Signaling Enzymes Introduction Flashcards

Chapter 3

1
Q

What are the basic examples of signaling enzymes?

A

kinases, phosphatases, and G proteins (GAPs and GEFs)

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2
Q

What do signaling proteins do?

A

they convert conformational changes into catalytic activity changes

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3
Q

Signaling proteins often act as ____.

A

switches

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4
Q

How do enzymes speed up a reaction?

A

By reducing the free-energy barrier

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5
Q

Which enzyme is on the top arrow and which is on the bottom arrow?

A

Top: kinase “writer”
Bottom: phosphatase “eraser”

one adds phosphate and one takes it away

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6
Q

What are the different mechanisms where an enzyme can lower the activation energy?

A

a) binding and orienting reactive groups
b) providing acid & bases; achieves activation of an attacking nucleophile group
c) providing binding site; binding energy can reduce the FEB (ex. hydrolysis)
d) altering mechanism to form reaction intermediate with less of a FEB

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7
Q

What can enzymes not alter in a reaction?

A

deltaG

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8
Q

What do enzymes do to reach equilibrium?

A

they accelerate the approach to equilibrium

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9
Q

What three amino acids occur with phosphorylation?

A

tyrosine (unfavorable) & serine/threonin (neutral)

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10
Q

A kinase reaction is ____.

A

irreversible

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11
Q

Describe this form of catalysis

A

Enzyme orients two substrate molecules to be able to react with one another.

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12
Q

Describe this form of catalysis

A

Binding of the substrate rearranges electrons to allow for partial positive and negative charges to favor a reaction

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13
Q

Describe this form of catalysis

A

Enzyme strains the substrate to forcing it towards a transition state which favors a reaction.

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14
Q

The relative abundance of each species is determined by their ____.

A

Relative free energy

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15
Q

Which of these is the most stable?
A, A’, or A”

A

A

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16
Q

What does this represent?

A

ligand binding; reduces free energy of A’

17
Q

What does this represent?

A

phosphorylation; reduces free energy of A”

18
Q

What refers to a ligand or modification-induced change in the secondary, tertiary, or quaternary structure of a protein?

A

allosteric conformation change

19
Q

What are allosteric regulators?

A
  • activators - molecule locked in activity
  • inhibitors - molecule locked in inhibition
20
Q

What does this depict?

A

active-site conformation; different forms which the enzymes can take on due to allosteric binding

21
Q

What kind of conformational change does this depict?

A

disorder/order transitions (secondary structure)

22
Q

What kind of conformational change does this depict?

A

tetiary structure transitions

23
Q

What kind of conformational change does this depict?

A

quaternary structure transitions