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The enzyme whose activity decreases in both acidic and basic environments is pepsin. Pepsin is an enzyme found in the stomach that functions optimally at a pH of around 2. In environments that are either too acidic or too basic, the structure of pepsin can be denatured, leading to a decrease in enzymatic activity.

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What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?

Allosteric inhibitors bind to a specific site on an enzyme (allosteric site) other than the active site, inducing a conformational change that decreases enzyme activity. This alteration prevents the substrate from binding to the active site, thus blocking the enzyme's ability to catalyze reactions.


How does temperature change the action of enzymes?

Temperature can affect enzyme activity because enzymes work best within specific temperature ranges. At low temperatures, enzyme activity decreases as the molecules move more slowly, decreasing the likelihood of enzyme-substrate collisions. At high temperatures, enzyme activity can be disrupted because the enzyme structure can become denatured, leading to a loss of function. Optimal temperature for enzyme activity varies depending on the specific enzyme.


What is the loss of carbon-fixing activity of the enzyme RuBP carboxylase directly proportional to?

The loss of carbon-fixing activity of the enzyme RuBP carboxylase is directly proportional to the rate of photorespiration in the plant. As photorespiration increases, the enzyme's efficiency in fixing carbon dioxide decreases, leading to reduced photosynthetic productivity.


What will most likely happen to an enzyme if it is placed in an environment that is too acidic or too basic?

If an enzyme is placed in an environment that is too acidic or too basic, its structure can be denatured, which means its active site will change shape and it will no longer be able to catalyze reactions effectively. This will decrease or even stop its enzymatic activity.


Does the pH affect the rate in which chymosin works?

Yes, the activity of chymosin, an enzyme involved in cheese making, is influenced by pH. Chymosin works best at its optimal pH level, which is usually slightly acidic. Deviations from this pH can affect the enzyme's activity and may slow down or inhibit its function.

Related Questions

How do you use inhibitor in a sentence?

An enzyme inhibitor is a substance that binds to an enzyme and decreases the enzyme's activity.


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.


Why as the temperature of blood increases the pH decreases?

As the temperature of blood increases, the activity of enzymes that regulate pH decreases, leading to a decrease in pH. This happens because enzymes function optimally within a specific temperature range, and when this range is exceeded, enzyme activity is disrupted, resulting in a pH decrease.


What happens to the activity of sucrase as the pH becomes more alkaline?

Sucrase activity decreases as the pH becomes more alkaline. This is because sucrase works optimally in a slightly acidic environment, and the enzyme becomes less effective at breaking down sucrose into glucose and fructose when the pH is too alkaline.


What is the function of sulphuric acid in the experiment of enzyme activity?

H2SO4 is used to denature the enzyme and stop the reaction instantly. by adding H2SO4,it will prevent further reaction of the enzyme onto the substrate and the rate of enzyme reaction can be measured in the specific time


Why might enzyme's activity decrease at very high temperatures?

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.


What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?

Allosteric inhibitors bind to a specific site on an enzyme (allosteric site) other than the active site, inducing a conformational change that decreases enzyme activity. This alteration prevents the substrate from binding to the active site, thus blocking the enzyme's ability to catalyze reactions.


How does temperature change the action of enzymes?

Temperature can affect enzyme activity because enzymes work best within specific temperature ranges. At low temperatures, enzyme activity decreases as the molecules move more slowly, decreasing the likelihood of enzyme-substrate collisions. At high temperatures, enzyme activity can be disrupted because the enzyme structure can become denatured, leading to a loss of function. Optimal temperature for enzyme activity varies depending on the specific enzyme.


What happens to pepsin in high pH levels?

Pepsin is an enzyme that functions optimally in acidic environments, such as the stomach's low pH. In high pH levels, like those found in the small intestine, pepsin becomes denatured and its enzymatic activity decreases or stops altogether.


What is the effect of pH upon the relative enzyme activity?

Different enzymes work best at different pH. This is refered to as the ideal pH for the enzyme. For example, the digestive enzyme trypsin works best at an acidic pH while alkaline phosphatase works best at a basic pH. Therefore, enzyme activity varies with pH and this variation depends on the enzyme being studied


What is the loss of carbon-fixing activity of the enzyme RuBP carboxylase directly proportional to?

The loss of carbon-fixing activity of the enzyme RuBP carboxylase is directly proportional to the rate of photorespiration in the plant. As photorespiration increases, the enzyme's efficiency in fixing carbon dioxide decreases, leading to reduced photosynthetic productivity.


What is the optimum pH for tyrosinase?

The optimum pH for tyrosinase activity is typically around pH 6.5 to 7.5. This enzyme functions best in slightly acidic to neutral conditions. Extremes in pH levels can denature the enzyme and reduce its activity.