Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.
Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.
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费氏丙酸杆菌焦磷酸依赖性磷酸果糖激酶的动力学机制。
DOI：
10.1021/bi00313a014
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发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Cook,PF
中科院分区：
文献类型：
--
作者：
Bertagnolli,BL;Cook,PF
摘要：采用十二烷基硫酸钠（SDS）凝胶银染色法纯化了弗氏丙酸杆菌无机焦磷酸盐依赖性d -果糖-6-磷酸1-磷酸转移酶。在果糖6-磷酸（F6P）磷酸化的方向上，当MgPPj在F6P的几个水平上变化时，得到了一个相交的初始速度模式。在逆反应方向上，反应物为Mg2+、P′和果糖1,6 -二磷酸（FDP）。P的变化，几个水平的Mg2+和一个水平的FDP给出了一个相交的模式。当这种模式在几个额外的FDP水平上重复时，数据与pH 8.0和25 c下完全随机的交互反应物机制一致。从Haldane关系[(5±1.5)X 10“3 M]计算出的结果与确定的^^磷酸依赖的磷酸果糖激酶(焦磷酸：d -果糖-6-磷酸1-磷酸转移酶，EC 2.7一致。1.90)催化反应
Byron L. Bertagnolli and Paul F. Cook* abstract: Inorganic pyrophosphate dependent D-fructose-6-phosphate 1-phosphotransferase from Propionibacterium freudenreichii was purified to apparent homogeneity by the criterion of silver staining on sodium dodecyl sulfate (SDS) gels. In the direction of phosphorylation of fructose 6-phosphate (F6P), an intersecting initial velocity pattern is obtained when MgPPj is varied at several levels of F6P. In the reverse reaction direction, the reactants are Mg2+, P¡, and fructose1, 6-bisphosphate (FDP). Variation of P¡ at several levels of Mg2+ and a single level of FDP gives an intersecting pattern. When this pattern is repeatedat several additional FDP levels, data are consistent with a fully random terreactant mechanism at pH 8.0 and 25 C. The calculated from the Haldane relationship [(5±1.5) X 10 “3 M] agrees with that determined^^ rophosphate-dependent phosphofructokinase (pyro-phosphate: D-fructose-6-phosphate 1-phosphotransferase, EC 2.7. 1.90) catalyzes the reaction