Enxyme Kinetics I Flashcards

1
Q

no matter how many substrate, is there a limit to Product

A

yes, there is

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2
Q

as [S] rises, what happens to Vo

A

Vo rises too but only at initial point

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3
Q

what is the reaction order for E+S»> ES

A

zero-order when [S]&raquo_space; [E]

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4
Q

which is the rate limiting step between ES»>E+P and E + S&raquo_space;>ES

A

ES»>E+P (k2)

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5
Q

Is V0 directly proportional to [S] always true

A

no, the enzyme differs

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6
Q

What is the theoretical speed limit at which an enzyme will not work any faster because it has reached it speed limit

A

Vmax

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7
Q

As [S] increases, Vo approaches Vmax true/false

A

true

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8
Q

As [S] increases, what happens to [ES]

A

it increases too

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9
Q

when does [ES] stop increasing

A

when [ES] =[E]T because [E]T=[ES] + [E]

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10
Q

Km is the

A

Michaelis constant

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11
Q

Km is related to

A

measure of the affinity of the enzyme for the substrate units in terms of concentration

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12
Q

Km is the combination of which constants

A

k2+k1/k1

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13
Q

Km is a measure of

A

ES binding or affinity

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14
Q

Small Km means

A

tight binding

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15
Q

large Km means

A

weak binding

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16
Q

Describe low [S] and high [S]

A

at low [S[, 1/2 Vmax =Km
at high [S] Vo= Vmax[S] /Km and Vo=Vmax

17
Q

this is the # molecule of substrate converted to product by 1 enzyme molecule in 1 second (units of s-1)

A

Kcat

18
Q

What is the rate-limiting step at saturation

A

Kcat

19
Q

What tells you how good an enzyme is when they are working on 2 different substrates

A

specificity constant Vo= Kcat[E]T[S]/[S] + Km

20
Q

what is Vo when [s] &laquo_space;Km

A

Vo=Kcat [E]T[S]/Km

21
Q

Kcat/Km tells you

A

how efficiently an enzyme

22
Q

how is catalytic perfection achieved

A

when a reaction rate is diffusion-controlled (10^8-10^9)

23
Q

When does Kcat/Km approach its “diffusion limit”

A

when the enzyme carries out catalysis every time a collision occurs between E and S

24
Q

Whar are the modes in which subtrate binds to a enzynme

A
  1. Invoving a ternary complex
  2. No ternary complex
25
Q

Which reaction modes does enzyme & substrate bind in random order or order

A

Ternary complex

26
Q

Which reaction follows a ping-pong mechanism

A

no ternary complex

27
Q

What is the difference between ordered and ping pong

A
  1. the product is removed individually in Ping-pong mechanism
  2. the enzyme conformation is changed as product is removed so E’ in ping-pong
28
Q

What does binding of a modulator do the substrate unit

A

it changes the conformation of the substrate, making it more active

29
Q

What is the advantage of inhibiting the first enzyme in a pathway

A

because it is allosterically regulated by final product of the pathway allowing feedback inhibition