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. Author manuscript; available in PMC: 2017 Jun 1.
Published in final edited form as: J Phys Chem B. 2016 Apr 29;120(26):6021–6037. doi: 10.1021/acs.jpcb.6b01911

Figure 1.

Figure 1

Dynamics of the Michaelis–Menten enzyme. (A) Probabilities of the free enzyme pE and bound enzyme pES states as a function of substrate concentration. As the amount of substrate [S] increases, more enzyme is found in the bound state rather than the free state. (B) The rate of product formation for a nonallosteric enzyme. The rate of product formation has the same functional form as the probability pES of the enzyme– substrate complex, as illustrated by eqs 2 and 7.