嗜热甲烷八叠球菌磷酸转乙酰酶的稳态动力学分析
Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila.
作者信息
Lawrence Sarah H, Ferry James G
机构信息
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500, USA.
出版信息
J Bacteriol. 2006 Feb;188(3):1155-8. doi: 10.1128/JB.188.3.1155-1158.2006.
Abstract
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.
摘要
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。
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本文引用的文献
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Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila.结构和功能研究表明了嗜热甲烷八叠球菌磷酸转乙酰酶的催化机制。
J Bacteriol. 2006 Feb;188(3):1143-54. doi: 10.1128/JB.188.3.1143-1154.2006.
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Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila.
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Role of arginines in coenzyme A binding and catalysis by the phosphotransacetylase from Methanosarcina thermophila.精氨酸在嗜热甲烷八叠球菌磷酸转乙酰酶辅酶A结合及催化中的作用。
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