Abstract:
Related Henri-Michaelis–Menten (HMM) and simple single-substrate enzyme kinetics model explored in different directions for more than a century. In the current paper we are concerned with a possible generalization of this rate equation which projected by F. Kargi , that is assumed to be useful both in the case that the total enzyme or substrate is in excess and the quasi-steady-state is produced. We conclude that this generalization is not enough dramatically and put another generalization based on application of the quasi-steady-state conservation equations and condition for both substrate and enzyme. The standard HMM equation is obtain via (a) applying the conservation equation only for the enzyme, (b) assuming the quasi-steady-state …show more content…
v = d[P]/(dt )= Vmax[S]/((KM + [S]))
Equation (a): Henri Michaelis-Menten HMM equation
Firstly; Michaelis–Menten equation (1) describe the enzymatic reactions rate , the concentration present as (S ) substrate , maximum rate ( ) by the system, The Michaelis constant is the substrate concentration .
E+S □(↔┴k ) ES □(→┴kb ) E+P
E.q. (b): enzymatic reactions rate at which the product in the reaction
Secondly; By this mathematical model, the enzyme (E) binding to a (s) substrate to form ES which will convert to product finally , the , , and represent the rate constants, the double arrows show a reversible process of theenzyme-substrate …show more content…
The reaction rate is measured in enzyme kinetics as well as the impacts of alter the conditions of the reaction are investigated. The Studying of kinetics enzyme in that way able to discover the mechanism of catalytic for this enzyme. its role in metabolism, how an agonist or a drug may inhibit the enzyme and how controlled its activity. Enzymes are protein molecules which treatment other molecules — the enzymes' substrates. These aim molecules bind to active site of enzyme as well as are convert into products through a chain of procedures recognize as the enzymatic mechanism. As enzyme-catalysed reactions are saturable, their rate of catalysis does not show a linear response to increasing substrate. If the initial rate of the reaction is measured over a range for the concentrations of substrate, the reaction rate (v) rise as [S] increases. However, as [S] increase, the enzyme becomes saturated with substrate as well as the rate reaches Vmax, the maximum of enzyme
Related Henri-Michaelis–Menten (HMM) and simple single-substrate enzyme kinetics model explored in different directions for more than a century. In the current paper we are concerned with a possible generalization of this rate equation which projected by F. Kargi , that is assumed to be useful both in the case that the total enzyme or substrate is in excess and the quasi-steady-state is produced. We conclude that this generalization is not enough dramatically and put another generalization based on application of the quasi-steady-state conservation equations and condition for both substrate and enzyme. The standard HMM equation is obtain via (a) applying the conservation equation only for the enzyme, (b) assuming the quasi-steady-state …show more content…
v = d[P]/(dt )= Vmax[S]/((KM + [S]))
Equation (a): Henri Michaelis-Menten HMM equation
Firstly; Michaelis–Menten equation (1) describe the enzymatic reactions rate , the concentration present as (S ) substrate , maximum rate ( ) by the system, The Michaelis constant is the substrate concentration .
E+S □(↔┴k ) ES □(→┴kb ) E+P
E.q. (b): enzymatic reactions rate at which the product in the reaction
Secondly; By this mathematical model, the enzyme (E) binding to a (s) substrate to form ES which will convert to product finally , the , , and represent the rate constants, the double arrows show a reversible process of theenzyme-substrate …show more content…
The reaction rate is measured in enzyme kinetics as well as the impacts of alter the conditions of the reaction are investigated. The Studying of kinetics enzyme in that way able to discover the mechanism of catalytic for this enzyme. its role in metabolism, how an agonist or a drug may inhibit the enzyme and how controlled its activity. Enzymes are protein molecules which treatment other molecules — the enzymes' substrates. These aim molecules bind to active site of enzyme as well as are convert into products through a chain of procedures recognize as the enzymatic mechanism. As enzyme-catalysed reactions are saturable, their rate of catalysis does not show a linear response to increasing substrate. If the initial rate of the reaction is measured over a range for the concentrations of substrate, the reaction rate (v) rise as [S] increases. However, as [S] increase, the enzyme becomes saturated with substrate as well as the rate reaches Vmax, the maximum of enzyme