Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosph
Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosph
复制标题
环腺苷 3:5-单磷酸对体内细菌糖原合成调节的贡献。
DOI：
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发表时间：
1979
影响因子：
4.8
通讯作者：
W. Sternheim
中科院分区：
文献类型：
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作者：
D. N. Dietzler;M. P. Leckie;J. Magnani;M. J. Sughrue;P. Bergstein;W. Sternheim
当果糖、甘油或琥珀酸作为氮饥饿培养的大肠杆菌W 4597（K）的唯一碳源和能量来源时，表达糖原合成和己糖磷酸之间关系的方程的动力学常数的值与葡萄糖作为唯一碳源和能量来源时观察到的值不同。在指数生长或氮饥饿的培养过程中添加葡萄糖，使用其他碳源之一减缓了糖原合成的速率，并将常数的值向单独使用葡萄糖的培养物中观察到的值转移。在使用葡萄糖的培养物的指数生长期间添加环AMP（环腺苷3 '：5'-单磷酸）导致常数的值向使用除葡萄糖之外的碳源的培养物中观察到的值移动。在本报告研究的所有代谢条件下，腺苷酸能荷（（ATP + 1/2 ADP）/（ATP + ADP + AMP））和糖原合成限速酶ADP-葡萄糖合成酶（葡萄糖1-磷酸腺苷酰转移酶，EC 2.7.7.27）的水平相同。这里提供的数据表明，我们在糖原合成定量关系中观察到的差异是使用葡萄糖的细胞和使用其他碳源之一的细胞中环腺苷酸水平不同的结果。由于环腺苷酸不影响ADP-葡萄糖合成酶在体外的速度，显然在细胞水平的环腺苷酸的变化会导致目前未知的（和以前未检测到的）这种酶的效应细胞水平的转变。这种效应物水平的变化明显改变了酶在体内对底物葡萄糖1-磷酸和激活剂果糖1，6-二磷酸的反应。
When either fructose, glycerol, or succinate served as a sole source of carbon and energy in nitrogen-starved cultures of Escherichia coli W4597(K) the values of the kinetic constants of the equation that expresses the relationship between glycogen synthesis and hexose phosphates were different from the values observed when glucose was the sole source of carbon and energy. Addition of glucose during either exponential growth or nitrogen starvation to a culture using one of the other carbon sources slowed the rate of glycogen synthesis and shifted the values of the constants toward the values observed in cultures using glucose alone. Addition of cyclic AMP (cyclic adenosine 3':5'-monophosphate) during exponential growth of a culture using glucose caused the values of the constants to be shifted toward the values observed in cultures using a carbon source other than glucose. In all of the metabolic conditions studied in this report the adenylate energy charge ((ATP + 1/2 ADP)/(ATP + ADP + AMP)) and the level of the rate-limiting enzyme of glycogen synthesis, ADP-glucose synthetase (glucose 1-phosphate adenylyltransferase, EC 2.7.7.27), were the same. The data presented here indicate that the difference we observed in the quantitative relationship for glycogen synthesis is the result of the different cellular levels of cyclic AMP in the cells using glucose and the cells using one of the other carbon sources. Since cyclic AMP does not affect the velocity of ADP-glucose synthetase in vitro, apparently a change in the cellular level of cyclic AMP causes a shift in the cellular level of a presently unknown (and previously undetected) effector of this enzyme. The shift in the level of this effector evidently alters the response of the enzyme in vivo to the substrate glucose 1-phosphate and the activator fructose 1,6-diphosphate.