The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S].
- Assuming the steady state condition
and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and .
(Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)
An enzyme catalyses the reaction S P. The rate of the reaction depends on the concentration of substrate. Since substrate concentration changes through the reaction, we estimate the rate of the reaction at the very beginning of the reaction where changes in [S] is less. Then the initial rate of the reaction vo can be represented as a function of [S].
Michaelis Menten postulated that free enzyme reacts with the substrate reversibly to form an enzyme-substrate complex and this reaction occurs quickly. The ES complex then breakdown into free enzymes and products and this reaction is comparatively slower.
When the enzyme is first mixed with an excess of substrate, [ES] is very less. This period is called the pre-steady state and lasts for microseconds. Soon, the reaction achieves a steady state where [ES] remains constant over time. The measured vo reflects the steady state.
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