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Biothermo (OAT) 2
| Question | Answer |
|---|---|
| What is an anabolic reaction? | A reaction where small molecules assemble to form a larger molecule. |
| What is a catabolic reaction? | A reaction where large molecules are broken down into smaller molecules. |
| What is an exergonic reaction? | A reaction that releases free energy; it is spontaneous and has a negative ΔG. |
| What is an endergonic reaction? | A reaction that absorbs free energy; it is nonspontaneous and has a positive ΔG. |
| What is the difference between kinetic and potential energy? | Kinetic energy is energy in motion (e.g., jumping); potential energy is stored energy (e.g., glycogen). |
| How can nonspontaneous reactions be driven forward? | By coupling them with exergonic reactions, such as ATP hydrolysis. |
| What is the role of an enzyme? | Enzymes act as catalysts by lowering the activation energy of a reaction, increasing the reaction rate. |
| What is the active site of an enzyme? | The region of the enzyme where the substrate binds. |
| What is an allosteric site? | A secondary binding location on an enzyme where effectors (activators or inhibitors) bind. |
| What is the induced fit model? | When a substrate enters the active site, both the enzyme and substrate change shape slightly to better facilitate the reaction. |
| What is the enzyme-substrate complex? | The intermediate formed when a substrate binds to the active site of an enzyme. |
| List the key characteristics of enzyme function. | Substrate specific; unchanged by the reaction; catalyze both forward and reverse reactions; function varies with pH and temperature; bind substrates via induced fit. |
| What are ribozymes? | Enzymes made of RNA rather than protein. |
| What is competitive inhibition? | A substance mimics the substrate and binds to the active site, blocking substrate binding. It can be overcome by increasing substrate concentration. Km increases; Vmax stays the same. |
| What is noncompetitive inhibition? | A substance binds to the allosteric site (not the active site). The substrate can still bind, but the reaction is prevented. Km stays the same; Vmax decreases. |
| How do competitive and noncompetitive inhibition differ in their effect on Km and Vmax? | Competitive: Km increases, Vmax unchanged. Noncompetitive: Km unchanged, Vmax decreases. |
| How is ATP formed, and is it exergonic or endergonic? | ATP is formed via phosphorylation, creating an energy-rich triphosphate bond. ATP formation is endergonic. |
| How is ATP broken down, and is it exergonic or endergonic? | ATP is broken down via hydrolysis, releasing energy and phosphate. ATP hydrolysis is exergonic. |
| What is the primary role of ATP in the cell? | ATP stores energy from exergonic reactions (like those in the electron transport chain) and uses it to fuel endergonic reactions. |
| What is Vmax? | The maximum velocity of a reaction when the enzyme is fully saturated with substrate. |
| What is the Michaelis Constant (Km)? | The substrate concentration at which the reaction rate is half of Vmax. |
| What does a small Km indicate? | High binding affinity — less substrate is needed to reach Vmax. |
| What does Km inversely represent? | Binding affinity between the enzyme and substrate. |
Created by:
smurtab