Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis.
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.
Poolman
B
B
Department of Microbiology, University of Groningen, Haren, The Netherlands.
Bosman
B
B
Kiers
J
J
Konings
W N
WN
D004734:Energy Metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D013294:Lactococcus lactis / Q000201:enzymology*; D007785:Lactose / Q000378:metabolism; D008433:Mathematics; D010736:Phosphoglycerate Mutase / Q000378:metabolism; D013291:Streptococcus / Q000201:enzymology*
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010736:Phosphoglycerate Mutase; D007785:Lactose