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MCD Metabolism > energetics and enzymes > Flashcards

energetics and enzymes Flashcards

enzyme kinetics: explain how enzyme activity may be measured using spectrophotometry and how experimental values of reaction velocity at different substrate concentrations can be used to derive Km and Vmax for an enzyme. Explain the effects of competitive and non-competitive inhibitors on Km and Vmax

1
Q

define Vmax

A

maximum rate

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2
Q

does Vmax change when a competitive inhibitor is added

A

no

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3
Q

does Vmax change when a non-competitive inhibitor is added

A

yes - it decreases

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4
Q

define Km

A

1/2 Vmax

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5
Q

does Km change when a competitive inhibitor is added

A

yes - it increases

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6
Q

does Km change when a non-competitive inhibitor is added

A

no

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7
Q

Vmax and Km diagram

A

diagram from metabolism 2

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8
Q

Lineweaver-Burk plot

A

y-axis: 1/V; x-axis: 1/[substrate]; y-intercet is 1/Vmax; x-intercept is -1/Km

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MCD Metabolism (21 decks)

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