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Enzymes
| Question | Answer |
|---|---|
| Enzymes | "biological catalysts" that function to increase the rate of chemical reactions in the body. Most are proteins (amino acid chains) that have a very specific shape due to hydrogen bonds. |
| the enzyme is only the CATALYST for the reaction, making it faster, but does NOT change the reaction itself. List three things it does NOT change..? | 1) It is not itself changed at the end of a reaction (only the substrate is changed) 2)Does not change the nature of the reaction. (EX: it doesn't change the fundamental breaking down of the sugar, just accelerates it 3)Does not change the final result |
| "Lock and Key" | Enzymes have a very specific shape due to hydrogen bonding. Just like a key in a lock, only a specific substrate (i.e. sucrose) will "fit" in the enzyme sucrase's active site. Thus enzymes only work with their own particular substance. |
| What do enzymes look like? draw one | Just draw a random squiggle, and include the active site as a little 1/2 triangle |
| What four things control enzyme activity? Just list them. | 1)Temperature 2)pH 3) concentration of cofactors and coenzymes 4)concentration of enzyme and substrate |
| How does temperature control enzyme activity | If the temperature is too hot, the enzyme protein will be denatured (its protein structure will be altered). EX: cooking an egg white breaks the proteins bonds so it is not folded up w hydrogen bonds anymore. |
| How does pH control enzyme activity? | Each enzyme is most effective in a certain pH, depending on where in the body it does its work. EX: Pepsin, enzyme in stomach, is most efficient in pH of 1-2 while Trypsin, in the small intestine, works better in a more alkaline pH of 8. |
| Where is Pepsin located, in what pH does it most efficiently work and what happens when it reaches the small intestine? | Pepsin is an enzyme in the stomach that works best in a pH of 1-2. It stops working when it reaches the small intestine because pH of 8 is too alkaline, but it is simply digested since after all it is just a protein. |
| what is a Cofactor? (give some examples). What is the more important cofactor in the human body? | Cofactor is an inorganic, non-protein component needed for enzyme function. It is an enzyme "helper". EX: iron, copper, calcium, zinc, magnesium: Mg is needed by 300 different enzymes). Sometimes an enzyme has a special cofactor site. |
| What is a coenzyme? give an example | an organic molecule (derived from water soluble vitamins) that is needed for enzyme function. EX: vitamin B |
| How does the concentration of enzyme and substrate control enzyme activity? | Enzyme activity is most efficient when there are equal concentrations of enzyme and substrate. (EX: If there is a ton of sucrose and only a couple sucrase enzymes, it would go very slowly.) |
| Enzyme Pathways: be familiar with drawing a pathway and how the elimination of a certain enzyme (i.e. "e56") would change the outcome of the reaction | EX: SUBA-->SUB B--> SUB C etc, you can branch off each substrate but make sure you have a different enzyme over each arrow (e4 e6 etc.) If she says a certain enzyme is "missing" then cross off the arrow, meaning all substrates after that arrow won't exist |
| Talk about the disease PKU. What is it and what enzyme is missing? | phenylketonuria is a disease in which a person is missing the enzyme phenylalanine hydroxylase (which converts phenylalanine to tyrosine). There will b a buildup of phenylalanine, a neurotoxin that causes mental retardation. |
| How can PKU be detected and what is done to counteract its effects if caught early enough? | PKU can be detected by blood or urine test 12 hours after birth. If detected then parents are instructed to feed the baby a diet low in phenylalanine |
Created by:
kalmetina
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