lecture 9 - intro to enzymes Flashcards

1
Q

How do enzymes catalyse thermodynamically favourable reactions?

A

By lowering the activation energy required

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2
Q

What is required for a reaction to reach a high-energy transition state?

A

Activation energy supplied

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3
Q

What is the activation energy, as read off a reaction progress graph?

A

The difference in energy between the reactants and the activated complex/transition state

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4
Q

How do enzymes influence forward and reverse reactions?

A

By decreasing activation energy, the forward and reverse reactions are accelerated equally

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5
Q

What is the symbol for change in free energy?

A

ΔG

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6
Q

What is the symbol for activation energy?

A

Ea OR ΔG‡

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7
Q

How does ΔG change when an enzyme is introduced to a reaction?

A

There is no change, only ΔG‡ decreases

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8
Q

What type of molecule makes up the majority of enzymes?

A

Proteins

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9
Q

What is the function of glycogen phosphorylase

A

An enzyme that aids in glycogenolysis - breaking highly branched glycogen into glucose monomers

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10
Q

What are the 6 main classes of enzymes?

A

Oxidoreductants, transferases, hydrolases, lyases, isomerases, ligases

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11
Q

What is the role of an oxidoreductant enzyme?

A

Facilitate redox reactions, with electron transfer

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12
Q

What is the role of a transferase enzyme?

A

Facilitate the transfer of functional groups

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13
Q

What is the role of a hydrolase enzyme?

A

Facilitate the hydrolysis/cleavage of molecules using H2O

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14
Q

What is the role of lyase enzymes?

A

Facilitate the Non-hydrolytic breaking or making of a bond

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15
Q

What is the role of isomerase enzymes?

A

facilitate the transfer of atoms/groups within a molecule to yield an isomeric form

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16
Q

What is the function of ligase enzymes?

A

Join 2 molecules together via the formation of a new bond. this is usually couple to ATP cleavage

17
Q

Ligase enzyme reactions are usually coupled to what reaction?

A

ATP cleavage, which provides energy

18
Q

What is a cofactor?

A

A non-protein compound or metal ion that is required for an enzyme’s catalysis

19
Q

What are the 2 classes of cofactor?

A

Metal ions and coenzymes

20
Q

What are metal ion cofactors?

A

Lewis acids (electron pair acceptors) that can participate in acid-base catalysis

21
Q

Are metal ions Lewis Acids or Bases?

A

Lewis Acids (electron pair acceptors)

22
Q

How do metal ions act as cofactors?

A

They form coordination compounds with precise geometries for positioning reactants exactly where they need to be.

23
Q

What are some common examples of metal ion cofactors?

A

Mg2+, Zn2+, Fe2+/Fe3+

24
Q

What are coenzymes?

A

Small organic molecules that act as cofactors/cosubstrates

25
How do coenzymes act as cofactors?
They are carriers of electrons, atoms or functional groups
26
What are coenzymes often derived from?
Vitamins
27
How do enzymes make reactions favourable via reaction coupling?
The coupling of a non-spontaneous and spontaneous reaction can result in an overall spontaneous reaction
28
where do cofactors bind?
the active site
29
What coenzyme facilitates glycogen phosphorylase activity by binding to the active site?
PLP - pyridoxal phosphate