enzymes Flashcards

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1
Q

what are some characteristics of enzymes?

A
  • high molecular weight
  • biological catalysts
  • denature at high temps/pH
  • specific to reactions they catalyse
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2
Q

what is meant by induced fit?

A
  • proteins have 3D flexibility
  • once bound to a substrate, enzymes change shape to form an exact fit
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3
Q

why are enzymes catalysts?

A

they lower the activation energy needed to drive a reaction

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4
Q

why do high temperatures denature enzymes?

A
  • bonds that stabilise secondary and tertiary structures are broken
  • enzyme loses its shape and the active site is altered
  • can no longer fit the substrate
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5
Q

what is optimum temperature and how does it work?

A
  • max temperature before enzymes denature
  • useful as the molecules are colliding more frequently so there is a higher chance of successful collisions
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6
Q

why must pH be kept constant?

A
  • hydrogen bonds are unaffected
  • active site remains unchanged
  • substrate can successfully bind
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7
Q

why does pH denature enzymes?

A
  • lower pH means more hydrogen ions
  • this breaks the forces of attraction ad bonds that hold enzymes together so they lose their shape
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8
Q

what are competitive inhibitors?

A

molecules similar to the substrate bind to the enzyme

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9
Q

what is the effect of competitive inhibitors?

A
  • ROR is decreased
  • can reach maximum ROR but at a slower rate
  • this can be overcome by increasing substrate concentration
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10
Q

what are non- competetive inhibitors?

A

molecule binds to a different part of the enzyme so the substrate still fits but induced fit cannot occur

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11
Q

what are the effects of non-competitive inhibitors?

A
  • ROR is reduced and can never reach maximum rate of reaction
  • increasing substrate concentration does NOT effect these inhibitors
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12
Q

describe and explain how a normal reaction profile would change if the reaction was catalysed by an enzyme.

A
  • activation energy is lowered
  • substrate and product energy stay the same
  • substrate fits into active site and form an enzyme substrate complex
  • force exerted on bonds in substrate so lowers activation energy
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13
Q

what is an intracellular enzyme and give examples?

A

produced and function inside cell
- catalase
- polymerase
- helicase

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14
Q

what is an extracellular enzyme and give examples?

A

transported out of the cell by vesicles
- amylase
- lipase
- protease

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15
Q

what is feedback inhibition?

A

end product acts as an inhibitor to stop enzyme reactions

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16
Q

what is a cofactor?

A
  • non protein component which helps an enzyme carry out its function
  • coenzyme + prosthetic group
17
Q

cofactor for amylase?

A

Cl-

18
Q

what is the prosthetic group for carbonic anhydrase?

A

Zn2+

19
Q

what is a coenzyme?

A

a non protein organic molecule that isn’t permanently attached to an enzyme, but is needed to allow the enzyme to function

20
Q

how do cofactors increase enzyme activity?

A
  • bind to enzyme
  • active site temporarily changes so substrate can have an increased likelihood of binding successfully
21
Q

what is possible when substrate binds to enzyme?

A

can weaken bonds in the substrate