Enzyme kinetics Briggs-Haldane equation

BRIGGS-HALDANE EQUATION STEADY-STATE ASSUMPTION ENZYME KINETICS UNI-UNI MECHANISM Bromohydroxyacetone phosphate,... 

The general theory of enzyme kinetics is based on the work of L. Michaelis and M. L. Menten, later extended by G. E. Briggs and J. B. S. Haldane.la The basic reactions (E = enzyme, S = substrate, P = product) are shown in equation 2.1 ... 

STEADY-STATE TREATMENT. During the steady state, the concentrations of various enzyme intermediates are essentially unchanged that is, the rate of formation of a given intermediate is equal to its rate of disappearance. This assumption was first introduced to the derivation of enzyme kinetic equations by Briggs and Haldane ... 

A mathematical equation indicating how the equilibrium constant of an enzyme-catalyzed reaction (or half-reaction in the case of so-called ping pong reaction mechanisms) is related to the various kinetic parameters for the reaction mechanism. In the Briggs-Haldane steady-state treatment of a Uni Uni reaction mechanism, the Haldane relation can be written as follows ... 

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-... 

The flux expression in Equation (4.16) displays the canonical Michaelis-Menten hyperbolic dependence on substrate concentration [S], We have shown that this dependence can be obtained from either rapid pre-equilibration or the assumption that [S] [E]. The rapid pre-equilibrium approximation was the basis of Michaelis and Menten s original 1913 work on the subject [140], In 1925 Briggs and Haldane [24] introduced the quasi-steady approximation, which follows from [S] 2> [E], (In his text on enzyme kinetics [35], Cornish-Bowden provides a brief historical account of the development of this famous equation, including outlines of the contributions of Henri [80, 81], Van Slyke and Cullen [203], and others, as well as those of Michaelis and Menten, and Briggs and Haldane.)... 

A model for enzyme kinetics that has found wide applicability was proposed by Michaelis and Menten in 1913 and later modified by Briggs and Haldane. The Michaelis-Menten equation relates the initial rate of an enzyme-catalyzed reaction to the substrate concentration and to a ratio of rate constants. This equation is a rate equation,... 

The kinetics of the general enzyme-catalyzed reaction (equation 10.1-1) may be simple or complex, depending upon the enzyme and substrate concentrations, the presence/absence of inhibitors and/or cofactors, and upon temperature, shear, ionic strength, and pH. The simplest form of the rate law for enzyme reactions was proposed by Henri (1902), and a mechanism was proposed by Michaelis and Menten (1913), which was later extended by Briggs and Haldane (1925). The mechanism is usually referred to as the Michaelis-Menten mechanism or model. It is a two-step mechanism, the first step being a rapid, reversible formation of an enzyme-substrate complex, ES, followed by a slow, rate-determining decomposition step to form the product and reproduce the enzyme ... 

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