Ch. 7 Flashcards

1
Q

How are enzyme rates modified (2 methods)?

A
  1. Noncovalent binding of pathway intermediates to stimulate or inhibit
    enzyme activity
  2. Covalent modification by attachment of chemical groups
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2
Q

What are the 3 common patterns of regulation?

A
  1. Feedback inhibition
  2. Positive regulation
  3. Irreversible reactions
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3
Q

For biosynthetic pathways, the _____ is usually a negative allosteric effector for a branch point enzyme.

A

end product

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4
Q

How does feedback inhibition work?

A

Acts to maintain a steady state in which the end product is utilized as rapidly at it is synthesized

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5
Q

What are the 3 patterns of feedback inhibition?

A
  1. Simple
  2. Cumulative
  3. Concerted
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6
Q

What is simple feedback inhibition? In what type of biosynthetic pathway is it encountered?

A
  • Regulation by a single end-product
  • Encountered in linear biosynthetic pathways and sometimes branched biosynthetic pathways
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7
Q

What is concerted inhibition?

A

Both end products must bind to the regulatory enzyme simultaneously to achieve any inhibition

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8
Q

What is cumulative inhibition?

A

The enzyme is not completely inhibited by any single end product

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9
Q

Is cumulative inhibition additive? Explain.

A

Cumulative but not additive
- One end product might inhibit the enzyme by 25% and a second might inhibit the enzyme by 45% –> both together might inhibit the enzyme 60% (not 70%)

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10
Q

Why is it important that a single end product not shut down a common enzyme of a branch point?

A

Because shutting down a common enzyme of a branch point would prevent the synthesis of all end products

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11
Q

When would branched pathways be regulated by simple feedback inhibition?

A

When a reaction shared by the various branches uses enzymes that have the same catalytic sites but different effector sites (isoenzymes)
- Isoenzymes catalyze the same reaction but are responsive to different end products

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12
Q

What is positive regulation?

A

Regulation by an intermediate in a second pathway (GKL-2)
- One pathway produces an intermediate (G) –> combines with K in a second pathway –> produce L

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13
Q

What happens in “precursor activation” (another pattern of positive regulation)?

A

Precursor intermediate stimulates a regulatory enzyme “downstream” in the same pathway
- Ensures that the rate of the downstream reactions matches that of the upstream reactions

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14
Q

What are the 2 generalizations regarding irreversible reactions at branch points?

A
  1. The reactions catalyzed by regulatory enzymes are usually at metabolic branch points
  2. Regulatory enzymes often catalyze reactions that are physiologically irreversible
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15
Q

What happens when the effector binds to the allosteric site?

A

The protein undergoes a conformational change, and this changes its kinetic constants

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16
Q

What are most regulatory enzymes regulated by?

A

Conformational changes

17
Q

What does multimeric mean?

A

Having multiple subunits

18
Q

What do multimeric regulatory enzymes consist of? What does each component do?

A
  1. Regulatory subunit
    - Bind effectors –> conformational change –> inhibit or activate catalytic subunit
  2. One or more catalytic subunits
    - Bear the active sites and bind the substrate
19
Q

How does covalent modification occur?

A

By the reversible attachment of chemical groups to activate or inhibit the protein

20
Q

What groups can be added in covalent modification?

A
  • Acetyl groups
  • Phosphate groups
  • Methyl groups
  • Adenyl groups
  • Uridyl groups