ENZYME INHIBITION AND REGULATION Flashcards

1
Q

a non-prescription drug irreversibly inhibits prostaglandins and thromboxane synthesis by inhibiting cyclooxygenase

A

ASPIRIN

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2
Q

the inactive precursor of a proteolytic enzyme

A

zymogen or proenzyme

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3
Q

Any substance that can diminish the velocity of an enzyme-catalyzed reaction

A

inhibitor

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4
Q

regulated by molecules called effectors (also called modifiers) that bind noncovalently at a site other than the active site

A

Allosteric enzymes

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5
Q

inhibitors bind to enzymes through covalent bonds

A

irreversible inhibitors

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6
Q

Effectors that inhibit enzyme activity

A

negative effectors

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7
Q

inhibitors typically bind to enzymes through noncovalent bonds, thus dilution of the enzyme–inhibitor complex results in dissociation of the reversibly bound inhibitor

A

Reversible inhibitors

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8
Q

those that increase enzyme activity

A

positive effectors

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8
Q

two most commonly encountered types of reversible inhibition

A

competitive
noncompetitive

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9
Q

catalyzed by a family of enzymes called protein kinases that use adenosine triphosphate (ATP) as a phosphate donor

A

Phosphorylation

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10
Q

This type of inhibition occurs when the inhibitor binds reversibly to the same site that the substrate would normally occupy and, therefore, competes with the substrate for that site

A

Competitive inhibition

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11
Q

Phosphorylation reactions are catalyzed by a family of enzymes called

A

protein kinases

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12
Q

an example of competitive inhibitor

A

STATIN DRUGS

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13
Q

TRUE / FALSE:
Enzymes subject to regulation of synthesis are often those that are needed at only one stage of development or under selected physiologic conditions

A

TRUE

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14
Q

structural analogs of the natural substrate for this enzyme, and compete effectively to inhibit HMG-CoA reductase

A

STATIN DRUGS

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15
Q

regulating cellular enzyme activity based on the production of enzymes in an inactive form

A

Proteolytic enzyme and zymogen

15
Q

This type of inhibition is recognized by its characteristic effect on Vmax

A

Noncompetitive inhibition

16
Q

generated in an inactive form and then later, when they are needed, are converted to their active form

A

proteolytic enzymes

17
Q

occurs when the inhibitor and substrate bind at different sites on the enzyme

A

Noncompetitive inhibition

18
Q

an enzyme that catalyzes the breaking of peptide bonds that maintain the primary structure of a protein

A

proteolytic enzyme

19
Q

a molecule that inactivates enzymes by forming a strong covalent bond to an amino acid side-chain group at the enzyme’s active site

A

irreversible enzyme inhibitor