Enzyme Kinetics Flashcards

1
Q

Write out Michaelis Constant

A

Km=(K-1+k2)/k1

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2
Q

How do you find Km?

A

S when Vmax/2

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3
Q

What is Km?

A

Concentration of S which gives 1/2Vmax

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4
Q

Competitive Inhibition does what to Vmax and Km?

A

Km varies Vmax doesn’t change

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5
Q

Non-competitive Inhibition does what to Vmax and Km?

A

Km stays constant. Vmax varies

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6
Q

What is a common mechanism of allosteric control?

A

inhibition of rate limiting enzyme by end products

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7
Q

What type of curve do allosteric enzymes produce?

A

sigmoidal curve

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8
Q

Give an example of allosteric regulation

A

Haemoglobin

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9
Q

A small Km means what?

A

more “efficient” enzyme

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10
Q

Draw the Michelins-Menton enzyme substrate thing

A

E+S->//E+P

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