There are several things that determine an enzyme's activity. The main determinants include the structure of the enzyme, temperature, pH and so much more.
The percent activity of enzymes at pH 3.5 can vary significantly depending on the specific enzyme in question, as each enzyme has an optimal pH at which it functions best. Many enzymes, particularly those from acidic environments, may exhibit high activity at pH 3.5, while others that prefer neutral or alkaline conditions may show reduced activity. To determine the exact percent activity, experimental data specific to the enzyme must be consulted. Generally, enzyme activity is highest at their optimal pH and decreases outside of that range.
Enzymes are highly sensitive to changes in temperature and pH. They also can be affected by the presence of specific cofactors or inhibitors that can modulate their activity. Additionally, the substrate concentration can impact the rate at which enzymes function.
pH can influence the stability and activity of enzymes by affecting their charge and conformation. Enzymes have an optimal pH at which they function most efficiently, and deviations from this pH can lead to denaturation or loss of activity. Changes in pH can disrupt the hydrogen bonds and electrostatic interactions that stabilize the enzyme's structure, leading to a loss of its catalytic activity.
Enzymes are typically proteins, although some RNA molecules can also exhibit catalytic activity as enzymes.
Enzymes activity is affected by temperature. At a very high temperature, enzymes became denature that means they lose their original shape, which is important for them to react. Thus, enzyme activity decreases at a very high temperature.
The enzyme curve helps us understand how enzymes work by showing the relationship between enzyme concentration and reaction rate. It helps us determine the optimal conditions for enzyme activity and how enzymes can be inhibited or enhanced.
Extracellular enzyme activity is easier to determine because extracellular enzymes are released outside the cell and can be directly measured in the surrounding environment. In contrast, intracellular enzymes are contained within the cell, requiring cell disruption to access them for measurement, which can introduce variability and complexity to the assay.
One, by the genetically controlled 'copy number' of the number of individual enzymes available to the cytoplasm; two, by the concentration {or presence} of control factors that determine the activity of individual enzymes; and three, by the presence or absence of various termination factors that determine which Version of an enzyme is to be produced.
No, enzymes do not require ATP for their catalytic activity.
The percent activity of enzymes at pH 3.5 can vary significantly depending on the specific enzyme in question, as each enzyme has an optimal pH at which it functions best. Many enzymes, particularly those from acidic environments, may exhibit high activity at pH 3.5, while others that prefer neutral or alkaline conditions may show reduced activity. To determine the exact percent activity, experimental data specific to the enzyme must be consulted. Generally, enzyme activity is highest at their optimal pH and decreases outside of that range.
what i know is enzymes are denatured in organic solvents loosing their activity.
lysosomal enzymes
Temperature
Enzymes are highly sensitive to changes in temperature and pH. They also can be affected by the presence of specific cofactors or inhibitors that can modulate their activity. Additionally, the substrate concentration can impact the rate at which enzymes function.
All enzymes have optimal conditons, when it will work at its best. For example, if the temprature is too high the protein can become denatured. This is alos the case with Ph. Substrate level also affects enzyma activity because the more substartes there are, the more enxymes can bind to them.
pH can influence the stability and activity of enzymes by affecting their charge and conformation. Enzymes have an optimal pH at which they function most efficiently, and deviations from this pH can lead to denaturation or loss of activity. Changes in pH can disrupt the hydrogen bonds and electrostatic interactions that stabilize the enzyme's structure, leading to a loss of its catalytic activity.
Temperature, pH, substrate concentration