Enzymes Flashcards

1
Q

What are three ways in which enzymes are specific?

A

temperature - function optimally over a narrow range
pH - function optimally over a narrow range
substrate - are specific to a particular substrate

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2
Q

What are the rules enzymes must follow during catalysis?

A

they will not catalyse a thermodynamically unfavourable reaction
- gibbs free energy must be less than zero (negative)

they will not alter the equilibrium of the reaction

they will remain unchanged at the end of the reaction

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3
Q

What is the site of catalysis known as? What does it consist of?

A

the site of catalysis is the active site
- site where the enzyme-substrate complex forms

it consists of two domains

  • binding site = substrate binding
  • catalytic site = chemical transformation takes place
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4
Q

What is the difference between the lock and key hypothesis and the induced fit hypothesis?

A

lock and key
- assumes that only one specific enzyme will be able to react with the substrate
= does not provide a model for every catalytic process

induced fit
- assumes the substrate induces the required orientation of groups in the active site necessary for binding and catalysis
= occurs as the substrate gets closer to the enzyme

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5
Q

What are the methods by which enzymes lower activation energy?

A

enzymes position/align the substrate correctly so that it may attain the appropriate transition state

enzymes provide a surface or environment
- molecules in solution rely on collisions so the enzyme provides a stable surface to collide on/with

enzymes assist in weakening the bonds by

  • causing changes in bond energy = due to interactions with the functional groups in the active site
  • changing electron densities = due to interactions with the functional groups in the active site
  • inducing distortion and bond strain = due to binding the substrate to the active site
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6
Q

What units is enzyme activity usually measured in?

A

micromoles of substrate transformed per second/minute

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7
Q

What are the factors affecting the rate of reaction?

A

enzyme concentration
- is the limiting factor when there is excess substrate

substrate concentration
- is the limiting factor when enzyme concentration is constant
= reaction occurs until all the enzymes are bound

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8
Q

What is Michealis Constant (Km)?

A

concentration of the substrate that corresponds to half of the maximum rate of reaction
- gives an indication of the affinity of the enzyme for the substrate
= is inversely proportional to the affinity of the enzyme for its substrate

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9
Q

What does a low/high Km mean?

A

Km - Michealis Constant

low Km - enzyme has a high affinity for its substrate
= needs little to become saturated

high Km - enzyme has low affinity for its substrate
= needs a lot to become saturated

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10
Q

What is Vmax?

A

is a limiting value

- the rate of reaction when the enzyme is fully saturated by substrate

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11
Q

What is the difference between the Michealis-Menten equation and the Lineweaver-Burk plot?

A

the Lineweaver-Burk plot is the reciprocal of the Michealis-Menten equation

the Michealis-Menten equation is more useful for determining data
- plot gives a straight line

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