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Vmax is the maxim initial velocity (Vo) that an enzyme can achieve. Initial velocity is defined as the catalytic rate when substrate concentration is high, enough to saturate the enzyme, and the product concentration is low enough to neglect the rate of the reverse reaction. Therefore, the Vmax is the maximum catalytic rate that can be achieved by a particular enzyme.
Km is determined as the substrate concentration at which 1/2 Vmax is achieved. This kinetic parameter therefore importantly defines the affinity of the substrate for the enzyme.
These two parameters for a specific enzyme defines:
Vmax - the rate at which a substrate will be converted to product once bound to the enzyme.
Km - how effectively the enzyme would bind he substrate, hence affinity.
Wiki User
∙ 12y ago
Wiki User
∙ 12y agoThis would have to be done via experiments. One would use a spectrophotometer, and record the rate at different substrate concentrations. The point at which the rate seems to no longer increase would be the Vmax. This relates to Michaelis-Menten equation of v=Vmax[S]/km+[S]
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Suppose that the enzyme concentration was increased by a factor of four what would be the value of km and vmax?
KM would not change, since it is a constant. Vmax would half, because Vmax depends on the concentration of the enzyme.
What does increased Vmax suggest?
An increase in Vmax suggest an increase in the amount of enzyme in the reaction. Also this increase in Vmax deceases the Km vaule, which means less substrate is needed.
How do you estimate the value of Vmax for two different concentrations of the substrate?
The Vmax would be the highest rate, when the enzyme is fully saturated. So as you increase substrate the Vmax will increase to a certain point (Vmax). Beyond that point, no matter how much substrate you add the Vmax will not increase.
What are k-series and v-series enzymes?
A K-Series enzyme is an enzyme that changes the Km of an enzyme on the michaelis menten or lineweaver burk graphs A V-series enzyme affects the Vmax
Calculation fraction of enzyme bound to substrate?
The calculation fraction of enzyme bound to substrate is used when determining the Michaelisâ??Menten equation. It is widely used in the enzyme kinetics.
What is the simple definition of saturation kinetics in biochemistry?
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.
What is michelis menten curve how it is useful in the study of enzyme kinetics?
The michaelis menten cruve is a plot of initial velocity vs substrate concentration. From this plot one can measure a Vmax and Km.
Does vmax increase with increasing amount of enzyme?
Yes, Vmax has a linear relationship with the amount of enzyme. This in turn deceases the Km of the reaction.
The initial rate of an enzyme catalysed reaction depend on?
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.
Is Vmax a threshold of substrate concentration for initiation of an enzymatic reaction?
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}
How might amino acid change affect the enzyme?
The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
How do you calculate vmax value?
The Vmax value in enzyme kinetics is determined by measuring the initial rate of reaction at varying substrate concentrations and plotting them on a graph. The Vmax is the maximum velocity achieved by the enzyme when it is saturated with substrate. It is typically determined by extrapolating the initial velocity data to when the enzyme is fully saturated with substrate.
What is the type of enzyme inhibition in which the Km changes but the Vmax does not?
competitive
Suppose that the enzyme concentration was increased by a factor of four what would be the value of km and vmax?
KM would not change, since it is a constant. Vmax would half, because Vmax depends on the concentration of the enzyme.
What does increased Vmax suggest?
An increase in Vmax suggest an increase in the amount of enzyme in the reaction. Also this increase in Vmax deceases the Km vaule, which means less substrate is needed.
How do you estimate the value of Vmax for two different concentrations of the substrate?
The Vmax would be the highest rate, when the enzyme is fully saturated. So as you increase substrate the Vmax will increase to a certain point (Vmax). Beyond that point, no matter how much substrate you add the Vmax will not increase.
What happens to the vmax when a competitive reversible inhibitor is added to an enzyme?
The vmax stays the same as the competitive reversible inhibitor does not affect catalysis in the enzyme-substrate.
