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The higher the substrate concentration, the higher the rate of reaction, up till the point when the limiting factor is no longer the concentration of substrate but other factors like enzyme concentration of temperature.
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.
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
because the amount of the other variables are the same, no change. once 4.0 g of lactose substrate or whatever it is is at it's maximum reaction rate, it can do no one reaction therefore there was no reaction in the 8.0 g of substrate. Because the reaction volume was also doubled; so there was no change in concentration of substrate.
pH, temperature, substrate concentration and enzyme concentration influences the rate of 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.
The higher the substrate concentration, the higher the rate of reaction, up till the point when the limiting factor is no longer the concentration of substrate but other factors like enzyme concentration of temperature.
Saturation Kinetics- an enzyme reaction in which there is enough enzymes to constantly have a substrate bound them and therefore the reaction is occurring at Vmax. This velocity is only limited by the concentration of substrates, not the enzyme.
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?
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
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.
The initial velocity of a gradually increases during enzyme substrate reaction. The concentration of the substrate also increases with it.
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
Oddly phased question in my opinion. Vmax is only effected by the amount of enzyme present in the reaction. Substrate concentration has zero effect on Vmax. There for I believe the answer in no. {Enzyme concentration is responsible for this}
Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.
Temperature, pH, Substrate concentration, Enzyme concentration, Inhibitor concentration (ex. ammonia)
pH Temperature Ionic Strength Aw Substrate Concentration Substrate location.