Kemp R G, Foe L G
Mol Cell Biochem. 1983;57(2):147-54. doi: 10.1007/BF00849191.
We have reviewed the allosteric regulatory properties of skeletal muscle phosphofructokinase and recent results on the phosphorylation of this enzyme. The number and affinities of various ligand binding sites are described, and a simple three state model is presented to explain the kinetic and ligand-binding properties of the enzyme. Data describing a lack of fit to a concerted transition model are presented. The widespread occurrence of partial phosphorylation of phosphofructokinase at a specific site near the carboxyl terminus is documented, as well as the lack of significant kinetic consequences of such phosphorylation.
我们回顾了骨骼肌磷酸果糖激酶的变构调节特性以及该酶磷酸化的最新研究结果。描述了各种配体结合位点的数量和亲和力，并提出了一个简单的三态模型来解释该酶的动力学和配体结合特性。给出了与协同转变模型不符的数据。记录了磷酸果糖激酶在羧基末端附近特定位点的部分磷酸化的广泛存在，以及这种磷酸化缺乏显著动力学影响的情况。
