Chapter 7 Kinetics and Regulation Flashcards

1
Q

What is the first order reaction, and what is the proportionality constant unit?

A
  • This is when the velocity of a reaction is directly proportional to reactant concentration and it uses the units s^-1
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2
Q

What is the second order reaction’s proportionality constant units?

A

its per molar per second, M^-1s^-1

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3
Q

How is enzyme kinetics measured ?

A

When you measure velocity as a function of substrate concentration with a fixed amount of enzyme

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4
Q

What is the difference between K1 and K^-1 and K2

A

-K1 is how fast the enzyme binds
-K^-1 is how fast the Enzyme disassociates
-K2 is how fast the substrate is converted into product

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5
Q

How is initial velocity determined ?

A
  • it is determined by measuring product formation as a function of time and then determining the velocity soon after the reaction has started
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6
Q

What is the Michaelis Menten equation

A

V0=Vmax([S]/[S]+Km)
-and we ignore the bottom [S] if it is much much smaller than the Km.

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7
Q

What is the Lineweaver Burk equation?

A

1/Vo=Km/Vmax*1/S+1/Vmax

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8
Q

k2 is also known as ?

A

kcat

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9
Q

If [E]T is known what equation is useable ?

A

Vmax=k2[E]T

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10
Q

If the [S]«Km, what can we assume about the [E]T

A

we can assume that free enzyme [E]~[E]T

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11
Q

Kcat/Km is a measure of ______________

A

catalytic efficiency

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12
Q

The _______Kcat over the _________ the Km better the result. We always want a ________Kcat and a ________ Km

A

Higher, smaller,Higher,smaller

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13
Q

What is the rate limiting step?

A

The rate of formation of the enzyme substrate complex,K1

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14
Q

Diffusion limits the value of K1 around what value

A

~10^8-10^9 s^-1M^-1

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15
Q

-What are sequential reactions?

A

It is a formation of ternary complex consisting of thee two substrates and the enzyme

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16
Q

What are double displacement reactions? What are the also known as?

A

it is a formation of a substituted enzyme intermediate, they are also known as ping-pong reactions

17
Q

What are allosteric enzymes and what do they do?

A

-They are catalysts and information Sensors
-it controls the flux of biochemical reactions in metabolic pathways
- Without them metabolic chaos would occur

18
Q

What allows the allosteric enzyme to do generation of complex metabolic pathways ?

A

Their regulatory properties allow for that

19
Q

_________________catalyze the committed step of metabolic pathways,________________ facilitate the remaining steps

A

Allosteric enzymes, Michaelis Menten enzymes

20
Q

How does the synthesizes of F get regulated?

A

By the feedback inhibition , it sends a message to A when there is too much F being made and it eventually inhibits the process.

21
Q

How does the pathway product F inhibit enzyme e1

A

it binds to the regulatory site on the enzyme that is distinct from the active site

22
Q

Which type of model describes the behavior of allosteric enzyme

A

The concerted model

23
Q

What are the features of the concerted model

A

-The enzyme exists in two different quaternary structures, designated T(tense) and R(relaxed)
-T and R are in equilibrium , with T being the more stable state
-The R state is enzymatically more active than the T state
-All active sites must be in the same state

24
Q

What will help favor the conversion of more enzymes to the R state.

A

The disruption of T<–>R equilibrium by the binding of substrate

25
Q

Which state will most enzymes be in as concentration increases?

A

The R(relaxed) state

26
Q

what disrupts the R<–>T equilibrium when they bind enzyme

A

Allosteric regulators

27
Q

What stabilizes the T and R state

A

-Inhibitors stabilize T state
-Activators stabilize R state

28
Q

What is the disruption of T<–>R equilibrium by substrate called

A

Homotropic effect

29
Q

What is the disruption of T<–>R equilibrium by regulators called

A

Heterotropic effect

30
Q

What is the sequential model

A

it is a model for allosteric enzymes that proposes subunits undergo sequential changes in the structure