Enzymes Flashcards

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1
Q

Lock and Key model

A
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2
Q

Induced fit model

A
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3
Q

Factors affecting enzyme function

A
  • pH, salinity, temperature, cofactor association
    • Apoenzyme: enzyme without its cofactor
    • Holoenzyme: enzyme with its cofactor
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4
Q

Enzyme Regulation

A
  • covalent modification i.e. phosphorylation
  • proteolytic cleavage (zymogens)
  • Association with other proetins
  • Allosteric regulation (feedback inhibition)
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5
Q

Proteolytic cleavage

A

i.e. zymogens

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6
Q

Saturation

A

All active sites are occupied by substrate, so increasing [s] will not increase the rate (Vmax)

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7
Q

Km (michaelis constant)

A
  • Substrate concentration at 1/2 Vmax
  • The smaller the Km, the greater affinity for the substrate
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8
Q

Michaelis-Menten equation

A
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9
Q

Lineweaver-Burk Plots

A
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10
Q

Competitive, uncompetitve, noncompetitive

inhibition

A
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11
Q

Oxidoreductases

A

catalyze redox reactions (electron transfer)

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12
Q

Transferases

A

catalyze transfer of functional groups

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13
Q

Hydrolases

A

catalyze cleavage of molecules driven by the addition of water

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14
Q

Lyases

A

catalyze addition of atoms or groups to a double bond

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15
Q

Isomerases

A

catalyze transfer of functional groups within a

molecule (creates different isomers of the same molecule)

i.e. mutase

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16
Q

Ligases

A

catalyze linking two molecules into a larger one