Median KM for the entire data set of enzymes and natural substrates
Range | ~100 µM |
---|---|
Organism | Generic |
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.4403 right column bottom paragraphPubMed ID21506553 |
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), 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. [ref 16]" |
Entered by | Uri M |
ID | 111413 |