Lecture 7 - Enzyme Kinetics Flashcards

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1
Q

Substrates bound to enzymes by

A

Electrostatic bonds
H-bonds
Van der waals forces
hydrophobic interactions

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2
Q

Isomerase

A

catalyze intramolecular rearrangements of molecules

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3
Q

reverse reaction of lyase

A

synthase

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4
Q

Molecules that naturally regulate enzyme activity are

A

reversible noncompetitive inhibitors

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5
Q

enzyme is fully active when it has

A

sugar + ADP

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6
Q

Feedback Inhibition

A

Metabolic pathway turned off by its end product (inhibitor)

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7
Q

Kinase adds or removes PO4?

A

adds

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8
Q

transition state complex

A

increase reaction rates by decreasing the amount of energy required

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9
Q

Factors that influence enzyme catalyzed reactions

A

temperature
pH
enzyme concentration
substrate concentration

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10
Q

Km

A

Substrate concentration at which the reaction rare = ½ maximal value

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11
Q

Vmax

A

Maximal rate of product formation when substrate concentration is high

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12
Q

Characterization of Protein

A

-molecular masss
-isoelectric point
-chromatography

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13
Q

Kcat

A

Measure of catalytic activity

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