Lecture 1 - Enzyme Kinetics I Flashcards

1
Q

example of how drugs often alter enzyme activity:

A

HIV1 protease - target for AIDs therapy

four drugs used to treat HIV, interact with active site “tunnel”, drugs mimic a protein chain, but they cannot be cleaved by the enzyme and they block activity

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2
Q

what do enzymes offer within biological practices?

A

enzymes offer catalysis which ensure the CONTROL of biological processes

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3
Q

what is biological catalysis:

A

biological catalysis is a process in which an enzyme lowers the activation energy for a catalysed process

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4
Q

what does the binding of an enzyme to a substrate provide?

A

a transition state

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5
Q

two models of enzyme-substrate binding:

A

(1) induced fit

(2) lock & key

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6
Q

summary of biological catalysis:

A
  • enzymes increase rate of reactions
  • they reduce the activation energy of a reaction making it more rapid
  • enzymes do not alter reaction equilibrium
  • enzymes are generally specific for a single chemical reaction
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7
Q

what changes over the course of enzyme reaction:

A

during an enzyme reaction, substrate and product concentrations change

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8
Q

to understand how the enzyme works, we need to:

A

examine the speed of reaction and the affinity of the enzyme for substrate

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9
Q

to measure an enzyme catalysed reaction we need to:

A

identify something that changes to measure

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