Perturbation Theory in the Catalytic Rate Constant of the Henri-Michaelis-Menten Enzymatic Reaction (Journal article)
Bakalis, E./ Kosmas, M./ Papamichael, E. M.
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.
|Institution and School/Department of submitter:||Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας|
|Keywords:||enzyme catalyzed reactions,transient phase kinetics,perturbation theory,variational iteration method,biochemical reaction model,steady-state assumption,cysteine proteinases,kinetics,systems,equations|
|Link:||<Go to ISI>://000310316100001|
|Publisher:||Springer Verlag (Germany)|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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