The mentioned assumptions and definitions regardingthe Michaelis-Menten modellead to the Michaelis-Menten equation (for a more detailed derivation, see below), wherekm= (k-1+ k2) / k1, and where the "0" in v0implies that this equation is only valid for describing the initial rates, where no significant amount of product has been formed. The 2 constants Vmaxand kmwill be described on the following pages.

V0= Vmax[S]/Km+[S]

Of course, the assumptions regarding the model do not apply to all enzymatic reactions; therefore, it is sometimes necessary to use more complicated models to describe them. However, the Michealis-Menten equation applies to many different enzymatic reactions, often involving several more steps than the 2-step mechanism proposed by Michaelis and Menten. Thus, enzymes that show a hyperbolic relationship between v0and [S] are said to follow Michaelis-Menten kinetics. [1]

References

  1. Lehninger, Albert L.; Nelson, David L.; Cox, Michael M. (2008). Principles of Biochemistry (5th ed.). New York, NY: W.H. Freeman and Company. ISBN 978-0-7167-7108-1.

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