Table 3.
Kinetic parameters of acetate kinase reaction.
| Kinetic parameters | Sulfate-reducing bacteria | |
|---|---|---|
| Desulfovibrio piger 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.