Chapter 6b Flashcards

Enzymes

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1
Q

Small amount of energy input required in order for chemical reactions to occur

A

Activation energy

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2
Q

Substance that helps a chemical reaction to occur

A

Catalyst

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3
Q

special molecules that catalyze biochemical reactions

A

enzyme

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4
Q

Chemical reactants to which an enzyme binds

A

Substrate

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5
Q

Alteration of the natural properties on an enzyme and render it weak or ineffective

A

Denaturation

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6
Q

Inorganic helper ions such as iron or magnesium

A

Cofactor

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7
Q

Organic helper molecules such as Vitamin C

A

Coenzyme

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8
Q

What factors determine the rate of an enzymatic reaction?

A

Activation energy typically through heat energy

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9
Q

Does a higher activation energy result in a faster or slower reaction rate?

A

Higher the activation energy, the slower the reaction will be

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10
Q

What is the source of activation energy for most chemical reactions?

A

Heat energy

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11
Q

Why does increased temperature increase the rates of reaction?

A

Heat speeds up the motion of molecules, causing them to collide with more force, and more often

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12
Q

Cellular reactions cannot use heat energy from their surroundings as activation energy. Why not?

A

The activation energies for most cellular reactions are too high for heat energy from the surroundings to overcome

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13
Q

How does an enzyme catalyze a reaction? How does it lower the activation energy?

A

They lower the activation energy by binding to the reactant molecules and holding them in such a way as to make the chemical bond-breaking and bond-forming process easier

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14
Q

What is the “active site” and what properties give it it’s specificity?

A

The place on the enzyme where the substrate binds; there is a unique combination of R-groups present at an enzyme’s active site

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15
Q

What are some benefits and some drawbacks of having a high level of specificity?

A

It is vulnerable to environmental influences that alter it’s structure but it is for a specific chemical reaction

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16
Q

Name some environmental changes that might denature an enzyme.

A

Temperature, pH

17
Q

What is the “lock and key” model?

A

The idea that the enzyme active site and substrate fit together perfectly in one step

18
Q

How does the lock and key model differ from the “induced fit” model?

A

In the induced fit, the enzyme and substrate are specific to each other, but also undergo changes in their conformation upon binding

19
Q

What happens to enzymes once they have catalyzed a reaction?

A

It will always return to its original state at the completion of the reaction

20
Q

What is competitive inhibition? How does it help regulate enzyme activity and therefore chemical reaction rate?

A

An inhibitor molecule is similar enough to the substrate that it can bind to the active site and block the substrate from binding; the inhibitor molecule competes with the substrate for active site binding

21
Q

What is non-competitive inhibition? How does it differ from competitive inhibition?

A

An inhibitor molecule binds to the enzyme in a location other than the active site; activity of the enzyme is greatly reduced

22
Q

What is allosteric inhibition? How does it help regulate enzyme activity?

A

An inhibitor molecule binds to the enzyme in a location other than the active site, resulting in reduced affinity of the enzyme for its substrate; cause slight conformational changes at the active site so substrate bind less efficiently

23
Q

How does allosteric inhibition differ from allosteric activation?

A

Inhibition makes the substrate bind less efficiently and activation makes the substrate bind more efficiently

24
Q

What is the purpose of cofactors and coenzymes? How are they similar? How are they different?

A

Several enzymes don’t work well, or at all, unless they are also bound by specific non-protein helper molecules; cofactors are inorganic and coenzymes are organic

25
Q

How do cofactors and coenzymes assist in the regulation of enzymatic reactions?

A

Several enzymes don’t work well, or at all, unless they are also bound by specific non-protein helper molecules

26
Q

Give an example of “compartmentalization” of enzymes. How is this used by eukaryotic cells to regulate chemical reactions?

A

Metabolic enzymes in the mitochondria; or digestive enzymes in lysosomes; enzymes required only for certain cellular processes can be housed separately inside structures along with their substrates

27
Q

Give an example of compartmentalization of enzymes.

A

Metabolic enzymes in the mitochondria; or digestive enzymes in lysosomes

28
Q

What is “feedback inhibition?” Give examples of feedback inhibition in cellular respiration.

A

The use of a reaction product to regulate its own further production; the cellular production of amino acids and nucleotides