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14 Cards in this Set
- Front
- Back
What is the name of the process in which a kinase activates an inactive enzyme? |
Phosphorylation |
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What does a phosphatase do to an inactive enzyme to activate it? |
It removes a phosphate atom |
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What three things control the rate of enzyme-catalysed reactions? |
Regulatory allosteric enzymes, feedback control, and covalent modifications |
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What's the name of the site where a regulator molecule binds with an allosteric enzyme? |
The allosteric site |
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What is the result of an allosteric enzyme changing the shape of an enzyme? |
The enzyme's active site is changed |
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In feedback control, how does the end product of a reaction interact with an enzyme when its levels are too high? |
The end product of a series of reactions binds to the allosteric site, stopping production of intermediate compounds of the reaction. |
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In feedback control, how does the regulator molecule react when the end product levels are too low? |
The regulator molecule dissociates from the allosteric site on the enzyme, returning it to its original condition. |
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How is enzyme activity regulated with covalent modification? |
Covalent bonds in the polypeptide chain of an enzyme are formed or broken |
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In what form/state are zymogens and proenzymes formed? |
In their inactive state |
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Zymogens include 2 enzymes and 1 type of hormone. What are they? |
Proteases (digestive enzymes that hydrolyzed protein), protein hormones, and blood clotting enzymes |
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What two places are zymogens primarily produced in? |
The blood and pancreas |
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By what process is a zymogen activated? |
Covalent modification |
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When insulin is produced in the pancreas, what is it called? |
Proinsulin |
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What interaction takes place with proinsulin's 33 amino acid polypeptide chain in order for proinsulin to become insulin? |
The chain is removed, separating the A and B chains of proinsulin. |