镁离子在布氏锥虫磷酸果糖激酶催化的反应中的作用。
The roles of magnesium ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei.
作者信息
Cronin C N, Tipton K F
机构信息
Department of Biochemistry, Trinity College, Dublin, Ireland.
出版信息
Biochem J. 1987 Oct 1;247(1):41-6. doi: 10.1042/bj2470041.
Abstract
The involvement of Mg2+ ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei was studied. The true substrate for the enzyme was shown to be the MgATP2-complex, and free Mg2+ ions are also required for enzyme activity. At concentrations of MgATP2- of 2.92 mM and greater, and a fructose 6-phosphate concentration of 1 mM and in the presence of EDTA as a Mg2+ buffer, the Km value for Mg2+ was determined to be 294 +/- 18 microM. Neither MgATP nor free ATP is an inhibitor of the enzyme, although apparent inhibition by the latter can be observed as a consequence of the decrease in free Mg2+ by chelation.
摘要
研究了Mg2+离子在布氏锥虫磷酸果糖激酶催化反应中的作用。结果表明，该酶的真正底物是MgATP2-复合物，并且酶活性也需要游离的Mg2+离子。在MgATP2-浓度为2.92 mM及以上、果糖6-磷酸浓度为1 mM且存在EDTA作为Mg2+缓冲剂的情况下，测定Mg2+的Km值为294±18 μM。MgATP和游离ATP都不是该酶的抑制剂，尽管由于螯合导致游离Mg2+减少，可观察到后者有明显的抑制作用。
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