Enzymes - AP Biology

The stomach is an acidic environment; therefore, one would expect pepsin to be most active at an acidic pH. The answer choice “2” is the most acidic pH. It is also the pH that is generally found in the stomach. Although a pH of 6 is slightly acidic, it is not the pH found in the stomach.

A catalyst is responsible for a decrease in activation energy of a reaction. This allows an enzyme to use less energy to manipulate its substrate into a transition state.

Enzymes are biological molecules that help catalyze reactions by lowering the energy of activation and increasing the rate of a reaction. They can do this by a number of mechanisms including: providing a template for substrates to join together in an efficient manner; distorting a substrate so it approaches the unstable/transition state; and providing a microenvironment conducive to a reaction. Inhibitors and activators can affect enzymes activity by slowing down and increasing enzyme activity respectively.

Enzyme activity can be affected by environmental factors such as temperature and pH. This is because proteins denature and lose their shape at high temperatures and extreme pHs. Most enzymes prefer to act under a temperature close to body temperature. Optimal pH is usually physiologic at pH 6 to 8; however, digestive enzymes prefer lower pH around 2 to 3 (e.g. pepsin, which makes sense because pepsin works in acidic conditions within the stomach).

Enzymes are all proteins, however there are some RNA molecules that have been found to catalyze reactions, but they are termed ribozymes, not enzymes. They speed up reactions by lowering the activation energy of a reaction and do not change the energy states of the reactants or products.

Proteins can control rates of reaction and regulate cell processes, form muscle tissue, and transport substances into and out of cells. They do not store energy in fat cells.

Enzymes lower the activation energy in chemical reactions in cells. They do not alter the composition of products of chemical reactions.

The reactants of enzyme-catalyzed reactions are known as substrates. Enzymes catalyze formation of products from their substrates. Inhibitors hinder the efficacy of enzymes, thereby decreasing the rate of reactions, and nucleotides are the monomers of DNA and RNA.

The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.

Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.

The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.

pH and temperature affect enzyme activity, as there is an optimal pH and temperature for each enzyme, and a pH or temperature too far from the optimal level can cause the enzyme to denature. Substrate concentration affects enzyme activity; increasing substrate concentration will increase the rate of reaction to the point that the enzymes are saturated.

There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.

You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.

Temperature, pH, and substrate concentration all affect the function of an enzyme; therefore, the correct answer is all of these.

The correct answer to this question is they function under a narrow pH range.

Enzymes do indeed function under a narrow pH range. A narrow pH range is needed because enzymes speed up reactions by lowering the activation energy and in order to do this very specific conditions must be met. Coenzymes are not always needed and they are certainly not consumed in a reaction. Enzymes also are proteins so they are polymers of amino acids, not carbohydrates. Also enzymes have no part in the creation of ATP.

Statement I is false because increasing the substrate concentration will only help overcome competitive inhibition. Noncompetitive inhibition can only be overcome if the inhibitor is removed from the enzyme.

Statement II is also false because competitive inhibitors do not change the active site. They bind to the active site and prevent substrates from binding. Noncompetitive inhibitors bind elsewhere on the enzyme and alter the shape of the active site, thereby preventing substrate binding.

Statement III is true because noncompetitive inhibition does not affect the enzyme affinity for substrates. The enzyme still has the same affinity, but the substrates can’t bind because of the altered active site.

Competitive inhibition occurs when an substrate or inhibitor compete with the normal substrate for binding the active sight of an enzyme. The proper functioning of the enzyme depends on the concentration ratio of inhibitor to enzyme or substrate to enzyme. The competitive inhibition of the enzyme in this case by the antibiotic has potentially bactericidal or bacteriostatic effect on the bacteria until that antibiotic concentration decreases. Negative feedback involves the product of a set of metabolic reactions inhibiting the formation of a precursor of that metabolic pathway, thereby decreasing its own production.

Negative feedback interrupts a metabolic pathways by producing a substrate that inhibits enzymes in the beginning steps of the metabolic cycle. If a chemical is "mimicking" substrate C or causing Substrate C to be produced before other steps in a cycle, the enzyme is inhibited by the excess of substrate C thus the pathway can not continue. Most such molecules are proteins that interact with enzymes.

A substrate that acts as a "positive motivator" of, or to enhance a metabolic pathway, is also known as a positive feedback regulator or a substance that has a positive feedback mechanism.

Noncompetitive inhibition is a type of enzymatic alteration that results in changes to enzymatic function without alterations to the active site. If the active site was to be blocked, this compound would function via competitive inhibition. The other terms do not describe any type of enzymatic inhibition process in the human body. Be able to distinguish the difference between competitive and noncompetitive inhibition.