Abstract
The Henry–Michaelis–Menten (HMM) mechanism of enzymatic reaction is studied by means of perturbation theory in the reaction rate constant k 2 of product formation. We present analytical solutions that provide the concentrations of the enzyme (E), the substrate (S), as well as those of the enzyme-substrate complex (C), and the product (P) as functions of time. For k 2 small compared to k −1, we properly describe the entire enzymatic activity from the beginning of the reaction up to longer times without imposing extra conditions on the initial concentrations E o and S o , which can be comparable or much different.
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We thank the unknown referees for their useful and constructive criticism.
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Bakalis, E., Kosmas, M. & Papamichael, E.M. Perturbation Theory in the Catalytic Rate Constant of the Henri–Michaelis–Menten Enzymatic Reaction. Bull Math Biol 74, 2535–2546 (2012). https://doi.org/10.1007/s11538-012-9761-x
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DOI: https://doi.org/10.1007/s11538-012-9761-x