Enzymes & Enzyme Kinetics Flashcards

1
Q

What are enzymes?

A

Protein catalysis that

  1. increase the velocity of the reaction and
  2. not consumed during the reaction
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2
Q

What kind of shape do enzymes have?

A

Three-dimensional that fit the shape of reactant (substrate)

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3
Q

What is the name RNA with catalytic activity?

And what does it catalyse?

A

Ribozyme

Cleavage and synthesis of phosphodiester bond

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4
Q

Common property of enzymes as biological catalyst?

A

Increase the velocity of spontaneously occurring reaction WITHOUT altering the chemical equilibrium

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5
Q

What do enzymes do to the activation energy (Ea) and the rate of reaction (RoR)?

A

Lower the Ea so RoR increases

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6
Q

How do enzymes differ from other catalysts?

A
  1. Highly specific
    - interact with 1 or few substrate
    - catalyse only one type of reaction
  2. Highly efficient
    - increase RoR x100-1000
  3. Act under mild physiological conditions
    - pATM, pH7, 37ºC
  4. Activity and synthesis strongly regulated in cells
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7
Q

What is holoenzyme?

A

An active enzyme with its non-protein component

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8
Q

What is apoenzyme?

A

An inactive enzyme without its non-protein component

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9
Q

What is the non-protein moiety made of?

A

Cofactor - metal ion Zn2+/Fe2+ (bind tightly)

Coenzyme - small organic molecule (bind loosely)

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10
Q

In what ways do coenzymes associate with enzymes?

A

Cosubstrates - transiently associate; disassociate from enzyme in altered state

Prosthetic group - permanently associate; return to original form

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11
Q

Give 3 examples of Coenzymes and where they are derived from

A

*NAD - from nicotinic acid (B3)

Coenzyme A - from pantothenic acid (B5)

**FAD - from riboflavin (B2)

  • (nicotinamide adenine dinucleotide)
  • *(flavin adenine dinucleotide)
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12
Q

What are prosthetic groups?

A

Tightly bound cofactors (covenant bond)

Can be metal ion or organic molecule

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13
Q

What are cofactors?

A

Type of enzyme partner group that aids in enzyme functionality (Zn2+/Fe2+)

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14
Q

What are coenzymes?

A

A specific type of cofactor that are ‘organic’, works in active site, NAD, FAD

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15
Q

What is the relationship between holoenzymes, apoenzymes, non-protein component?

A

Holoenzyme = apoenzyme + non-protein component

K = [apoenzyme][non-protein component]
——————————————————-
[holoenzyme]

If K -> 0 then strong interaction (prosthetic group)

If K > 0 then weak interaction (coenzyme)

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16
Q

What are the 6 classifications of enzymes?

A
  1. Oxidoreductases
  2. Transferases
  3. Hydrolases
  4. Lyases
  5. Isomerases
  6. Ligases
17
Q

What do oxidoreductases do?

A

Redox

18
Q

What do transferases do?

A

Transfer atom groups

19
Q

What do hydrolases do?

A

Hydrolysis

20
Q

What do lyases do?

A

+/- atom groups to/from | or || bonds

21
Q

What do isomerases do?

A

Rearrange atoms

22
Q

Ligases

A

Use ATP to combine molecules

23
Q

Write the equation(s) for enzyme catalysis

A

E + S -> ES

ES -> E + P

=> E + S -> ES -> E + P

E.g.
Sucrase + sucrose -> ES -> Sucrase + glucose + fructose