Kinetic properties of adenosine triphosphate sulfurylase of intestinal sulfate-reducing bacteria.

ABSTRACT

The investigation of specific activity of ATP sulfurylase and kinetic properties of the enzyme in cell-free extracts of intestinal bacterial strains Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 is presented. The microbiological, biochemical, biophysical and statistical methods were used in the work. The optimal temperature (35°C) and pH 8.0-8.5 for enzyme reaction were determined. An analysis of kinetic properties of ATP sulfurylase has been carried out. Initial (instantaneous) reaction velocity (V0), maximum amount of the product of reaction (Pmax), the reaction time (half saturation period, τ) and maximum velocity of the ATP sulfurylase reaction (Vmax) have been defined. Michaelis constants (Km(Sulfate), Km(ATP), Km(APS), and Km(Pyrophosphate)) of the enzyme reaction were demonstrated for both D. piger Vib-7 and Desulfomicrobium sp. Rod-9 intestinal bacterial strains.