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
Q

How do coenzymes act as cofactors?

A

They are carriers of electrons, atoms or functional groups

26
Q

What are coenzymes often derived from?

A

Vitamins

27
Q

How do enzymes make reactions favourable via reaction coupling?

A

The coupling of a non-spontaneous and spontaneous reaction can result in an overall spontaneous reaction

28
Q

where do cofactors bind?

A

the active site

29
Q

What coenzyme facilitates glycogen phosphorylase activity by binding to the active site?

A

PLP - pyridoxal phosphate