it slows down the reaction time of the enzyme because there are too many substrates bumping into each other and make it harder for them to bind to the enzymes.
It doesn't
It doesn't
It doesn't
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.
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
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.
Factors that affect the rate of enzyme activity include temperature, pH, substrate concentration, and enzyme concentration. Temperature and pH can alter the shape of the enzyme, affecting its ability to bind to the substrate. Changes in substrate and enzyme concentration can affect the frequency of enzyme-substrate collisions, which impacts the rate of reaction.
Tobin can conclude that the reaction rate is directly proportional to the enzyme concentration when excess substrate is present. This is because at higher enzyme concentrations, all substrate molecules are already bound to enzyme active sites, leading to a maximal reaction rate even with excess substrate.
The three factors that affect the rate of a biochemical reaction are temperature, substrate concentration, and enzyme concentration. Temperature influences the kinetic energy of molecules involved in the reaction, substrate concentration determines the amount of reactants available for the reaction, and enzyme concentration affects the number of catalysts available to facilitate the reaction.
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.
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.