enzyme kinetics Flashcards

1
Q

difference between a cofactor and a coenyme

A

cofactors don’t get used up but coenzymes do

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2
Q

what enzyme is an example of an induced fit

A

hexokinase

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3
Q

what is Km

A

substrate conc where enzyme velocity is 1/2 max

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4
Q

what is Kcat

A

describes the rate limiting step of any enzyme catalyzed faction, turnover number aka measure of substrate molecules turned over per enzyme molecule per second

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5
Q

three kinds of reversible inhibitors

A

competitive uncompetitive mixed

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6
Q

what does competitive inhibitor bind

A

e

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7
Q

what does uncompetitive inhibitor bind

A

ES copmlex

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8
Q

what does a mixed inhibitor bind

A

both E and ES complex

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9
Q

what type of an inhibitor is a noncompetitive inhibitor

A

mixed

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10
Q

what ratio do you use to compare enzymes

A

Kcat/Km

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11
Q

competitive inhibition- what happens to kcat and km

A

kcat doesn’t change and apparent Ck increases as [I] increases

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12
Q

in lineweaver burk plot, what is the x and y intercept and slope indicative of

A

x intercept= -1/Km, y intecept= 1/vmax, and slope is Km/Vmax

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13
Q

in mixed inhibition, what parameters are affected

A

All-kcat, vmax, and Km

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14
Q

in uncompetitive inhibitors, what parameters are affected

A

all three

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15
Q

regulation of enzymes 4 mechanisms

A

allosteric, covalent modification, binding of another reg protein, proteolytic cleavage for actuation

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