Activity of
acetate kinase in cell-free extracts and individual fractions and the kinetic properties of the
enzyme obtained from the Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 intestinal bacterial strains were presented at the first time. The highest activity of the
enzyme was measured in the cell-free extracts (1.52 ± 0.163 and 0.46 ± 0.044 U × mg-1
protein for D. piger Vib-7 and Desulfomicrobium sp. Rod-9, respectively) compared to other fractions. The specific activity of
acetate kinase in the extracts of both bacterial strains was determined at different temperature and pH. Analysis of the kinetic properties of the purified
acetate kinase was carried out. The
acetate kinase activity, initial (instantaneous) reaction rate (V0) and maximum rate of the
acetate kinase reaction (Vmax) in D. piger Vib-7 and Desulfomicrobium sp. Rod-9 intestinal bacterial strains were defined. Michaelis constants (KmAcetyl
phosphate and KmADP) of the
enzyme reaction (2.54 ± 0.26 and 2.39 ± 0.24 mM for D. piger Vib-7 as well as 2.68 ± 0.25 and 2.47 ± 0.27 mM for Desulfomicrobium sp. Rod-9, respectively) were calculated. The described results of
acetate kinase, an important
enzyme in the process of organic compounds oxidation and dissimilatory
sulfate reduction would be perspective and useful for clarification of the etiological role of these bacteria in the development of
inflammatory bowel diseases in humans and animals.