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Bio 540 - Biochem > Exam 2 - Enzyme Activity > Flashcards

Exam 2 - Enzyme Activity Flashcards

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1
Q

Is the active site and the substrate binding site the same?

A

No

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2
Q

What type of inhibition can be reversed by adding substrate?

A

Competitive Inhibition

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3
Q

What are the 3 types of reversible inhibitors?

A
  1. Competitive
  2. Uncompetitive
  3. Mixed
    1. Noncompetitive
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4
Q

Competitive inhibitors compete with the substrate for the [] ?

A

Substrate binding site

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5
Q
A
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6
Q

What rate constant is unchanged in competitive inhibition?

A

k3

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7
Q

What are the 2 conditions for a noncompetitive inhibitor?

A
  1. kI and kI’ have to be identical
  2. The Enzyme-substrate-inhibitor cannot make product
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8
Q

In noncompetitive inhibition why is the Km lowered?

A
  • Psyche
  • The Km is unchanged in noncompetitive inhibition
  • the Vmax is lowered
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9
Q

In mixed inhibition, KI and Ki’ are [] identical…

A

NOT identical

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10
Q

What happens to Km and Vmax with the following types of inhibition?

  1. Competitive
  2. Mixed
  3. Noncompetitive
  4. Uncompetitive
A
  1. Vmax is unchanged, Km can change
  2. Vmax is lowered, Km can go up or down
  3. Vmax is lowered, Km is unchanged
  4. Km is lowered, Vmax is lowered
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11
Q

Uncompetitive inhibitors bind to the [] complex only, but does not bind to the [] [] [] ….

A

ES

Substrate Binding Site

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12
Q

What is the difference between the active site and the substrate binding site?

A
  • Substrate binding site is the site to where the whole substrate binds to
  • Acive site are the specific catalytic residues within the substrate binding site.
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13
Q

Allosteric Regulation

  • Describes molecules that bind to proteins at some location [] than the substrate binding site - also called the [] site
  • Changes [] - positively or negatively
  • Targeting []
  • Normally small molecules < []
A
  • Other, Allosteric Site
  • velocity
  • Km
  • 3,000 Dal
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14
Q

A compound that alters enzyme activity by binding to sites outside of the substrate binding or active sites…

A

effector

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15
Q

What is any molecule that is bound to a macromolecule?

A

Ligand

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16
Q

What is a protomer?

A
  • single subunit in an oligomer
  • Usually identical polypeptides
17
Q

Enzymes that undergo [] regulation tend to be control points in metabolic pathways, or the [] [] []?

A
  1. allosteric
  2. Rate limiting step
18
Q

Enzymes subjected to allosteric regulation contain an additional binding site called the [] site…

A

allosteric

19
Q

Homotrophic Interactions involve what?

Are these interactions negative or positive?

A
  • the binding of 1 ligand to protomers affects binding of ligands on other protomers within the same oligomer
  • Usually positive interactions
20
Q

What type of activity curve to allosteric enzyes have?

A

altered sigmoidal curve

21
Q

Heterotrophic interactions involve what?

Are these interactions positive or negative?

A
  • Binding of one ligand affects the binding of a different ligand
  • Response can be positive or negative
22
Q

Protein Kinase A is an example of [] regulation

A

allosteric

23
Q

What enzyme degrades cAMP?

A

cAMP phosphodiesterase

24
Q

How is a protein kinase activated?

A
  • cAMP interacts with a repressing R group on the catalytic subunit of the protein kinase
  • therefore activating the protein kinase.
25
Q

Does cAMP and interact with Protein Kinase A?

A
  • Technically no - it effects the r-group negatively and removes it
26
Q

The first step that is distinct to a biochemical pathway…usually the first irreversible step?

A

The First Committed Step

27
Q

The reaction within a metabolic pathway that has the highest enery barrier, the slowest reaction…

A

The Rate Limiting Step

28
Q

What are the 6 mechanism by which enzymes increase the rates of reaction (or decrease the energy of activation)?

A
  1. Acid-Base Catalysis
  2. Substrate Strain
  3. Covalent Catalysis
  4. Transition State Stabilization
  5. Entropy effect
  6. Ground State destabilization

Bio 540 - Biochem (14 decks)

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