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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.
The more substrate the faster the rate of reaction up to a point where it levels out. Basically the enzymes and substrates bounce around until they meet the substrate that the enzyme can catalyse so obviously with more substrate there's more chance of he enzyme bumping into the right substrate
Enzymatic reaction rate, there's no term which is specifically used.
An enzyme
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.
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
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.
Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
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 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.
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.