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
URI: http://olympias.lib.uoi.gr/jspui/handle/123456789/8790
ISSN: 0092-8240
Link: <Go to ISI>://000310316100001
http://download.springer.com/static/pdf/92/art%253A10.1007%252Fs11538-012-9761-x.pdf?auth66=1386153529_17ff30b1735786832e784a448673321c&ext=.pdf
Publisher: Springer Verlag (Germany)
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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