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Q: Which segmant would be different if it were catalyzed by an enzyme?
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What would happen if most biochemical reactions are catalyzed by the same enzyme?

If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount.


Why do you need a catalyst during a enzyme reaction?

A catalyst speeds up the rate of a chemical reaction by lowering the activation energy needed for the reaction to occur. In the case of an enzyme-catalyzed reaction, the enzyme serves as a biological catalyst, allowing the reaction to occur more efficiently and at lower energy levels than it would without the enzyme.


Why would boiling an enzyme stop it from functioning?

Destroying the active site of an enzyme would no longer allow a substrate to bind to it, therefore stopping the enzyme from working.


Why is it necessary for a cell to produce one enzyme molecule for every substrate molecule that needs to be catalyzed?

Enzymes are catalysts that speed up chemical reactions by lowering the activation energy required to initiate the reaction. To efficiently catalyze a chemical reaction, one enzyme molecule binds to each substrate molecule in order to facilitate the reaction at a higher rate. This stoichiometry ensures that all substrates are converted into products in a timely manner.


What would be a good enzyme lab for ib biology?

A good enzyme lab for IB Biology could involve investigating how factors such as temperature, substrate concentration, or pH affect the activity of an enzyme like amylase. Students could test the enzyme activity under different conditions using a spectrophotometer to measure changes in absorbance, or by observing changes in the rate of a reaction such as the breakdown of starch. This type of lab allows students to explore enzyme kinetics and understand the factors that influence enzyme activity.

Related questions

What would happen if most biochemical reactions are catalyzed by the same enzyme?

If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount.


What is a question your trying to answer in a lab?

One question that a lab might be trying to answer is: What is the effect of temperature on enzyme activity? This type of experiment would involve testing how changes in temperature impact the rate of enzyme-catalyzed reactions in a controlled setting.


What would happen if an active site was blocked by another molecule?

If an active site is blocked by another molecule, it could prevent the substrate from binding to the enzyme, inhibiting the enzyme's function. This can lead to a decrease in the rate of the enzymatic reaction or complete inhibition of the reaction.


Why do you need a catalyst during a enzyme reaction?

A catalyst speeds up the rate of a chemical reaction by lowering the activation energy needed for the reaction to occur. In the case of an enzyme-catalyzed reaction, the enzyme serves as a biological catalyst, allowing the reaction to occur more efficiently and at lower energy levels than it would without the enzyme.


What could be added to an enzyme-catalyzed reaction to decrease its rate?

Decreasing the temperature of the system


Why would you expect the rate of an enzyme-catalyzed reaction to increase proportionately to enzyme concentration given an unlimited supply of substrate?

Increasing enzyme concentration typically leads to more enzyme-substrate complexes, thereby increasing the rate of the reaction. In the presence of excess substrate, the reaction rate is limited by the enzyme concentration, resulting in a proportional increase in the rate of the reaction with increasing enzyme concentration. This relationship holds until all substrate molecules are bound to enzyme molecules, reaching saturation.


Why would boiling an enzyme stop it from functioning?

Destroying the active site of an enzyme would no longer allow a substrate to bind to it, therefore stopping the enzyme from working.


Why is it necessary for a cell to produce one enzyme molecule for every substrate molecule that needs to be catalyzed?

Enzymes are catalysts that speed up chemical reactions by lowering the activation energy required to initiate the reaction. To efficiently catalyze a chemical reaction, one enzyme molecule binds to each substrate molecule in order to facilitate the reaction at a higher rate. This stoichiometry ensures that all substrates are converted into products in a timely manner.


What does enzyme catalyzed reaction mean?

To catalyze a reaction means to speed it up. Enzymes speed up reactions by bringing together the chemicals that are needed to react, rather than waiting for them to "bump into" each other by chance. If it weren't for enzymes, most reactions in living cells would happen too slowly to be useful.


What would an enzyme be called if it moves methyl groups between molecules?

It would be called a transferase. A transferase is defined as an enzyme which "transfers chemical groups between different molecules."Source:Daugherty, Ellyn. "Enzymes: Protein Catalysts." Biotechnology: Science for the New Millennium. St. Paul, MN: Paradigm, 2007. 143-44. Print.


At what pH would the enzyme be most effective?

The ideal pH for an enzyme's activity depends on the specific enzyme. Most enzymes have an optimal pH where they function most efficiently, typically within the range of pH 6 to 8 for many enzymes found in the human body. Extreme pH values can denature enzymes and reduce their activity. It is important to maintain the appropriate pH conditions to maximize enzyme effectiveness.


If an enzyme is a protein how might you change the specificity of such an enzyme?

What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.