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.
Highlights
U lcerative colitis is one of the most common acute inflammatory bowel diseases
The active agents of ulcerative colitis and inflammatory bowel diseases can be sulfate-reducing bacteria which occur in the gut flora of about 50% of healthy persons [7]
The dissimilation process occurring in these organisms involves adenosine phosphosulfate (APS) as the active intermediate compound [11, 16]
Summary
U lcerative colitis is one of the most common acute inflammatory bowel diseases. The development of this disease depends on human nutrition and the qualitative and quantitative composition of intestinal microbiocenosis [3, 12]. Hydrogen sulfide accumulated in the human intestine is cytotoxic and carcinogenic to its cells causing inhibition of cytochrome oxidase, oxidation processes of butyrate by colonocytes, and destruction of epithelial cells, ulcers, inflammation with subsequent development of colon cancer [3, 7, 12]. As far as it is aware, ATP sulfurylase from intestinal sulfate-reducing bacteria D. piger and Desulfomicrobium has never been well-characteri zed. The aim of our work was to study specific activity of ATP sulfurylase in cell-free extract of in-
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