Enzyme Kinetics Flashcards

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1
Q

What is the shape of the graph plotted of reaction rate against substrate concentration?
How do we estimate Km using this?

A

Hyperbolic graph and then levels out

Km is the substate concentration at half the Vmax

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2
Q

What is the Michealis - Menton equation regulated by?

What rule must there be for it to work?

A

Kinetic constants

K-1»>K2

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3
Q

What are 3 assumptions we must have?

A
  • concentration of substate is much larger than that of the enzyme so the amount of substrate bound by an enzyme is always small
  • Enzyme substate concentration does not change with time
  • Initial velocities must be used
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4
Q

What is the equation for MM?

A

Initial velocity = Vmax[S] / Km + [S]

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5
Q

When the MM is plotted, what shape is it and what kinetic value does it tend towards?

A

Hyperbolic and it tends towards Vmax

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6
Q

The lower the Km, the — the affinity?

A

Higher

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7
Q

What does the Kcat mean?

A

The turnover number of substrates to products over time

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8
Q

What do competitive inhibitors alter and not alter?

A

Alter the Km value but not the Vmax

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9
Q

What do non-competitive inhibitors alter?

A

Vmax

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10
Q

What 2 clinical examples can this help?

A

Control of angiotensin production

Treatment of heart failure

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