[Possible role of high molecular weight polyphosphates in ATP synthesis from exogenous adenine by the culture of Corynebacterium sp., strain VSTI-301].

An addition of exogenous adenine to an autolysing 72-hour culture of Corynebacterium sp., strain BSTI-301 results in accumulation of as much as 0,6--1,0 mp of ATP per 1 ml of medium. Extracellular ATP accumulation under such conditions is coupled with a considerable decrease of the intracellular content of 5'-phosphoribosyl-1-pyrophosphate, orthophosphate, pyrophosphate and two fractions of high-polymeric polyphosphates PPh3 and PPh4, as compared to the control. The activity of pyrophosphate phosphohydrolase (EC 3.6.1.1) and polyphosphate phosphohydrolase (EC 3.6.1.11) is thereby considerably decreased in the cells growing on exogenous adenine, while the activity of ADP-phosphotransferase (EC 2.7.4.1) is increased 2-fold. It was found that in experiments with 14C-adenine the intracellular content of both ATP and ADP remains unchanged despite a considerable accumulation of extracellular ATP in Corynebacterium sp., strain BSTI-301 cells.