Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila
Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila
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DOI：
10.1128/jb.188.3.1155-1158.2006
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发表时间：
2006-02-01
影响因子：
3.2
通讯作者：
Ferry, JG
中科院分区：
文献类型：
--
作者：
Lawrence, SH;Ferry, JG
磷酸转乙酰酶（EC 2.3.1.8）催化乙酰基从乙酰磷酸到辅酶A（CoA）的可逆转移，形成乙酰辅酶A和无机磷酸。对嗜热甲烷八叠球菌磷酸转乙酰酶的稳态动力学分析表明，该酶的动力学机制为三元复合动力学机制而非乒乓动力学机制。此外，产品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。动态光散射结果表明，该酶在溶液中是二聚体。
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.