Enzyme Catalysis Lec1 Flashcards

1
Q

What are catalysts?

A

Substance which accelerates a chemical reaction without being consumed.

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2
Q

Spontaneous reactions

A

Have -ve delta G
They are too slow so they need to be accelerated
Do this using enzymes

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3
Q

Ea (Activation Energy)

A

Prevents reactants becoming products instantaneously.
Energy input to convert stable reactants into unstable molecular transition state.
The Ea determines rate of reaction and the form of the transition state determines the size of the Ea.

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4
Q

What does enzyme catalysis do?

A

1) Alters the transition state species
2) Destabilise the ground state
Reduced activation energy to form the transition state.

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5
Q

Enzymes are?

A

Biological Catalysts.
Large Molecules held together by many non-covalent interactions.
Contain Active sites
Almost always proteins.
Act under mild reaction conditions (sensitive)

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6
Q

Enzymes are specific to …

A

Type of reaction
Positional specificity
Stereospecificity (active site is asymmetrical)

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7
Q

How enzymes catalyse a reaction

A

ES complex forms - substrate binds to active site

Free energy released when multiple weak bonds form between enzyme and substrate.

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8
Q

Active sites

A

Small part of total volume of enzyme
On inside of enzyme
Require large protein to shield active site (don’t want water to interact)
Unique microenvironment (can exclude water)

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9
Q

Substrate bound to enzymes by what attractions?

A

Electrostatic Interactions
Hydrogen Bonds
Van Der Waals Forces

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10
Q

Chemical Events at an active site

A

Binding and spacial orientation of substrates (two can come together to form one)
Ionic charge interactions
Induction of strain due to structure

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11
Q

What does enzymes being flexible mean/allow

A

Can change shape:
Contributes to stabilising transition state
Excludes water
Bring components of the reaction closer together

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12
Q

Active site binding

A

Induced fit - substrate binds to enzyme which changes conformation to become complementary to the substrate.
Specificity of binding depends on the precise arrangement of atoms in the active site.
‘Dynamic recognition’- induced fit

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13
Q

Lowering the transition state energy

A

Stabilisation lowers the energy; less energy needed for transition state/reaction to proceed.

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14
Q

Enzyme Catalysis equation

A

Kcat/Kuncat

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15
Q

Effects of pH on enzyme activity

A

Regulates efficiency of the catalysis
Can ionise the substrate
Can change catalytic efficiency by inducing change in structure of proteins

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16
Q

Why does each enzyme have optimum pH

A

H+ ions bind to or are released from carboxyl groups and amino groups that are present on the side chains of the amino acids.
Charges on amino acids change based on pH. Important for structure.
Most enzymes optima pH is close to conditions they normally operate in.

17
Q

Temperature

A

Increased temp=increased reaction
1) increases activity (bump into each other more)
2) active site effects (reversible)
3) denaturation
Increase temperature increases flexibilty of protein allowing formation of the transition state complex.

18
Q

7 Types of enzyme groups

A
Oxidoreductases 
Transferases
Hydrolases
Lysases
Isomerases
Ligases
Translocases
19
Q

Oxidoreductases

A

Catalyse transfer of e- from doner to an acceptor.

Oxidation/Reduction

20
Q

Transferases

A

Catalyse the transfer of functional group from one molecule to another eg. Phosphate

21
Q

Hydrolases

A

Catalyse the cleavage of bonds through addition of water or vice versa. e.g. kinases

22
Q

Lysases

A

Catalyses removal of group to form a double bond or addition of group to a double bond or cleaves involving e- rearrangements.

23
Q

Isomerases

A

Catalyses intramolecular rearrangements

24
Q

Ligases

A

Catalyse reactions in which two molecules are joined

25
Q

Translocases

A

Catalyses transfer from one side of a membrane to the other