kcat of reactions associated with:

Range Central-CE (carbohydrate energy) metabolism 79 s^-1: secondary metabolism 2.5s^-1 sec^-1
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 right 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 "As illustrated in Figure 2A, enzyme substrate pairs associated with central metabolic groups tend to have higher turnover numbers than intermediate and secondary ones. The median kcat of reactions associated with central-CE metabolism (79 s^-1) is ~30-fold higher than that of the reactions associated with secondary metabolism (2.5 s^-1). Enzymes associated with central-CE metabolism also exhibit an average kcat/KM value ~6-fold higher than those of intermediate and secondary metabolism (Figure 2B)."
Entered by Uri M
ID 111415