Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
enzymes and metaboli
| Term | Definition |
|---|---|
| Define metabolism. | The sum of all chemical reactions occurring in an organism. |
| Define metabolic pathway. | A series of enzyme-controlled reactions in which the product of one reaction becomes the substrate for the next. |
| Define anabolism. | The synthesis of complex molecules from simpler ones using energy. |
| Example of anabolism. | Protein synthesis or DNA replication. |
| Define catabolism. | The breakdown of complex molecules into simpler ones, releasing energy. |
| Example of catabolism. | Digestion or cellular respiration. |
| What are enzymes? | Biological catalysts that speed up chemical reactions without being consumed. |
| Why do enzymes increase reaction rates? | They lower the activation energy of a reaction. |
| Define activation energy. | The minimum energy required for a chemical reaction to start. |
| What is the active site? | A specific region of the enzyme where substrates bind. |
| Define substrate. | The molecule that the enzyme acts upon. |
| What model explains enzyme–substrate interaction? | The induced-fit model. |
| What is the induced-fit model? | The enzyme changes shape slightly to fit the substrate more precisely when the substrate binds. |
| What affects enzyme activity? | Temperature, pH, and substrate concentration. |
| How does temperature affect enzyme activity? | It increases activity as particles gain kinetic energy until an optimum; high temperatures cause denaturation. |
| How does pH affect enzyme activity? | Each enzyme has an optimal pH; extreme pH changes alter charges on R groups and denature the enzyme. |
| How does substrate concentration affect enzyme activity? | Activity increases as substrate concentration rises until enzymes become saturated and reach a maximum rate. |
| Define denaturation. | Loss of an enzyme’s specific three-dimensional structure and function due to factors like heat or pH changes. |
| Difference between an enzyme and a catalyst. | Enzymes are biological protein catalysts; catalysts can also be inorganic substances. |
| Define competitive inhibition. | An inhibitor resembles the substrate and binds to the active site, blocking substrate binding. |
| Define non-competitive inhibition. | An inhibitor binds to an allosteric site, changing the enzyme’s shape and reducing activity. |
| Example of competitive inhibition. | Malonate inhibiting succinate dehydrogenase in the Krebs cycle. |
| Example of non-competitive inhibition. | Cyanide inhibiting cytochrome oxidase in the electron transport chain. |
| Define allosteric site. | A site on the enzyme other than the active site where a molecule can bind and change enzyme activity. |
| Define end-product inhibition. | The final product of a metabolic pathway inhibits an earlier enzyme to regulate the pathway. |
| What type of inhibition is end-product inhibition? | Non-competitive, allosteric inhibition. |
| Why is end-product inhibition important? | It prevents overproduction of the end product and conserves energy and resources. |
| Example of end-product inhibition. | Isoleucine acting as an end-product inhibitor of threonine deaminase in isoleucine synthesis. |
| What are cofactors? | Non-protein molecules or ions that help enzymes function properly. |
| What are coenzymes? | Organic cofactors, often derived from vitamins, that assist enzyme activity. |
| What is ATP? | A small, energy-carrying molecule that stores and releases energy for cellular processes. |
| How is ATP related to metabolism? | It is produced by catabolic reactions and used to drive anabolic reactions. |
| Define phosphorylation. | The addition of a phosphate group to a molecule, often activating or deactivating enzymes. |
| Define enzyme specificity. | The tendency of an enzyme to catalyze only one particular reaction or act on a specific substrate. |
| What determines enzyme specificity? | The complementary shape and chemical properties of the active site and substrate. |
| Why are enzymes reusable? | They are not consumed or permanently changed during the reactions they catalyze. |
| What are immobilized enzymes? | Enzymes fixed to a surface or beads for repeated and controlled use in industrial processes. |
| Benefits of immobilized enzymes. | They are reusable, more stable, and easy to separate from reaction products. |
| Example of immobilized enzyme use. | Lactase immobilized on beads to produce lactose-free milk. |
Created by:
user-1970252