Michaelis-Menten equation Briggs-Haldane derivation

In the Briggs-Haldane derivation of the Michaelis-Menten equation, the concentration of ES is assumed to be at steady state, i.e., its rate of production [Eq. (3.12)] is exactly counterbalanced by its rate of dissociation [Eq. (3.13)]. Since the rate of formation of ES from E -(- P is vanishingly small, it is neglected. Equating the two equations and rearranging yields Eq. (3.14), where KM replaces (k2 + h)/k and is known as the Michaelis-Menten... 

An enzyme is said to obey Michaelis-Menten kinetics, if a plot of the initial reaction rate (in which the substrate concentration is in great excess over the total enzyme concentration) versus substrate concentration(s) produces a hyperbolic curve. There should be no cooperativity apparent in the rate-saturation process, and the initial rate behavior should comply with the Michaelis-Menten equation, v = Emax[A]/(7 a + [A]), where v is the initial velocity, [A] is the initial substrate concentration, Umax is the maximum velocity, and is the dissociation constant for the substrate. A, binding to the free enzyme. The original formulation of the Michaelis-Menten treatment assumed a rapid pre-equilibrium of E and S with the central complex EX. However, the steady-state or Briggs-Haldane derivation yields an equation that is iso-... 

Here we develop the basic logic and the algebraic steps in a modern derivation of the Michaelis-Menten equation, which includes the steady-state assumption introduced by Briggs and Haldane. The derivation starts with the two basic steps of the formation and breakdown of ES (Eqns 6-7 and 6-8). Early in the reaction, the concentration of the product, [P], is negligible, and we make the simplifying assumption that the reverse reaction, P—>S (described by k 2), can be ignored. This assumption is not critical but it simplifies our task. The overall reaction then reduces to... 

For most enzymes, the rate of reaction can be described by the Michaelis-Menten equation which was originally derived in 1913 by Michaelis and MENTEN 21 . Its derivation can be achieved by making one of two assumptions, one of which is a special case of the more general Briggs-Haldane scheme, whilst the alternative is the rapid-equilibrium method given in Appendix 5.3(2 ). 

In this section, we shall begin to see how the Briggs-Haldane steady state approach can be enlarged to derive steady state kinetics equations appropriate to more complex kinetic schemes. In doing this, there will be some pleasant surprises in that the form of these new steady state kinetic equations will follow the form of Michaelis-Menten equation (8.8) with a few adaptations not unlike those seen in the Uni Uni steady state kinetic scheme adapted to fit the presence of inhibitors (see Section 8.2.4). 

Because the busy metabolic traffic of cells produces a steady state more often than an equilibrium, much use has been made of an equation devised by Briggs and Haldane (1925) who showed that it was unnecessary to assume an equilibrium between [E] and [S]. They derived Equation (v), formally similar to the Michaelis—Menten equation but free from this assumption and suitable for steady-state conditions. 

Together with Eq. (11.7), Eq. (11.4) is known as the Michaelis-Menten equation. Later, Briggs and Haldane derived a more generalized equation from the same standpoint ... 

Derive the rate equation by employing (a) the Michaelis-Menten and (b) the Briggs-Haldane approach. Explain when the rate equation derived by the Briggs-Haldane approach can be simplified to that derived by the Michaelis-Menten approach. 

In addition to the preceding assumptions, there are three different approaches to derive the rate equation Michaelis-Menten approach [10], Briggs-Haldane approach [11], and numerical solution. 

It is important to note that the derivation of the rate law in the Briggs-Haldane mechanism gives the same result as in the Michaelis-Menten mechanism, namely the fundamental Michaehs-Menten equation (3.9). However, in the former case, the Michaelis constant Ka is increased by a factor k /k, compared with the latter case Vmax constant has the same meaning in both mechanisms. 

Michaelis and Menten, and later Briggs and Haldane, used the scheme shown in Equation II-4 to derive a mathematical expression that describes the relation between initial velocity and substrate concentration. (Consult a biochemistry textbook for the step-by-step derivation of this relationship, because it is important to be aware of the assump-... 

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