| 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 |