[Possible participation of pyrophosphate in ADP and ATP biosyntheses from exogenous adenine by a culture of Corynebacterium species VSTI-301]. / O vozmozhnosti uchastiia prirofosfata v biocinteze ADP i ATP iz ekzogennogo adenina kul'turoi Corynebacterium species BCTI-301.

The autolyzing culture of Corynebacterium species VSTI-301 producing the synthesis of ATP from exogenous adenine was found to contain enzyme systems, which phosphorylate AMP into ADP and ADP into ATP in the presence of pyrophosphate. The optimal conditions for manifestation of activities of both systems in a cell-free extract were determined. One of the enzymes, i. e. pyrophosphate : ADP phosphotransferase, was isolated and purified 76-fold.

[Possible role of high molecular weight polyphosphates in ATP synthesis from exogenous adenine by the culture of Corynebacterium sp., strain VSTI-301]. / Izuchenie vozmozhnoi roli vysokomolekuliarnykh polifosfatov v sinteze ATP iz ekzogennogo adenina kul'turoi Corynebacterium Species, shtamm 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.