Cellular concentration of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase

Range ~0.1 µM
Organism Unspecified
Reference Bar-Even A. et al., The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry. 2011 May 31 50(21):4402-10. doi: 10.1021/bi2002289. p.4404 left column top paragraphPubMed ID21506553
Primary Source [16] Heinrich, R., Schuster, S., and Holzhutter, H. G. (1991) Mathematical analysis of enzymic reaction systems using optimization principles. Eur. J. Biochem. 201 ,1 – 21.PubMed ID1915354
Method "Here [investigators] describe a global view of enzyme parameters with the aim of highlighting the forces that shape the catalytic efficiency of enzymes."
Comments "The median KM is ~100µM (Figure 1C BNID 111413), where ~60% of all KM values are in the range of 10-1000µM. The distribution of KM values implies an empirical constraint for the KM of metabolic enzymes toward their substrates, where the vast majority of enzymes (>99%) do not exhibit KM values below 0.1µM. Such a low KM characterizes, for example, the glycolysis enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase utilizing the substrate 1,3-bisphosphoglycerate, the cellular concentration of which is ~0.1µM. [primary source]"
Entered by Uri M
ID 111414