Enzymes - Lecture 2 Flashcards

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1
Q

Define international unit of enzyme activity ( U/UI)

A

The amount of enzyme that catalysed the conversion of one micro mole of substrate per minute.

1 mole = 1x10^6 micromole

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2
Q

What are 5 key features of enzymes ?

A

1) highly specific
2) unchanged after a reaction
3) they are proteins
4) increases rate of reaction
5) do not affect eq

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3
Q

What does the Michaelis - menton equation explain ?

A
  • explains how an enzyme works.
  • E+ S = ES = E + P
  • assumes that a specific complex is necessary in order for an enzyme to catalyse a reaction
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4
Q

Define Vmax

A
  • maximal rate where all enzyme active sites are saturated with substrates
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5
Q

What are the units for Vmax?

A

Mol/min

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6
Q

Define Km ( M)

A

Substrate concentration that gives half the maximum velocity

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7
Q

How is Vmax related to affinity?

A

Inversely proportional.

The lower the km value , the greater the affinity

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8
Q

How is Vmax related to enzyme concentration?

A

Proportional to each other

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9
Q

On a Lineweaver Burk plot , if the x intercept becomes closer to 0 what does this indicate ?

A

km increases

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10
Q

If the value on the y intercept of the Lineweaver Burk plot increases , what does this indicate ?

A

Vmax decreases

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11
Q

Dhow does a competitive inhibitor affect km and Vmax?

A
  • does not affect Vmax because eventually substrate conc will output inhibitor.
  • km will increase .
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12
Q

How does a non competitive inhibitor affects km and Vmax?

A
  • Vmax decreases because the overall turnover of enzymes decreases.
  • km stays the same because the non competitive inhibitor is not even binding to active site.
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13
Q

Define activity

A
  • another definition of rate - how much product is made per unit time.
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