Unit 1: Enzymes Flashcards

1
Q

What is the equilibrium constant equation ?

A

K = Kf/ Kr

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2
Q

What is the transition state ?

A

A part of any chemical reaction where old bonds are incompletely broken and new bonds are incompletely formed

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3
Q

What are 3 ways enzymes lower the transition state of a reaction ?

A
  • Proximity
  • Orientation
  • Microenvironment
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4
Q

What is proximity in relation to enzymes and the transition state ?

A

When enzymes bring substrates together and this increases rate by 10^5-10^8

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5
Q

What is orientation in relation to enzymes and transition state ?

A

When an enzyme orients substrates so that they can best attain the most favourable position to achieve transition state

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6
Q

What is microenvironment in relation to enzymes and transition state ?

A

The idea that an active site can provide protection to a non aqueous environment

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7
Q

What is the optimal conformation of a binding site ?

A

One that precisely contours the transition state of the reactants

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8
Q

How is catalysis achieved ?

A

When amino acid residues are brought close together in their tertiary structure to form an active site

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9
Q

What is the induced fit model of enzyme action ?

A

The idea that the active site moulds itself around the substrate. This leads to the enzyme changing conformation upon substrate binding

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10
Q

What is the Michaelis-Menten theory of kinetics ?

A

That enzymes act by increasing the rates of both the forward and reverse reactions equally. This does not change the equilibrium constant

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11
Q

What is the Michaelis-Menten kinetics equation ?

A

S + E <——> ES —–> P + E

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12
Q

What does E stand for in the Michaelis-Menten kinetics equation ?

A

E = Enzyme

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13
Q

What does S stand for in the Michaelis-Menten kinetics equation ?

A

S = Substrate

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14
Q

What does ES stand for in the Michaelis-Menten kinetics equation ?

A

ES = Enzyme substrate complex

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15
Q

What does P stand for in the Michaelis-Menten kinetics equation ?

A

P = Product

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16
Q

What is a hyperbolic curve ?

A

The relationship between the rate of reaction and concentration of the substrate

17
Q

What is the term used for the effect of temperature on reaction rate ?

A

Fundamental

18
Q

What is the term used for the effect of temperature on denaturation rate ?

A

Consequential

19
Q

What does the PH optimum often reflect ?

A

PH sensitive events at the active site

20
Q

What is the idea of an enzyme pathway ?

A

That enzymes rarely operate alone, they are part of a chain of reactions known as a pathway.

21
Q

What is an allosteric enzyme ?

A

Type of enzyme that can change its activity or shape in response to the binding of a molecule at a site other than its active site

22
Q

What shape do allosteric enzymes display on a graph ?

A

A sigmoidal S-shaped curve

23
Q

What is the function of an allosteric inhibitor ?

A
  • Stabilising the inactive state
  • This decreases affinity of enzyme for the substrate
24
Q

What is the function of an allosteric activator ?

A
  • Stabilising the active state
  • This increases the affinity of the enzyme for the substrate
25
Q

How can enzyme activity be controlled/ regulated (4) ?

A
  • Control by covalent modification, especially phosphorylation
  • Control by regulatory proteins and/ or nucleotides
  • Control through ion binding
  • Control through proteolysis
26
Q

What are enzymes that bring about phosphorylation called ?

A

Kinases- they induce phosphorylation

27
Q

What are enzymes that cause dephosphorylation called ?

A

Phosphatases- they cause dephosphorylation

28
Q

What are the 2 forms of kinase ?

A
  • Serine/threonine kinases
  • Tyrosine kinases
29
Q

What is the EF hand motif ?

A

The hand motion that says the calcium binding site is located in a tight loop connecting two alpha helixes (E and F)