Module 6 - 1 Flashcards

1
Q

What is the function of catalysts?

A

Lower energy required for reaction.

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2
Q

What is the difference between enzymes and chemical catalysts in terms of speed?

A

Enzymes are faster.

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3
Q

What are the conditions required for chemical catalysts?

A

Extreme temperature, pressure, and pH.

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4
Q

What is the specificity of enzymes compared to chemical catalysts?

A

Higher degree of specificity.

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5
Q

What is the Circe effect?

A

Enzyme rates of catalysis can approach the physical limit of rates of diffusion of molecules in solution.

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6
Q

What is the equilibrium equation for enzymes?

A

E + S <—->ES <—–> E + P.

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7
Q

What is the substrate?

A

The molecule acted upon by the enzyme.

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8
Q
A

The molecule produced by the enzyme.

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9
Q

What is the active site?

A

The portion of enzyme responsible for binding the substrate to formation of an enzyme-substrate complex.

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10
Q
A

Catalyze the interconversion of substrate and product.

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11
Q
A

Enzymes don’t rely on harsh conditions.

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12
Q

What is the specificity of catabolism?

A

Isn’t as specific.

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13
Q

What is the regulation of enzymes?

A

Responsive to the dynamic needs of the cell and organism.

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14
Q

What is the rate-determining step?

A

Roughly as fast as the binding of substrates to the enzymes.

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15
Q

What is the stereospecificity of enzymes?

A

Higher degree of specificity.

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16
Q

What is the function of the ES complex?

A

Catalyze the interconversion of substrate and product.

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17
Q

What is the 3D cleft?

A

The active site formed from different parts of the polypeptide chain.

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18
Q

What is the function of the active site?

A

Responsible for binding the substrate to formation of an enzyme-substrate complex.

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19
Q

What is the function of enzymes in terms of rate enhancements?

A

Offer incredible catalytic power.

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20
Q

What is an active site?

A

Small part of enzyme where substrate binds

21
Q
A

Unique microenvironments

22
Q

How are substrates bound to enzymes?

A

Multiple weak interactions

23
Q

What determines specificity of substrate binding?

A

Precisely defined arrangement of atoms

24
Q
A

Substrate binding causing flexibility in enzymes

25
Q

What is the lock and key model?

A

Model of enzyme-substrate interaction without conformation changes

26
Q

What is the hand in glove model?

A

Better model of enzyme-substrate interaction with conformation changes

27
Q

When is a reaction spontaneous?

A

When ΔG is negative

28
Q

What does spontaneous mean?

A

Reaction proceeds without input of energy and releases energy (exergonic)

29
Q

When can a reaction not take place spontaneously?

A

When ΔG is positive, input of free energy is required (endergonic)

30
Q

What happens at equilibrium?

A

No net change in concentrations of products and reactants, ΔG is zero

31
Q

What does ΔG of a reaction depend on?

A

Free energy of product minus free energy of reactants, independent of transformation steps

32
Q

What information does ΔG provide about reaction rate?

A

None, only indicates if reaction can take place spontaneously

33
Q

What is activation energy?

A

ΔG‡ between S and P determining rate at which equilibrium is reached

34
Q

How do enzymes lower activation energy?

A

Provide alternate, lower-energy pathway between substrate and product

35
Q

What is the relationship between reaction rate and activation energy?

A

Inverse and exponential

36
Q

What determines equilibrium of a reaction?

A

Difference in free energy between S and P

37
Q

Do enzymes influence the equilibrium of a reaction?

A

No, they do not influence the difference in free energy between S and P

38
Q

What is the role of enzymes in a reaction?

A

Lower activation energy and increase reaction rate.

39
Q

Do enzymes affect the equilibrium of a reaction?

A

No.

40
Q

What are the two modes of enzyme catalysis?

A

Chemical and binding effects.

41
Q

What are the forces that lower the activation energy?

A

Chemical and binding effects.

42
Q

What are the two binding effects of enzymes?

A

Substrate binding and transition-state stabilization.

43
Q

What is the role of substrate binding in enzyme catalysis?

A

Provides specificity and catalytic power.

44
Q

How much can catalytic mechanisms limited to binding properties increase reaction rates?

A

Over 10,000-fold.

45
Q

What is the conceptual overlap between substrate binding and transition-state stabilization?

A

They both involve the active site of the enzyme.

46
Q

What are the five ways substrate binding promotes reactions?

A

Reducing entropy, alignment of functional groups, desolvation of substrate, distortion of substrates, and induced fit.

47
Q

What are the four reasons enzymes are better than chemical catalysts?

A

Their speed, conditions, specificity, and regulation

48
Q

What conditions do enzymes function under

A

They function under physiological conditions

49
Q

Explain the regulation of enzymes

A

They are responsive to the dynamic needs of cell and Organism