Can someone explain michaelis menton kinetics simply?
Michaelis Menten kinetics explains the kinetics of a reaction, considering the initial stage of an enzyme catalyzed reaction. The initial stage is considered as its particulars are more easily definable. Km is the Michaelis constant and Kcat is the enzyme turnover number. KM is an indicator of the affinity that an enzyme has for a given substrate, and hence the stability of the enzyme-substrate complex. The stability of the enzyme complex determines its turnover number, which is nothing but the maximum number of moles of substrate that an enzyme can convert to product per catalytic site per unit time. I hope I have been simple enough. Well… If u want to known more click on to the following link: http://www.le.ac.uk/by/teach/biochemweb/… It has been explained in a very simple manner.
