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Enzymes
| Question | Answer |
|---|---|
| What is a cofactor? | Any substance that is essential for an enzymes reaction. |
| What is a coenzyme? | An organic cofactor |
| What is a prosthetic group? | A cofactor that is tightly bound to th enzyme molecule |
| What is a the name for a molecule that reduces the rate of an enzyme controlled reaction by bindingto the allosteric site? | Non-competitive inhibitor |
| Why can the substrate fit into an enzymes active site? | The shape of the active site is complementary to the substrate |
| What type of molecule is an enzyme? | Globular protein |
| What is formed when a reaction has occured but the products from a reaction are still bound to the enzyme? | Enzyme-product complex |
| What term describes a non-protein molecule that binds strongly to an enzyme to make it functional? | Prosthetic group |
| What term describes a non-protein molecule that binds loosely to an enzyme in order to make it functional? | Cofactor |
| What enzymes catalyse reactions inside cells? | Intracelluar |
| What enzymes catalyse reactions inside cells? | Extracellular |
| What phrase describes enzymes because they are molecules that speed up the rate of metabolic reactions but remain unchanged by the reactions | Biological catalyst |
| Where does the competitive inhinitor bind | The active site |
| What phrase describes the way in which cells regulate production of a molecule by using that molecule by using that molecule to inhibit one of the enzymes? | End-product inhibition? |
| What is the name given to an enzyme where a non-competitive inhibitor binds? | Allosteric site |
| Which enzyme hydrolyses proteins into short polypeptides? | Trypsin |
| What word is used to describe the fact that enzymes will catalyse che reaction but not others? | specific |
| What is the term used to describe when the enzyme concentration limits the rate of reaction because all other factors are at optimum. | Vmax |
| What is the name of the hypothesis of enzyme action that describes the enzymes active site as "nearly a complementary shape" to the substrates, so the active site changes shape to make it complementary, before returning to its original shape. | Induced fit |
| Which enzyme hydrolyses starch into maltose? | Amylase |
| What term describes an inactive precursor enzyme that can be activated by the addition of a cofactor? | Apoenzyme |
| Which hypothesis of enzyme actihe site is an exactly complementary shape to the substrates and remains that shape unchanged throughout the reaction | Lock and key |
| What term is given to the rate of reaction at 10⁰C higher than the original temperature divided by the rate of reaction at the original temperature? | Q10 |
Created by:
Golbs_Helmet