The first factor is Enzyme concentration or subtrate concentration.The rate of enzyme action is directly proportional to to the availability of enzyme provided the substrate concentration unlimited.Or the rate is directly proportional to the substrate concentration if enzymes are limited but if enzyme concentration is kept constant then upto the certain level the increase in substrate amount will no longer increase the rate of enzyme action.
Second factor is temperature.The rate if an enzyme action is always directly proportional to the increase in temperature but upto the specific limit called as optimum temperature.
Third factor is the pH value.Enzymes can work efficiently over a narrow range of pH called as Optimum pH.A minor change in pH value can denature the enzyme.
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
The rate-limiting step of an enzyme-catalyzed reaction is the slowest step in the reaction that determines the overall rate at which the reaction proceeds.
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
The rate of the enzyme-controlled reaction will increase until all enzyme active sites are saturated with substrate. After that point, the rate will remain constant as all enzyme molecules are already actively engaged, leading to saturation kinetics.
- with enzymes the rate of reaction is higher- an important characteristic of an enzyme is the specifity
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* Presence of enzyme * Change in pH * Change in temperature * Change in salt concentration.
Enzyme concentration has no effect on the rate of an enzyme-catalyzed reaction after reaching a saturation point where all enzyme active sites are occupied. At this point, adding more enzyme will not increase the reaction rate further.
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
The rate-limiting step of an enzyme-catalyzed reaction is the slowest step in the reaction that determines the overall rate at which the reaction proceeds.
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
The rate of an enzyme-catalyzed reaction is often referred to as the enzyme's catalytic activity or turnover rate. It is a measure of how quickly the enzyme can convert substrate molecules into products.
is to catalyse or increase the rate of reaction without any change in itself .
Presence of:Competitive inhibitorsNon-competitive inhibitorsAllosteric sitesNegative feedback inhibitionIncrease/decrease of enzyme/substrateCooperativity
The rate of the enzyme-controlled reaction will increase until all enzyme active sites are saturated with substrate. After that point, the rate will remain constant as all enzyme molecules are already actively engaged, leading to saturation kinetics.