Michaelis theory, extended

Chance (78) has discussed this experimental data in terms of the extended Michaelis theory which accounts for the similar peroxidatic action of peroxidase, the only difference being that with peroxidase the main reaction can proceed via the secondary complexes, whereas with catalase these complexes are inactive and the main reaction proceeds via the primary complexes. Representing the primary complexes by FeOOH and FeOOR he suggests the various reactions are ... 

Catalase and peroxidase do not follow the simple Michaelis theory and the theory is extended (7) to take into account the reaction of the enzyme-substrate complex and a hydrogen or electron donor (AH ) ... 

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 ... 

In 1913, Michaelis and Men ten presented a general theory for enzyme kinetics, extended later by Briggs and Haldane, which accounts for the velocity curve shown in Figure 5.5. This theory for reactions catalyzed by enzymes having a single substrate assumes that the substrate S binds to the active site of the enzyme E to form the enzyme-substrate complex ES, which yields the product P and the free enzyme E ... 

In order to explain this phenomenon in enzymatic catalysis, Michaelis and Menten and subsequent investigators. n. 12 have extended the theory postulated the reversible formation of a complex, ES, between the enzyme, E, and the substrate, S, prerequisite to the breakdown to the... 

---