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17 Cards in this Set
- Front
- Back
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Anabolic reaction |
Maintaining and building large organisms by synthesising large polymers, cells, tissues and organs |
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Catabolic reaction |
Breaking down organic molecules to release energy |
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Induced fit hypothesis |
Initial interaction between substrate and enzyme is weak Weak interaction induce change in tertiary structure of enzyme that strengthens binding Shape of active site change to fit more precisely around the substrate called conformation Change in shape of active site put strains on substrate making reaction occur more easily |
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Competitive inhibitor |
Has similar structure with substrate of enzyme Competes with substrate to bind to active site and prevent substrate from binding No enzyme substrate complex form so enzyme is inhibited |
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Non competitive inhibitor |
Bind to enzyme at different location other than active site called allosteric site Causes tertiary structure to change so active site change shape Active site no longer complementary to substrate so cannot form enzyme substrate complex Increasing concentration of substrate has no effect on rate |
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Cofactor features and function |
Non protein helper assisting enzyme with function Temporarily bind to enzyme Activate enzyme Transfer atoms or molecules from one reaction to another in multi step pathway Part of active site |
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Inorganic cofactor Example |
Get via diet Amylase - chloride ions for formation of correct shape active site |
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Coenzyme Example |
Organic cofactors get via diet from vitamins NAD - from vitamin B3 , transfer H+ ions between molecules in respiration Coenzyme A - from vitamin B5, breaks down fatty acid and carbohydrates in respiration |
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Prosthetic group Example |
Permanently and tightly bond to enzyme Zinc to carbonic anhydrase for metabolism of CO2 |
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Why are enzymes release in inactive form and wht are they called? |
To prevent damage to tissues or cells Apoenzymes, inactive precursor enzyme |
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What is it called after being activated by cofactor? How is it activated? |
Haloenzyme, precursor enzyme Changing active site |
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Others ways to activate enzyme |
Change in tertiary structure occur by action of another enzyme eg. Protease break bond in enzyme Change of pH or Temperature- called zymogens, proenzymes |
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Example of zymogen |
Inactive pepsinogen into active pepsin after getting released into stomach with low pH |
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Turnover rate |
Number of substrate molecules turned into product per minute |
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Enzyme action |
Molecules move and collide randomly For successful collisions, collide with right force and orientation Enzymes help molecules to collide more successfully and lower activation energy |
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Lock and key hypothesis |
Area witching tertiary structure has complementary active site to substrate Substrate bind to active site to form enzyme substrate complex React and form enzyme product complex and product leave site Substrate held by enzyme in particular way so right atom groups are close enough to react. Temporary bonds between active site and substrate weaken bonds within substrates helping reaction happens quicker |
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Feedback or End of product inhibition |
Product formed later in reaction chain non competitively inhibit enzyme occur earlier in reaction |
