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. 1999 Mar;181(6):1861–1867. doi: 10.1128/jb.181.6.1861-1867.1999

TABLE 1.

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

Organism Molecular massa (kDa)
Apparent Kmb (mM)
Reference(s)
Native enzyme Subunit Ac-CoA Ac-P Pi CoA
Thermotoga maritima 170 (α4) 34 0.023 0.024 0.11 0.03 This work
Methanosarcina thermophila 52 (α) 43 0.17 0.09 21
Clostridium thermoaceticum 88 (α4) 20 11
Clostridium acidiurici 63–75 31
Clostridium kluyveri 38–41 0.79–1.2 0.78 17 0.12 3, 18
Bacillus subtilis 90 0.06 0.48 10 0.096 28
Escherichia coli 160–250 (α2) 81 3 0.32 37, 46
Lactobacillus fermenti 68 0.087 26
Rhodopseudomonas palustris 55 (α) 52.5 4.7 0.15 42
Veillonella alcalescens 75–85 (α2) 32–40 195 45
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; Pi, inorganic phosphate; —, not determined.