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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.


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?

No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.


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?

Because evey substrate needs its own enzyme. Every substance has it depends upon the dissociation constant for the enzyme/substrate interaction. Some enzymes can catalyze reactions for low-affinity substrates, as long as the concentration of substrate molecules is great enough.


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.


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.


At what pH would the enzyme be most effective?

It depends on what type of Enzyme. Enzymes have different optimum pH depending on the environment they work in, for example and enzyme in the stomach of a human would have a pH of about 2 but an enzyme in human saliva has an optimum pH of 5.6.


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.