Poolman B, Bosman B, Kiers J, Konings W N
Department of Microbiology, University of Groningen, Haren, The Netherlands.
J Bacteriol. 1987 Dec;169(12):5887-90. doi: 10.1128/jb.169.12.5887-5890.1987.
The decreased response of the energy metabolism of lactose-starved Streptococcus cremoris upon readdition of lactose is caused by a decrease of the glycolytic activity (B. Poolman, E. J. Smid, and W. N. Konings, J. Bacteriol. 169:1460-1468, 1987). The decrease in glycolysis is accompanied by a decrease in the activities of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate mutase. The steady-state levels of pathway intermediates upon refeeding with lactose after various periods of starvation indicate that the decreased glycolysis is primarily due to diminished glyceraldehyde-3-phosphate dehydrogenase activity. Furthermore, quantification of the control strength exerted by glyceraldehyde-3-phosphate dehydrogenase on the overall activity of the glycolytic pathway shows that this enzyme can be significantly rate limiting in nongrowing cells.
在重新添加乳糖后,乳糖饥饿的嗜热链球菌能量代谢反应降低是由糖酵解活性下降所致(B. 普尔曼、E. J. 斯米德和W. N. 康宁斯,《细菌学杂志》169:1460 - 1468,1987年)。糖酵解的降低伴随着3 - 磷酸甘油醛脱氢酶和磷酸甘油酸变位酶活性的下降。在不同饥饿时间段后重新用乳糖喂养时,途径中间产物的稳态水平表明,糖酵解降低主要是由于3 - 磷酸甘油醛脱氢酶活性降低。此外,对3 - 磷酸甘油醛脱氢酶对糖酵解途径整体活性施加的控制强度进行量化显示,在非生长细胞中该酶可能是显著的限速因素。