Ch. 4 Enzymes and Energy Flashcards

1
Q

What are enzymes?

A

Class of proteins that serve as biological catalysts

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2
Q

What is the enzyme exception?

A

Ribozymes are made of RNA

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3
Q

What do enzymes do?

A

Increase rate of reaction
Not changed by reaction (can be used again)
Do not change nature of reaction - reaction could have occurred w/o enzyme, just much slower
Lowers activation energy of reaction

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4
Q

What is activation energy?

A

Energy required for reactants to engage in a reaction

–a barrier we have to overcome

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5
Q

Most molecules ____ the activation energy for a reaction.

A

Lack

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6
Q

Adding ____ increases the likelihood of a reaction occurring.

A

Heat

–increases rate of reaction, yet has some negative effects on cells.

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7
Q

____ help the reaction occur at lower temperatures.

A

Catalysts

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8
Q

Why do we have enzymes?

A

Because heat isn’t a great option in physiology to speed up a reaction

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9
Q

The function of an enzyme is dictated by its ____.

A

Structure

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10
Q

Describe the shape of enzymes.

A

Characteristic 3D shape or conformation, has pockets that serve as active sites in the enzyme

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11
Q

Enzyme reactants are called ____.

A

Substrates

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12
Q

Lock-and-key model

A

Substrates fit into the active site like a key to a lock

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13
Q

Induced-fit model

A

The initial fit is not always exact, but will change as the substrate moves into the active site

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14
Q

All enzymes end with the suffix ____.

A

-ase

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15
Q

Phosphatase?

A

Remove phosphate groups

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16
Q

Synthetase and Synthase?

A

Catalyze dehydration synthesis

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17
Q

Hydrolase?

A

Promote hydrolysis

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18
Q

Dehydrogenase?

A

Removes hydrogen atoms

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19
Q

Kinase?

A

Add phosphate groups

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20
Q

Isomerase?

A

Rearrange the atoms

21
Q

Does an enzyme that does the same job in two different organs have the same name?

A

Yes

–names are given to enzymes based on function

22
Q

What are isoenzymes?

A

Molecules that may be slightly different (in areas outside the active site)

23
Q

How is enzyme activity measured?

A

By the rate at which substrate is converted to product

24
Q

What influences enzyme activity?

A
  • Temperature (heat makes reaction occur faster)
  • pH (different enzymes activate at different pH levels)
  • Cofactors and coenzymes
  • Enzyme activation
  • Substrate concentration (adding more substrate = reaction occurs faster)
  • Possible stimulatory or inhibitory effects of products on enzyme function
25
Q

Most enzymes work really well at what temperature?

A

37ºC (our core body temperature)

26
Q

Enzymes exhibit peak activity within a ____ pH range.

A

Narrow

27
Q

pH changes will result in what?

A

Enzyme conformational changes

28
Q

True or False: Optimum pH reflects the pH of the fluid the enzyme is found in.

A

True

29
Q

What are coenzymes?

A

Organic molecules derived from water-soluble vitamins

Larger molecules, many enzymes require these to function properly

30
Q

What do coenzymes transport?

A

Hydrogen atoms and other small molecules between enzymes

31
Q

What are cofactors?

A

Help form the active site through a conformational change of the enzyme or help in enzyme-substrate binding.

Much smaller than coenzymes

32
Q

What types of ions are cofactors?

A

Metal ions such as Ca2+, Mg2+, Mn2+, Cu2+, Zn2+

33
Q

Can cofactors bind at different sites?

A

Yes

34
Q

What is zymogen?

A

Enzymes, particularly of the digestive system, are often produced in an inactive form called a Zymogen that is activated when needed

Make enzymes, store them, release when needed
–ex: pepsinogen –> pepsin

35
Q

Enzyme inhibition can be controlled through what?

A

Turnover, by which enzymes are degraded

36
Q

Enzyme activation often requires ____ ____ to phosphorylate or dephosphorylate the molecule.

A

Additional enzymes

37
Q

As the substrate concentration ____, so will the rate of the reaction until the enzyme becomes ____.

A

Increases; saturated

38
Q

What is meant by saturated?

A

Every enzyme in the solution is being used

39
Q

Will adding more substrate (in already saturated enzymes) increase the rate of the reaction?

A

No, if it’s saturated (all enzymes are being used), the reaction can’t increase

40
Q

Reversible Reactions

A

Sometimes a single enzyme can drive a reaction in two directions, depending on the concentration of substrate/product

When one side gets higher, the other reaction reverses; the law of mass action
–wants to be in equilibrium

41
Q

What are metabolic pathways?

A

Reactions linked together in a chain (or web)
–begin with an initial substrate and end with a final product, with many enzymatic steps along the way

Coupling a bunch of reactions together = metabolic pathway

42
Q

Are few metabolic pathways branched or linear?

A

Few are linear

Most include branches where several products can be produced

43
Q

End product inhibition

A

Branch points are often inhibited by a form of negative feedback in which one of the final products inhibits the branch point enzyme

44
Q

Allosteric Inhibition

A

The product binds to the enzyme at a location away from the active site and changes the 3D conformation of the enzyme
–influencing activity, but influencing it away from the active site (still gives us structural changes)

45
Q

End product in inhibition keeps the final product from ____.

A

Accumulating

46
Q

Endergonic Reactions

A

Chemical reactions that require an input of energy

Products contain more free energy than the reactants (trap some energy in products)

ex: glucose –> glycogen (synthesis reaction)…stored energy in our cells

47
Q

Exergonic Reactions

A

Releasing energy

Chemical reactions that produce energy. Products will have less free energy than the reactants.

Energy is used to make ATP for use in other endergonic reactions in the body.

ex: breaking glucose down into CO2 and water produces energy

48
Q

Coupled Reactions

A

Energy from the environment (food) is broken down in exergonic reactions to drive the endergonic reactions in our bodies.

Energy must be stored in a usable form, ATP

Use exergonic reactions to drive endergonic reactions