Enzymatic fluxes with more complex kinetics

4 Enzymatic fluxes with more complex kinetics 

Detailed kinetic analyses of mechanisms such as in Equation (4.37) and the determination of flux expression such as Equation (4.38) is a central theme of several 

As we have seen, the catalytic cycle flux provides a useful metric for analyzing enzyme kinetics. In this section, we analyze the turnover time for catalytic cycles and show that the quasi-steady rate law arises from the mean cycle time [151]. In addition, we show that for arbitrary mechanisms for a single-substrate reaction, the steady state rate law can always be expressed using the Michaelis-Menten form 

However, this expression does not provide the mean cycle time. Since a fraction of the transitions ES - E are through the reverse binding step ES — E + S, the mean cycle time is longer than Te es e computed by the above equation. 

The probability that a transition ES — E is through the reaction ES — E + P (rather than through ES - E + S) is given by  

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