AP Biology Chapter 8- Introduction To Metabolism Test

Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy required for the reaction to occur. They do this by binding to the reactant molecules and orienting them in a way that makes the reaction more favorable. Enzymes themselves are not consumed in the reaction and can be used repeatedly. Therefore, the correct answer is "Speed up chemical reaction."

Metabolism refers to all the chemical reactions that occur within an organism. These reactions include both the breakdown of complex molecules into simpler ones, known as polymer to monomer reactions, and the synthesis of complex molecules from simpler ones, known as monomer to polymer reactions. These reactions are crucial for maintaining life as they provide energy and building blocks for various biological processes. Therefore, the correct answer is "All of the chemical reactions in an organism."

Catabolism refers to the process of breaking down complex molecules into simpler ones. In this context, it specifically refers to polymer to monomer reactions that release ATP and break down. This means that large molecules, such as proteins or carbohydrates, are broken down into smaller units, such as amino acids or glucose, respectively. These reactions release energy in the form of ATP, which can be used by the organism for various cellular processes.

Anabolism refers to the process of monomer to polymer reactions that require ATP and build up. This means that smaller molecules (monomers) are combined to form larger molecules (polymers) with the input of energy in the form of ATP. Anabolism is responsible for the synthesis of complex molecules such as proteins, nucleic acids, and polysaccharides, which are essential for the growth and maintenance of an organism.

A competitive inhibitor is a type of inhibitor that binds to the active site of an enzyme, preventing the substrate from binding and inhibiting the enzyme's activity. This type of inhibitor competes with the substrate for binding to the active site. By occupying the active site, the competitive inhibitor effectively blocks the substrate from binding and slows down the enzyme's catalytic activity.

Denaturing an enzyme refers to the process of altering its shape, usually by exposing it to extreme temperatures or pH levels. This change in shape affects the active site of the enzyme, which is the region where it binds with its substrate. In this case, the correct answer suggests that denaturation of the enzyme causes a change in the shape of its active site, rendering it unable to function properly or work at all.

Allosteric enzymes are enzymes that can change their shape to switch between active and inactive states. This ability allows them to regulate their activity in response to specific signals or molecules in the cell. Unlike enzymes that are easily denatured or unable to be denatured, allosteric enzymes have a unique mechanism that allows them to modulate their function based on the needs of the cell. Therefore, the correct answer is "Enzymes that change shape to toggle between active and inactive."

When an inhibitor attaches to an allosteric enzyme, it causes a conformational change in the enzyme's shape, which leads to a decrease in its activity. This binding of the inhibitor molecule to the enzyme's allosteric site alters the enzyme's active site, making it less accessible to the substrate molecules. As a result, the enzyme becomes inactive and is unable to catalyze the reaction.

The active site is the part of the enzyme where the substrate is given an induced (tight) fit. This is where the enzyme and substrate interact and undergo a chemical reaction. The active site has a specific shape that complements the shape of the substrate, allowing for a precise and efficient binding. The induced fit refers to the conformational changes that occur in both the enzyme and substrate upon binding, ensuring a tight and optimal interaction.

Enzymes are a type of protein that act as catalysts in biochemical reactions. They help to speed up these reactions by lowering the activation energy required. Therefore, all enzymes are proteins. However, not all proteins are enzymes. Proteins have various other functions in the body, such as providing structure, transport molecules, and signaling molecules. So, while all enzymes are proteins, there are many other types of proteins that are not enzymes.

The correct answer is A and D because the substrate refers to the reactant(s) on which the enzyme acts, and in this case, it can react on both the products and the reactants.

ATP (adenosine triphosphate) has two high energy bonds. These bonds are located between the phosphate groups in the molecule. When one of these bonds is broken, it releases a significant amount of energy that can be used by cells for various metabolic processes. Therefore, ATP is often referred to as the "energy currency" of the cell.

ADP (adenosine diphosphate) has one high-energy bond. This bond is located between the second and third phosphate groups in the molecule. When this bond is broken, energy is released, and ADP is converted into ATP (adenosine triphosphate), which is the primary energy currency in cells.

Adenosine is made up of adenine and ribose. Adenine is a nitrogenous base and ribose is a sugar molecule. Adenosine is a nucleoside, which is a combination of a nitrogenous base and a sugar molecule. In the case of adenosine, adenine is bonded to ribose through a glycosidic bond.

Allosteric enzymes become active when an activator attaches to them. This activator molecule binds to a specific site on the enzyme, causing a conformational change in the enzyme's structure. This change allows the enzyme to bind to its substrate more effectively and catalyze the reaction. In contrast, an inhibitor molecule would bind to the enzyme and prevent it from becoming active. Therefore, the attachment of an activator is necessary for the activation of allosteric enzymes.

An enzyme inhibitor is a substance that slows down the activity of an enzyme. It does not completely stop the enzyme or denature it, but rather reduces its ability to catalyze chemical reactions. This can be achieved by binding to the enzyme and interfering with its active site, preventing the substrate from binding and the reaction from occurring at its normal rate. Inhibitors can be competitive, non-competitive, or uncompetitive, depending on their mode of action.

To overcome the inhibitor, increasing the concentration of substrate is an effective strategy. By increasing the concentration of substrate, more substrate molecules are available for the enzyme to bind to, which can help to compete with the inhibitor. This can potentially overcome the inhibitory effect and allow the enzyme to function at a higher rate. Increasing the concentration of substrate can also help to shift the equilibrium towards the formation of product, counteracting the inhibitory effect of the inhibitor.

AMP, or adenosine monophosphate, does not have any high-energy bonds. High-energy bonds are typically found in molecules like ATP (adenosine triphosphate) and GTP (guanosine triphosphate), where the bonds between the phosphate groups are easily hydrolyzed to release energy. In AMP, there is only one phosphate group, so it does not possess any high-energy bonds.

When a phosphate leaves ATP, it becomes ADP (adenosine diphosphate). The addition of an "i" to ADP indicates that it is inorganic. This means that the phosphate group is not bound to any organic molecule and is floating around freely. The presence of the inorganic phosphate does not have any specific effect on the reaction itself, hence it is just floating around with no significant impact. Therefore, the correct answer is A and B, indicating that the phosphate is inorganic and has no affect on the reaction.

A non-competitive inhibitor is an inhibitor that binds to a site on the enzyme other than the active site, causing a conformational change in the protein structure. This change prevents the enzyme from functioning properly, inhibiting its activity. In some cases, non-competitive inhibitors can act as poisons, causing harm to the organism. Therefore, the correct answer is B and C.