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首页> 外文期刊>Journal of bacteriology >Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis.
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Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis.

机译：甘油醛-3-磷酸脱氢酶在链球菌和链球菌乳酸中的控制对糖酵解。

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摘要

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.
机译：乳糖 - 饥饿的链球菌的能量代谢对乳糖Readition的响应降低是由糖酵解活性的降低引起的（B.博勒姆曼，ej smid和Wn Konings，J.bacteriol。169：1460-1468,1987） 。糖酵解的减少伴随着甘油醛-3-磷酸脱氢酶和磷酸性甘露出酶的活性的降低。在各种饥饿后在乳糖中改变乳糖后稳态水平表明，降低的糖醇分解主要是由于糖绿醛-3-磷酸脱氢酶活性减少。此外，通过甘氨醛-3-磷酸脱氢酶施加对糖酵母途径的总体活性的控制强度的定量表明，该酶可以是显着的速率限制在非创业细胞中。

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