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S1 Pharmacology > Enzymes > Flashcards

Enzymes Flashcards

1
Q

how does an enzyme work ?

A
  • enzymes decrease activation energy = increasing rate of reaction
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2
Q

what is the lock and key hypothesis ?

A
  • active site has rigid shape
  • substrate shape is complementary to active site
  • ESC is formed then EPC
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3
Q

what is the induced fit hypothesis ?

A
  • active site is flexible
  • active site changes shape to fit substrate
  • ESC then EPC formed
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4
Q

how does pH affect enzyme activity ?

A
  • enzymes active at optimum pH
  • high or low pH can denature enzymes as tertiary structure is disrupted
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5
Q

how does temperature affect enzyme activity ?

A
  • high temperature = denaturation
  • inc temp - inc ke more frequent collisions
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6
Q

what is an apoenzyme ?

A
  • inactive protein part of an enzyme
  • needs a cofactor to be active
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7
Q

what is a holoenzyme ?

A
  • enzyme along with cofactor
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8
Q

what is a cofactor ?

A
  • either organic or inorganic
  • help enzyme function
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9
Q

what is an inorganic cofactor ?

A
  • metal ions
  • eg. Zn2+ for carbonic anhydrase
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10
Q

what is an organic cofactor ?

A
  • prosthetic groups (heam)
  • coenzyme (NAD)
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11
Q

what is the difference between prosthetic groups and co-enzymes ?

A
  • co-enzymes are temporarily bound whereas prosthetic groups are tightly bound
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12
Q

what are the 6 classifications of enzymes ?

A
  • Ligase
  • Isomerases
  • Lyase
  • Hydrolases
  • Oxidoreductases
  • Transferases
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13
Q

what are transferase enzymes ?

A
  • transfer a functional group between molecules
  • eg. kinases transfer phosphate groups
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14
Q

what are ligase enzymes ?

A
  • catalyse synthesis of new covalent bonds using ATP
  • eg. DNA Ligase
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15
Q

what are oxidoreductase enzymes ?

A
  • catalyse transfer of electrons
  • eg. lactate dehydrogenase
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16
Q

what are isomerase enzymes ?

A
  • catalyse conversion of isomers, transferring groups within the same molecule
  • eg. cis trans isomers
17
Q

what are hydrolase enzymes ?

A
  • addition of water to break bonds
18
Q

what are 3 types of hydrolase enzymes ?

A
  • phosphatases (ester bonds)
  • lipases (ester bonds - lipids)
  • peptidases (peptide bonds - forms 2 products )
19
Q

what are lyase enzymes ?

A

-catalyse addition or removal of H20 , CO2 , NH3 to create double bonds

  • eg. dehydrase, decarboxylase. deaminase
20
Q

what are Isoenzymes ?

A
  • different amino acid sequence but catalyse the same reaction
21
Q

what is allosteric regulation ?

A
  • effector can bind to allosteric site and either speed up or slow down action
22
Q

what is feedback inhibition ?

A
  • the end product binds to an enzymes at the start of the pathway to stop further synthesis
23
Q

What do kinase enzymes do?

A
  • Add phosphate groups

S1 Pharmacology (16 decks)

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