Enzymes Flashcards

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0
Q

Active site

A

Binding site of an enzyme

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1
Q

Vmax

A

The point at which the enzymes are completely saturated

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2
Q

How do enzymes differ

A

By enantiomers

  • if its substrate is chiral
  • specicifity is huge
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3
Q

High Km

A

Lower affinity for substrate

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4
Q

Low Km

A

Higher sffinity for substrate

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5
Q

Half way to Vmax

A

Km

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6
Q

Competitive inhibition

A
  • when an inhibitor competes with the active site of a protein
  • does not change Vmax
  • imcreases the Km value (less affinity for substrate)
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7
Q

Noncompetitive inhibition

A
  • does not bind to the active site
  • catalytic reaction doesnt take place
  • Vmax goes down but Km remains unchanged
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8
Q

Hemoglobin

A
  • has four subunits that can bind oxygen
  • has *cooperativity
  • when the first subunit binds o2 is makes it easier for the second, then third and fourth
  • myoglobin only has a single subunit
  • in the tissues theres more co2 and acid which releases the o2 (bohr effect)
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9
Q

Bohr effect

A
  • at the tissues were more likely to let the oxygen go

- curve shifts

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10
Q

Enzyme regulation

A
  • need a way to turn them on and off
    1. Allosteric regulation
    2. Phosphorylation
    3. Zymogens
    4. Cofactors
    5. Association with other peptides
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11
Q

Allosteric regulation

A
  • you will have other molecules besides the substrate that will bind to the enzyme in some site other than the active site
  • sometimes they activate and sometimes they inhibit
  • when they binds the protein changes its shape
  • -if you change its shape you change itd ability to catslyze a rxn
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12
Q

A - b - c - enzyme - d - e

Positive and negative feedback

A

If there is alot of a b or c, you need to activate the enzyme(positive feedback)
-if theres alot of d or e you need to inactivate the enzyme(negative feedback)

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13
Q

Phosphorylation

A
  • Also know as covalent modification because youre adding a covalent bond
  • adding a phosphate group to an alcohol
  • promotes a conformation change in the protein because phosphates have alot of negative charges
  • sometimes it activates an enzyme and sometimes it deactivates an enzyme
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14
Q

Enzymes that phosphorylate a protein

A
  • kinases(use atp to provide the phosphate)
  • phosphorylases (dont use atp)
  • phosphatases dephosphorylate a protein
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15
Q

Zymogens

A

-Inactive precursers that become active upon proteolytic cleavage

16
Q

Cofactors

A

Metal ions or organic molecules