Enzyme kinetics and inhibition Flashcards

(32 cards)

1
Q

what is enzyme kinetics used for?

A

to determine quantitative relationships

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2
Q

what is a progress curve used for?

A

to measure product formation as a function of time

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3
Q

why does the slope of a progress curve begin by being linear and the gradually decrease?

A

because of product inhibition or enzyme inactivation

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4
Q

what do rate equations do?

A

describe chemical processes

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5
Q

what is the rate equation for a unimolecular reaction? bimolecular?

A

v=K[A]

v=K[A][B]

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6
Q

what with the rate of product formation generally increase with?

A

the amount of enzyme present

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7
Q

what is the michaelis-menten equation?

A

v=vmax[S]/Km+[S]

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8
Q

what is vmax?

A

where the reaction velocity reaches its plateau

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9
Q

what does reaction rate depend on?

A

[ES]

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10
Q

what does Km =?

A

K-1 + K2/K1

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11
Q

what indicates catalytic efficiency?

A

Kcat/Km

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12
Q

what does Kcat indicate?

A

how fast an enzyme can act, the number of catalytic cycles that each active site undergoes per time

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13
Q

what does Kcat=?

A

vmax/[E]total

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14
Q

for the simplest enzyme pathway what does Kcat =?

A

K2

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15
Q

what does a high affinity for substrate do to the progress curve?

A

pushes it left

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16
Q

on a progress curve at Vmax/2 what is Km?

17
Q

what is Km?

A

substrate affinity

18
Q

what is catalytic perfection?

A

when the enzymes rate is completely controlled by diffusion
Kcat/Km = 10^8-10^9

19
Q

what does a lineweaver-burk plot accomplish?

A

it linearizes michaelis-menten data

plots 1/V vs 1/[S]

20
Q

what does a lineweaver-burk plot give?

A

a negative slope, yintercept = 1/vmax, xintercept=-1/Km

21
Q

what two types of enzyme inhibition are there?

A

reversible or irreversible

22
Q

what is irreversible enzyme inhibition?

A

molecules that covalently modify the active site

23
Q

what is a transition state analog?

A

something that is often a better inhibitor than substrate analogs because they lower the ∆G

24
Q

what are reversible inhibitors?

A

normally bind to enzymes non-covalently and can be classified by where the bind and what reaction steps they block; these are kinetically distinguishable

25
what are some different types of reversible inhibitors? (4)
competitive, non-competitive, uncompetitive, mixed
26
what is a competitive inhibitor?
it binds at the active site so it competes with the substrate, depends on the [S] vs [I], mutually exclusive with the substrate
27
what does a competitive inhibitor appear to increase? Vmax?
Km | no change
28
what way does a competitive inhibitor push the M-M plot?
right, makes the L-B plots slope steeper
29
what is a noncompetitive inhibitor?
substrate and the inhibitor are not mutually exclusive bust the ESI complex is less active than the ES complex there are separate binding sites on the enzyme
30
non-competitive inhibitors effect on Km and Vmax? M-M plot?
decreases Vmax, no change to Km | M-M plot pushed down
31
whats an allosteric enzyme?
often have multiple subunits and show cooperativity: the subunits interact to give a sigmoidal curve instead of a hyperbolic one (M-M plot), thus they do not easily fit the M-M model.
32
how do allosteric effectors inhibit or activate?
inhibit using a pathway end product activate by a co-substrate, often involves an early or/and a committed step in a metabolic pathway