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

Table 3.: Kinetic parameters of acetate kinase reaction.

Kinetic parameters	Sulfate-reducing bacteria
Kinetic parameters	Desulfovibriopiger Vib-7	Desulfomicrobium sp. Rod-9
VmaxAcetyl phosphate (µmol × min-1 × mg-1 protein)	3.12 ± 0.32	1.03 ± 0.098***
KmAcetyl phosphate (mM)	2.54 ± 0.26	2.68 ± 0.25
VmaxADP (µmol × min-1 × mg-1 protein)	3.05 ± 0.31	0.98 ± 0.095***
KmADP (mM)	2.39 ± 0.24	2.47 ± 0.27

Comment: Vmax is maximum velocity of the enzyme reaction; Km is Michaelis constant which was determined by substrate (acetyl phosphate and ADP). Statistical significance of the values M ± m, n = 5; ***P<0.001, compared to the D. piger Vib-7 strain.