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Created by Emma Allde
over 9 years ago
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| Question | Answer |
| Oxidoreductases | add O2 or remove 2H |
| Lactase dehydrogenase is what kind of enzyme | oxidoreductase |
| Transferases | transfer of function groups from donors to acceptors a way of producing non-essential amino acids and moving around carbon skeletons and nitrogen |
| Hydrolases | hydrolytic reactions |
| Trypsin is what kind of enzyme | hydrolase |
| Isomerases | isomerisation reactions catalyse the transfer of functional groups within the same molecule |
| Ligases | form C-C or C-N-bonds with ATP cleavage to catalyse the formation of new covalent bonds the loss of a phosphate group (going one way) |
| Alcohol dehydrogenase is what kind of enzyme | oxidoreductase E.C. 1.1.1.1 |
| What do enzyme active sites contain that stabile the reaction | functional groups |
| Lock and Key hypothesis | the first enzyme model not perfect Enzyme has two substrates that it tries to bring together to interact |
| Induced Fit Model | Unfilled binding site suggests that the enzyme alters the shape of a substrate to make it more suitable for a reaction |
| Where does pepsin work + at what pH is it most effective | Enzyme in the stomach; most effective around pH of 2 |
| Where does trypsin work + at what pH is it most effective | Enzyme in the digestive system (intestines); most effective around pH of 6 |
| Where does alkaline phosphate work + at what pH is it most effective | Enzyme in the bloodstream; most effective around pH of 8 |
| What are isoenzymes | Enzymes with different protein structures which catalyse the same reaction Found in different cellular compartments (cytoplasm or mitochondria) because they have different biochemical roles |
| Are isoenzymes coded for by different enzymes | yes |
| Hexokinase/ glycokinase are examples of what | isoenzymes |
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