DNA, RNA, and Proteins - Biology

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 peptide bond is formed between the carboxyl group and amino group of adjoining amino acids. The energy in proteins is released when peptide bonds are broken. Peptide bonds also determine the primary structure of proteins.

An ionic bond is formed when one element loses an electron and another element gains an electron. Ionic bonds most frequently form between metals and non-metals, and are not commonly seen in proteins.

A glycosidic bond is formed between a carbohydrate and another molecule. Glycosidic bonds can help form carbohydrate polymers, like glycogen, or link sugars to other groups, like in the DNA backbone.

An ester bond can be found in fatty acids, and contains a carbonyl group next to an ether linkage.

Collagen is the most abundant protein in the human body. It adds great strength and flexibility to skin, tendons, and ligaments. These qualities are characteristic of structural proteins.

Globular proteins are generally rounded, protecting a nonpolar center from the aqueous environment around the protein. Most cytoplasmic proteins and enzymes are globular proteins. In contrast, fibrous proteins are generally elongated and designed for structural support; collagen is a fibrous protein, in addition to a structural protein. Integral proteins span the plasma membrane, often creating channels.

Proteins are classified into several categories based on where they perform their function. Peripheral membrane proteins span only one side of the lipid bilayer and thus have mobility. Unlike integral membrane proteins, which span the entire lipid bilayer, peripheral membrane proteins have the liberty of traveling from layer to layer as well as flip flop between the two bilayers.

Isomers are molecules that have the same molecular formula, but have different chemical structures. Isomerases are enzymes that are able to rearrange the structure of a molecule while keeping its chemical formula the same.

A protein consists of amino acids. Essential amino acids cannot be synthesized by the body, and must be included in the diet. A protein containing all of the essential amino acids is called a complete protein. An incomplete protein lacks one or more of the essential amino acids.

Neurotransmitters are chemicals that relay messages from one cell to the next. Enzymes are protein catalysts that speed up biological reactions. Minerals are inorganic compounds and are not present in the body in large amounts, with the exception of hydroxyapatite crystal found in bones. Electrolytes are ionic salts in the blood, tissue fluids, and cells, such as sodium, potassium, and chlorine.

Receptor proteins in a signal transduction pathways can be found both within the plasma membrane or cytosol; as a result, protein Y could potentially function as a receptor. The electron transport chain occurs in the mitochondria, and relies on the movement of electrons; the proteins that “move” these electrons, and subsequently pump protons (creating a gradient), are located in the inner membrane. An antiporter functions in a membrane as well due to its importance in creating and maintaining a concentration gradient. In a similar fashion, nuclear trafficking refers to the regulation or movement of molecules in and out of the nuclear membrane. Last, DNA replication occurs in the nucleus and does not involve a membrane of any sort; therefore, the membrane dwelling protein Y cannot function in this process.

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.