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Cooperativity in enzyme kinetics

Equation (4.31) gives us the equilibrium binding in the case of dual cooperativity, yet it does not tell us what cooperative binding has to do with enzyme kinetics. To illustrate the role of cooperativity in enzyme kinetics, consider the following [Pg.82]


Substrate Inhibition Substrate inhibition represents another example of cooperativity in enzyme kinetic reactions, but of a different profile than described to this point. With substrate inhibition kinetics, the velocity of a reaction increases (as expected for hyperbolic profiles) to an apex, however, beyond this point the velocity of the reaction decreases with increasing substrate concentrations (Fig. 4.7). [Pg.98]


See other pages where Cooperativity in enzyme kinetics is mentioned: [Pg.82]    [Pg.16]   
See also in sourсe #XX -- [ Pg.82 ]




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