Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila

被引：18
|
作者：
Lawrence, SH [1 ]
Ferry, JG [1 ]
机构：
[1] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
来源：
JOURNAL OF BACTERIOLOGY | 2006年 / 188卷 / 03期
关键词：
D O I：
10.1128/JB.188.3.1155-1158.2006
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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.
引用
收藏
页码：1155 / 1158
页数：4
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