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What happens to an allosteric enzyme when the concentration of substrate around the molecule increases?
When the concentration of substrate around an allosteric enzyme increases, more substrate molecules can bind to the active site and induce a conformational change in the enzyme. This can enhance the enzyme's catalytic activity by improving its binding affinity for the substrate or stabilizing the active conformation.
What is the optimal pH for maintaining a stable enzyme activity at a given substrate concentration of 10 mM?
The optimal pH for maintaining stable enzyme activity at a substrate concentration of 10 mM is typically around pH 7. Enzymes function best within a specific pH range, and deviations from this range can affect their activity. Maintaining the pH at around 7 helps to ensure that the enzyme is working efficiently at the given substrate concentration.
Can anyone help with this question Describe the relationship between substrate concentration and the initial reaction rate of an enzyme-catalyzed reaction Is this a linear relationship What happens t?
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
What factors increase the rates of enzyme-controlled reactions?
Factors that can increase the rates of enzyme-controlled reactions include higher substrate concentration, optimal pH and temperature conditions, the presence of cofactors or coenzymes, and specific enzyme activators. Additionally, enzyme concentration and the absence of competitive inhibitors can also enhance reaction rates.
Increasing the concentration of a substrate substance slows down the rate of reaction?
No, if you increase the concentration of a substance there is a more likely chance of particle collisions occurring. Meaning the higher the concentration the faster the rate of reaction. Imagine people walking around in an empty room, the more people there are in the room, the more likely it is that they will begin to bump into each other, it's the same with particles. The bumping into each other (or collisions) is what will increase the rate of reaction. Conversely if you lower the concentration, there is a lot less chance that the tiny particles will collide with one another meaning the rate of reaction will decrease. Hope this Helps!
What are the two different types of inhibition?
Increasing the temperature excessively - if an enzyme is heated too much (usually around 40°C) the enzyme will become denatured. This will prevent it from working permanently. Decreasing the temperature - decreases enzyme activity Enzyme inhibitors - heavy metals poison enzymes by binding to the active site, preventing the enzyme from binding to the substrate molecule.
What factors affect enzyme activity?
Temperature - too cold the enzyme will still work but slowly, too hot and the enzyme will become denatured . As temperature increases, the kinetic energy of the molecules increases so they move around more, meaning that there are more collisions between the enzymes and substrate molecules and therefore more reactions. pH - different types of enzymes work best in different pH environments. A change in pH interferes with the shape of the enzymes active site (where it bonds and reacts with substrate) and therefore does not fit the shape of the substrate as well so the enzyme is unable to work on the substrate. enzyme and substrate concentration - how many there is of each. Changing the concentrations of enzyme and substrate concentrations will affect the number of collisions between them and therefore the number of reactions. enzyme inhibitors - these are molecules which bind to enzymes, reducing their activity (many drugs are enzyme inhibitors). co-factors - these are chemical compounds which bind to enzymes and which are needed by the enzyme to work on substrate molecules. They are often called helper molecules.
How long does it take to sterilize mushroom substrate?
Sterilizing mushroom substrate typically takes around 1-2 hours.
What happens during diffusion?
Diffusion is the movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached. This process occurs passively, without the need for energy input, and allows for nutrients, gases, and wastes to be exchanged across cell membranes. Diffusion is essential for maintaining cell homeostasis and proper function in living organisms.
What is the optimum conditions of carbohydrase?
The optimum conditions for carbohydrase activity typically include a neutral pH (around 7), a temperature around 37°C, and a sufficient substrate concentration for the enzyme to work efficiently. Additionally, the presence of cofactors and ions like calcium or magnesium might also be needed for optimal enzyme activity.
What happens to the rate of enzyme reaction when you increase the enzyme concentration?
As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
What is the typical concentration of sodium to potassium intracellularly?
The typical concentration of sodium is lower than potassium intracellularly. Sodium concentration is around 10-15 mM, while potassium concentration is around 140-150 mM inside the cell. This concentration gradient is maintained through the action of the sodium-potassium pump.
