosporum catalyzes phosphoryl transfer from carbamyl phosphate in ADP to form ATP. The phosphoryl transfer reaction has an obligatory requirement for tetrahydrofolate presumably as a cofactor for a proper conformation of the active site. Carbamyl phosphate is an analog of formyl phosphate-a potential intermediate in the normal enzymic reaction. The ability of the enzyme to promote synthesis of ATP from carbamyl phosphate and ADP supports a stepwise chemical reaction mechanism for the enzyme in which formyl phosphate participates as a tightly bound intermediate.