Without knowing the enzyme you are interested in, it is hard to give an exact answer. It all depends on the amount of the substrate, temperature, the resultant product, whether either is involved in a chain reaction or a simple reaction and if there is a co-enzyme involved.
See the link below for more information on the reaction:
saturation limit
40
69 F
The rate of a reactions usually increases when catalyzed by an enzyme. For maximum rate of activity, the enzyme needs optimal conditions.
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 function of an enzyme is to increase the rate of a reaction.
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
The rate of a reactions usually increases when catalyzed by an enzyme. For maximum rate of activity, the enzyme needs optimal conditions.
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.
when heating it it prevents the enzyme from adapting faster and that takes time for the enzyme to adapt which will take more time and make the rate at which the reaction occurs slower. did i answer ur question? :)
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.
It's 350 - I'm n biology HNRS
At low substrate concentrations, the rate of enzyme activity is proportional to substrate concentration. The rate eventually reaches a maximum at high substrate concentrations as the active sites become saturated.
When an enzyme is saturated the amount of substrate added no longer as an effect on the rate of the reaction.
Noncompetitive inhibitors decrease the rate of an enzyme reaction by bonding to an enzyme somewhere other than the active site, deforming it and permanently disabling the enzyme, so that enzyme can never function again, so the rate of reaction decreases.
The measure is the rate of reaction.
The function of an enzyme is to increase the rate of a reaction.
add more substrate. The rate of the reaction drops when the enzyme no longer has a maximum number of substrate molecules to interact with. Above the maximum substrate concentration, the rate will not be increased by adding more substrate; the enzyme is already working as fast as it can. An enzyme can catalyze a certain number of reactions per second, and if there is not sufficient substrate present for it to work at its maximum velocity, the rate will decrease. Therefore, to keep the enzyme working at its maximum, you must add more substrate.
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.