Lawrence Sarah H, Ferry James G
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500, USA.
J Bacteriol. 2006 Feb;188(3):1155-8. doi: 10.1128/JB.188.3.1155-1158.2006.
Phosphotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. A steady-state kinetic analysis of the phosphotransacetylase from Methanosarcina thermophila indicated that there is a ternary complex kinetic mechanism rather than a ping-pong kinetic mechanism. Additionally, inhibition patterns of products and a nonreactive substrate analog suggested that the substrates bind to the enzyme in a random order. Dynamic light scattering revealed that the enzyme is dimeric in solution.
磷酸转乙酰酶（EC 2.3.1.8）催化乙酰基从乙酰磷酸可逆地转移至辅酶A（CoA），形成乙酰辅酶A和无机磷酸。对嗜热甲烷八叠球菌的磷酸转乙酰酶进行的稳态动力学分析表明，存在三元复合物动力学机制而非乒乓动力学机制。此外，产物和非反应性底物类似物的抑制模式表明，底物以随机顺序与酶结合。动态光散射显示该酶在溶液中为二聚体。
