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14 Cards in this Set

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  • Back

What is the name of the process in which a kinase activates an inactive enzyme?

Phosphorylation

What does a phosphatase do to an inactive enzyme to activate it?

It removes a phosphate atom

What three things control the rate of enzyme-catalysed reactions?

Regulatory allosteric enzymes, feedback control, and covalent modifications

What's the name of the site where a regulator molecule binds with an allosteric enzyme?

The allosteric site

What is the result of an allosteric enzyme changing the shape of an enzyme?

The enzyme's active site is changed

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.

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.

How is enzyme activity regulated with covalent modification?

Covalent bonds in the polypeptide chain of an enzyme are formed or broken

In what form/state are zymogens and proenzymes formed?

In their inactive state

Zymogens include 2 enzymes and 1 type of hormone. What are they?

Proteases (digestive enzymes that hydrolyzed protein), protein hormones, and blood clotting enzymes

What two places are zymogens primarily produced in?

The blood and pancreas

By what process is a zymogen activated?

Covalent modification

When insulin is produced in the pancreas, what is it called?

Proinsulin

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.