[Detection of C-P-lyase activity in a cell-free extract of Escherichia coli].

A system has been developed for in vitro testing of E. coli C-P-lyase (the enzyme cleaving C-P bonds in phosphonates). NADH, ATP, and the system of ATP regeneration were necessary but not sufficient for expression of the C-P-lyase activity in cell-free extracts of E. coli. Experimental evidence suggests that glucose 6-phosphate and (or) glucose activate C-P-lyase, serving as precursors in the formation of (alkylphosphono)ribose, an intermediate in the reaction. Guanine is the most likely acceptor of the phosphate group.