Write down about substrate concentration?
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Substrate Concentration
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Increasing substrate concentration increases the frequency with which the enzyme and substrate collide. As a result enzyme-substrate complexes form more quickly and the rate of reaction increases.
However, there is a limit as eventually there all the enzyme active sites are already occupied with substrate - the enzyme active sites become saturated. Any further increase in substrate concentration has no further effect on the reaction rate.
Substrate Concentration
It has been shown experimentally that if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will increase until it reaches a maximum. After this point, increases in substrate concentration will not increase the velocity (delta A/delta T). This is represented graphically in Figure 8.
It is theorized that when this maximum velocity had been reached, all of the available enzyme has been converted to ES, the enzyme substrate complex. This point on the graph is designated Vmax. Using this maximum velocity and equation (7), Michaelis developed a set of mathematical expressions to calculate enzyme activity in terms of reaction speed from measurable laboratory data.
The Michaelis constant Km is defined as the substrate concentration at 1/2 the maximum velocity. This is shown in Figure 8. Using this constant and the fact that Km can also be defined as:
Km=K-1 + K2 / K+1
K+1, K-1 and K+2 being the rate constants from equation (7). Michaelis developed the following
Michaelis constants have been determined for many of the commonly used enzymes. The size of Km tells us several things about a particular enzyme.
A small Km indicates that the enzyme requires only a small amount of substrate to become saturated. Hence, the maximum velocity is reached at relatively low substrate concentrations.
A large Km indicates the need for high substrate concentrations to achieve maximum reaction velocity.
The substrate with the lowest Km upon which the enzyme acts as a catalyst is frequently assumed to be enzyme's natural substrate, though this is not true for all enzymes.
Enzyme Concentration
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Increasing the amount of enzyme also increases the frequency of with which the enzyme and substrate collide. As a result enzyme-substrate complexes form more quickly and the rate of reaction increases. However, there is a limit as eventually there will be more enzyme molecules that substrate. Some enzymes become redundant as they won't have any substrate to bind. Any further increase in enzyme concentration has no further effect on the reaction rate.
Note that if there is excess substrate (the first part of the graph) the line can be approximated to a straight line.
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Substrate Concentration. Increasing substrate concentration increases the frequency with which the enzyme and substrate collide. As a result enzyme-substrate complexes form more quickly and the rate of reaction increases.
Substrate concentration: Increasing substrate concentration also increases the rate of reaction to a certain point. Once all of the enzymes have bound, any substrate increase will have no effect on the rate of reaction, as the available enzymes will be saturated and working at their maximum rate.
A simple chemical reaction with a single substrate shows a linear relationship between the rate of formation of product and the concentration of substrate, as shown below: ... (A) At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration.
Increasing Substrate Concentration increases the rate of reaction. This is because more substrate molecules will be colliding with enzyme molecules, so more product will be formed.
The amount of enzyme present in a reaction is measured by the activity it catalyzes. ... The relationship between activity and concentration is affected by many factors such as temperature, pH, etc.
If all of the enzymes in the system bind to the substrate, the additional substrate molecules must wait for the enzyme to become available after the reaction is complete. This means that as the enzyme concentration decreases, the reaction rate will decrease.
Enzymes will work best if there is plenty of substrate. As the concentration of the substrate increases, so does the rate of enzyme activity. However, the rate of enzyme activity does not increase forever.
where Km = (k−1 + k2)/k1 is named the Michaelis constant (after the author of the equation); vmax = k2[E]0. The Michaelis constant numerically equals the substrate concentration at which v = vmax/2.
formula - v=\frac{V_\text{max }[{S}]}{K_{{M}}+[{S}]}
v = velocity of reaction
V_\text{max } = maximum rate achieved by the system
[{S}] = concentration of a substrate
K_{{M}} = Michaelis constant