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Biochemistry Exam 2 > Lecture 14: Enzyme Regulation > Flashcards

Lecture 14: Enzyme Regulation Flashcards

1
Q

How are metabolic enzymes regulated?

A

compartmentalization: different locations
enzyme concentration: on/off switch
enzyme activity: volume control
hormone signals and second messengers: master regulators

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2
Q

Substrate level control acts on a _____ reaction

A

single

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3
Q

Feedback control targets a ________ in the pathway

A

different step

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4
Q

Activators ____ more products

A

promote

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5
Q

Inhibitors ____ more products

A

prevent

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6
Q

What do isozymes do?

A

catalyze the same reaction but with different efficiencies

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7
Q

What do reversible covalent modifications do?

A

add 1+ functional groups to activate/inactive the enzyme

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8
Q

What is the donor molecule in phosphorylation modification?

A

ATP

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9
Q

What is an example of a modified protein in phosphorylation modification?

A

glycogen phosphorylase

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10
Q

Protein function of phosphorylation modification

A

glucose homeostasis; energy transduction

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11
Q

Donor molecule of acetylation modification

A

acetyl CoA

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12
Q

Example of modified protein in acetylation modification

A

histones

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13
Q

protein function of acetylation modification

A

DNA packing; transcription

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14
Q

Donor molecule of myristoylation modification

A

myristoyl CoA

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15
Q

myristoylation modification example of modified protein

A

Src

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16
Q

myristoylation modification protein function

A

signal transduction

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17
Q

ADP ribosylation donor molecule

A

NAD+

18
Q

ADP ribosylation example of modified protein

A

RNA polymerase

19
Q

ADP ribosylation protein function

A

transcription

20
Q

Farnesylation modification donor molecule

A

farnesyl pyrophosphate

21
Q

Farnesylation modification example of modified protein

A

Ras

22
Q

Farnesylation modification protein function

A

signal transduction

23
Q

gamma- Carboxylation modification donor molecule

A

HCO3-

24
Q

gamma- Carboxylation modification example of modified protein

A

thrombin

25
Q

gamma- Carboxylation modification protein function

A

blood clotting

26
Q

Sulfation modification donor molecule

A

3’-phophoadenosine-5’-phophosulfate

27
Q

Sulfation modification example of modified protein

A

fibrinogen

28
Q

Sulfation modification protein function

A

blood clot formation

29
Q

ubiquitination modification donor molecule

A

ubiquitin

30
Q

ubiquitination modification example of modified protein

A

cyclin

31
Q

ubiquitination modification protein function

A

control of cell cycle

32
Q

Why is phosphorylation activating?

A
  1. thermodynamics: ATP hydrolysis can drive unfavorable reactions
  2. kinetics: physiological processes dictate reaction rate
  3. cell processes: ATP amounts dictated by metabolism (energy charge), signal transduction amplification (catalytic turnover)
  4. shape and charge complementarity: each phosphate adds (-2) charge and (3+) H-bonds
33
Q

Kinases _____ phosphates

A

ADD

34
Q

phosphatase ____ phosphates

A

REMOVE

35
Q

Allosteric binding does or does not occur at the active site?

A

does not

36
Q

Heteroallostery definition

A

effector binds at the allosteric site

37
Q

Homoallostery definiton

A

cooperatively

38
Q

Binding of CTP to ACTase prefers what site?

A

T/inactive site

39
Q

Binding of ATP prefers to ACTase prefers what site?

A

R/active site

40
Q

histone acetylation ______ transcription

A

promotes

41
Q

histone phosphorylation _____ transcription

A

prevents

42
Q

Histone methylation does what for transcription?

A

promotes or prevents

Biochemistry Exam 2 (12 decks)

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