Acetate kinase Activity and Kinetic Properties of the Enzyme in Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 Intestinal Bacterial Strains



Ivan V Kushkevych*
Laboratory of Molecular Biology and Clinical Biochemistry, Institute of Animal Biology of NAAS of Ukraine, Vasyl Stus St 38, Lviv 79034, Ukraine


Article Metrics

CrossRef Citations:
0
Total Statistics:

Full-Text HTML Views: 361
Abstract HTML Views: 227
PDF Downloads: 97
Total Views/Downloads: 685
Unique Statistics:

Full-Text HTML Views: 249
Abstract HTML Views: 140
PDF Downloads: 76
Total Views/Downloads: 465



© Ivan V. Kushkevych; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* Address correspondence to this author at Laboratory of Molecular Biology and Clinical Biochemistry, Institute of Animal Biology of NAAS of Ukraine, Vasyl Stus St 38, Lviv 79034, Ukraine; Tel: +380 32 270 25 04; Fax: +380 32 270 23 89; E-mail: ivan.kushkevych@gmail.com


Abstract

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.

Keywords: Acetate kinase, inflammatory bowel diseases, kinetic analysis, sulfate-reducing bacteria.