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首页> 外文期刊>FEBS Letters >The interaction of fructose 2,6‐bisphosphate with an allosteric site of rat liver fructose 1,6‐bisphosphatase
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The interaction of fructose 2,6‐bisphosphate with an allosteric site of rat liver fructose 1,6‐bisphosphatase

机译:果糖2,6-二磷酸与大鼠肝中的变构位点果糖1,6-二磷酸酶的相互作用

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>Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleimide by low concentrations of fructose 2,6-bisphosphate or high concentrations of fructose 1,6-bisphosphate. The partially inactivated enzyme has a much reduced sensitivity to high substrate inhibition and has lost the sigmoid component of the inhibition by fructose 2,6-bisphosphate; this compound is a simple linear competitive inhibitor of the modified enzyme. The results suggest that fructose 2,6-bisphosphate can bind to the enzyme at two distinct sites, the catalytic site and an allosteric site. High levels of fructose 1,6-bisphosphate probably inhibit by binding to the allosteric site.
机译:低浓度的果糖2,6-二磷酸或高浓度的果糖1,6-二磷酸可以保护>鼠肝果糖1,6-二磷酸酶免受 N -乙基马来酰亚胺的部分灭活。部分灭活的酶对高底物抑制的敏感性大大降低,并失去了果糖2,6-双磷酸酯的抑制作用中的乙状结肠成分。该化合物是修饰酶的简单线性竞争抑制剂。结果表明,果糖2,6-二磷酸酯可以在两个不同的位点(催化位点和变构位点)与酶结合。高水平的果糖1,6-二磷酸酯可能通过结合至变构位点而受到抑制。

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