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Enzymes
| Question | Answer |
|---|---|
| What is an exergonic reaction? | generate/ release energy, "spontaneous" i.e. formation of chemical bond. |
| What is an endergonic reaction? | require energy. i.e. melting, breaking bonds. |
| What is a redox reaction? | Coupled reaction where energy transfer occurs REDUCTION: gain electron, or gain H. OxIDATION: lose electron, or lose H. |
| Define anabolism | total series of chemical reactions in synthesis of organic compounds |
| Define catabolism | series of chemical reactions that break down larger molecules |
| What does the suffix -ase indicate? | Enzyme |
| What impact do enzymes have on activation energy? | Lower it; allows reactants to move closer and reactions to occur more rapidly. |
| What is the difference between free energy in a catalyzed vs. un-catalyzed reaction? | No difference. |
| What organic molecule is an enzyme? | Protein. |
| What property determines enzyme function? | Shape, as per lock-and-key model. |
| What is the induced fit hypothesis? | Binding of the substrate to the enzyme changes the enzyme structure, further speeding up the reaction. |
| What is a coenzyme? | Non-protein organic molecule binding to enzymes near the active site. |
| Describe the role of NAD+ | Nicotinamide Adenine Dinucleotide is a coenzyme found in the cells of all organisms. Participates in oxidation as the electron carrier. Reacts to form NADH. |
| What is a cofactor? | Non-protein, possibly inorganic substance essential to enzyme activity. I.E. K+ or Ca+2 |
| Effect of temperature on enzymes. | High temperature will denature the protein. Low temperature will possibly slow reaction but protein remains intact. |
| Effect of pH on enzyme. | Enzymes perform according to prescribed pH, will become denatured outside of their range. |
| What effect does substrate and product concentration have on reaction? | Provide biofeedback mechanism, control rate of reaction. |
| What is an allosteric interaction? | Allosteric effector bound to enzyme changes its shape and temporarily stops enzyme reaction. Works as a negative control of enzyme interaction. |
| What is competitive inhibition? | Competition between regulatory compound and substrate for the binding site in an enzyme. Greater balance of regulatory binding shuts down or slows pathway. |
| What is non-competitive inhibition? | Inhibitory chemical binds to enzyme outside of its active site. |
| Describe irreversible inhibition. | Inhibitory chemical permanently binds to enzyme and denatures the protein. I.E. penicillin, nerve gas. |
| What are 5 ways to alter the function of an enzyme? | Raise temperature, change pH, bind allosteric effector, introduce inhibitory chemical, alter the concentration of substrate. |
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esculenta
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