通过蛋白质磷酸化对糖酵解和糖异生的调控。

The control of glycolysis and gluconeogenesis by protein phosphorylation.

作者信息

Hers H G

出版信息

Philos Trans R Soc Lond B Biol Sci. 1983 Jul 5;302(1108):27-32. doi: 10.1098/rstb.1983.0035.

DOI:10.1098/rstb.1983.0035

Abstract

Fructose 2,6-bisphosphate has been discovered as a potent stimulator of liver phosphofructokinase. It is also an inhibitor of fructose 1,6-biphosphatase and a stimulator of PPi: fructose 6-phosphate phosphotransferase from higher plants. It is formed from fructose 6-phosphate and ATP by a 6-phosphofructo 2-kinase and hydrolysed by a fructose 2,6-bisphosphatase. These two enzymes have very similar physicochemical properties and could not be separated from each other. They are substrates for cyclic-AMP-dependent protein kinase, which inactivates the first enzyme and activates the second.

摘要

2,6-二磷酸果糖已被发现是肝脏磷酸果糖激酶的一种强效刺激剂。它也是1,6-二磷酸果糖酶的抑制剂，以及高等植物中焦磷酸：6-磷酸果糖磷酸转移酶的刺激剂。它由6-磷酸果糖激酶催化6-磷酸果糖和ATP生成，并由2,6-二磷酸果糖酶水解。这两种酶具有非常相似的物理化学性质，无法彼此分离。它们是环磷酸腺苷依赖性蛋白激酶的底物，该激酶会使第一种酶失活并激活第二种酶。