Table 2.

Molecular and kinetic properties of purified AK from eubacteria and M. thermophila

OrganismMolecular massa(kDa)Apparent Kmb(mM)Reference(s)
Native enzymeSubunitAcetateATPAc-PADP
Thermotoga maritima 90 (α2)44400.70.443This work
Methanosarcina thermophila 94 (α2)53222.8 1
Clostridium thermoaceticum 60 (α)1351.64c 32
Bacillus stearothermophilus 160 (α4)431201.22.30.8 24
Escherichia coli 70 (α2)4070.070.160.5 13
Salmonella typhimurium 70 (α2)4070.070.160.5 13
Rhodopseudomonas palustris 47 (α2)45401.10.00260.087 41
Veillonella alcalescens 88 (α2)4217010c 5c 1.3c 4,25
Clostridium acetobutylicum 78 (α2)421602.5<16 10
Acholeplasma laidlawii 120–130 (α2)5138.5d 0.3d 0.1d 0.24d 16
  • a Molecular masses of native enzymes were determined by gel filtration, and those of subunits were determined by SDS-PAGE. The proposed subunit composition of the native enzyme is given in parentheses.

  • b Ac, acetyl; P, phosphate; —, not determined.

  • c Values to give half-maximal rates in sigmoidal reaction kinetics.

  • d Values determined at low ionic strength.