Protein Function - Biology

Enzymes are biological catalysts that increase the rate of a chemical reaction. This is accomplished by lowering the activation energy for the reaction. Enzymes increase the rate of a reaction, but do NOT increase the amount of products formed in the reaction. They simply cause the products to be formed faster.

A catalyst speeds up the rate of a reaction by lowering the activation energy, which is caused by the high energy transition state. Enzymes are a class of catalyst specific to biological processes, accelerating these processes by lowering activation energy and transition state energy. Catalysts and enzymes may help reactions move faster, but they do not affect the final equilibrium amounts of reactants and products.

Pepsin is an enzyme in the stomach that digests proteins. Because it is active in the stomach, which is highly acidic, pepsin best functions at a low pH between 2 and 2.5.

Pepsinogen is secreted by chief cells and converted into active pepsin after catalyzation by hydrochloric acid. The acid is secreted by parietal cells in response to gastrin secretion by G cells. After the stomach contents enter the duodenum of the small intestine, the acid is neutralized by bicarbonate secretions from the pancreas. This prevents the acid from damaging the walls of the small intestine.

Catalysts are molecules that are capable of increasing reaction speed. Enzymes are a particular subset of catalysts; enzymes are proteins that can aid in biological reactions and are crucial to many metabolic processes that occur in cells. Enzymes lower the activation energy of a given reaction, allowing the reaction to proceed faster. The active site of an enzyme is the region of the enzyme that can bind a substrate, when a substrate collides into the enzyme molecule. Joining of an enzyme and substrate results in a chemical reaction whereby the substrates are converted into products. The active site of an enzyme is specific to the substrate's shape, like a lock-and-key mechanism.

Enzymes work by lowering the activation energy of a reaction, which can occur either by bringing reactants closer together or by destabilizing the transition state. They do not affect the equilibirum of the reaction, meaning they do not affect the amount of reactants or products. They simply increase the speed at which products can be formed by reducing the amount of energy needed to power the reaction.

Enzymes are biological catalysts that bind to specific substrates. Enzyme activity is tightly regulated by activators and/or inhibitors. Enzymes will change shape as a result in an induced fit when bound to their substrates, activators, and/or inhibitors. Since enzymes are proteins, environmental changes will affect their activity. For example, high temperatures will denature the protein, rendering the enzyme inactive. Isozymes are a group of enzymes that do not have the exact same amino acid sequence, yet they catalyze the same reactions. Enzymes need cofactors, such as prosthetic groups and/or coenzymes in order to function properly. The precursors to coenzymes are vitamins in the diet.

Temperature and pH can affect enzyme activity because they may alter the shape and effectiveness of the enzyme through protein denaturation. Likewise, the availability of reactants and substrates controls the amount of product that the enzyme can catalyze during the reaction. If they are present in low concentrations, then they will inhibit the enzyme’s activity.

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.

A competitive inhibitor will temporarily bind to the active site on an enzyme. This forbids substrates from entering the enzyme's active site and stops the enzyme from catalyzing the reaction.

In contrast, non-competitive inhibitors will bind to other regions of the enzyme, outside of the active site, and cause the active site to change shape. This change then prevents substrates from binding.

Inhibitors are able to prevent maximum enzymatic rates in a variety of ways. Some inhibitors, like noncompetive inhibitors, are able to attach at a point on the enzyme and alter its conformation. Competitive inhibitors, however, bind directly at the active site, which prevents substrate from entering the enzyme.

Competitive inhibitors are the only inhibitor type to bind directly to the enzyme actve site.

An inhibitor binds to an enzyme and stops it from performing its normal function. It does not destroy the enzyme and does not change the amount present, but it decreases the amount of activity of that enzyme.

Most inhibitors work by binding to an enzyme so that the substrate cannot bind to the enzyme, and thus the function cannot take place.

Inhibitors generally affect functionality by interfering with the reaction without altering the amount of substrate or enzyme molecules.

The correct answer is competitive inhibiiton by Compound A. You can gather that because Compound A's inhibitory properties were negated, the reaction rate increased. As a result, competitive inhibition by Compound A takes place since the reaction rate increases as reactant concentration increases which occurs regardless of inhibitor presence (assuming enough enzymes are present). In contrast, the concentration of reactants would be irrelevant in the case of allosteric regulation either by Compound A or an unknown compound. Enzyme Breakdown would not result in an increase of the reaction rate.

A noncompetitive inhibitor does not directly compete with the substrate binding to the substrate-binding site of an enzyme. The inhibitor instead binds to another site on the enzyme, which alters the enzyme's affinity for its substrate; therefore, adding more substrate would not cause a change in enzymatic activity.

Hemoglobin is a protein found in red blood cells. It has a high affinity to bind to oxygen, carbon dioxide, and carbon monoxide. In the lungs, where oxygen concentrations are high, hemoglobin will bind to oxygen molecules and carry them through the blood to deliver to the cells of the body. Oxygen can then be used by these cells to gain energy through oxidative phosphorylation and the electron transport chain, which require oxygen as an electron receptor.

Though hemoglobin can bind carbon dioxide, most carbon dioxide waste is dissolved in the blood in the form of bicarbonate and carbonic acid. Hemoglobin's high affinity for carbon monoxide means that, when the gas is present in excess, it can block the binding sites for oxygen. This is the reason for the toxicity associated with carbon monoxide poisoning.

Proteins have the most diverse functions in biological systems. Their remarkable diversity in function is due to their diversity in structure. Structural proteins, such as tubulin and collagen, have a fibrous structure that aids their function. Enzymes have active sites that allow them to bind specific molecules (substrates) and enact a conformational change to facilitate chemical reactions. Signaling proteins include several types of hormones, known as peptide hormones. Protein receptors are commonly found embedded in the cell membrane and contain active sites to bind substrates, hydrophilic regions to interact with the cell environment and extracellular space, and hydrophobic regions to interact within the lipid bilayer.