| Question |
Answer |
| Prosthetic group | Coenzyme or metal ion that is tightly bound |
| Holoenzyme | enzyme plus prosthetic group |
| Apoenzyme/apoprotein | Enzyme without cofactor/coenzyme |
| Catalyses reactions by | Degrading nutrients, conserving and transforming chemical energy and making biological macromolecules from simple building blocks |
| Active site | A pocket within the enzyme which provides desirable environment in order to catalyse reactions |
| What's special about the active site? | The surface of the active site is lined with amino acids with side groups that bind the substrate and participate in the chemical catalysis |
| What do enzymes do to the equilibrium of a reaction? | They don't change the equilibrium |
| Enzyme kinetics | How the rate of an enzyme-catalysed reaction changes in response to experimental parameters |
| How does the enzyme become saturated? | With increasing amounts of substrate, more and more enzyme is bound by substrate and eventually the enzyme becomes saturated (all molecules are in ES form). Adding more substrate will not speed up the rate of reaction. |
| State the Michaelis-Menton Equation | V0= Vmax[S] / Km+[S] |
| How is enzyme activity regulated? | Via allosteric regulators that cause a change in the 3D structure of the enzyme thereby increasing or decreasing the activity of the enzyme regulating flux through a metabolic pathway |
| Km | substrate concentration required to achieve half-maximal activity; low Km= substrate bound tightly to enzyme |
| Vmax | rate of reaction of maximum velocity |
| How is Vmax and Km affected by competitive inhibition? | Vmax is unaffected but Km is increased |
| How is Vmax and Km affected by uncompetitive inhibition | Vmax is decreased but Km is decreased |
| How is Vmax and Km affected by non-competitive inhibition | Km is unaffected but Vmax is decreased |
Beef Production
