BoC Enzymes Flashcards

1
Q

What are 6 main types?

A

oxoreductases, transferases, hydrolases, lyases, iosomerase, ligase

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2
Q

Draw out enzyme reaction scheme

A

see notes

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3
Q

What is kd

A

k2/k1

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4
Q

What is km?

A

(k2+k3)/k1

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5
Q

k3 also known as

A

kcat

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6
Q

What 2 monosaccharides do bacterial cell walls contain?

A

N-acetylglucosamine and N-acetyl muramic acid

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7
Q

Draw bacterial cell wall

A

see notes

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8
Q

Lysozyme binds…

A

the sugar moiety of the peptidoglycan layer, has a hydrophobic active site cleft

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9
Q

Draw lysozyme action basic

A

see notes

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10
Q

This mechanism illustrates principles of…

A

Geometric effects, nucleophilic attack, acid catalysis

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11
Q

What is an example of an irreversible inhibitor?

A

Nerve agent sarin, interacts with acetylcholinesterase

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12
Q

What is a suicide inhibitor and what is an example of one?

A

Enzyme starts to catalyse reaction of inhibitor, forms covalent bond, can’t proceed further, stuck with inhibitor eg. penicillin for glycopeptide transferase

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13
Q

What is an eg of a competitive inhibitor?

A

Methotrexate, a chemo drug that mimics folic acid, competes with folic acid for thymine synthesis, folic acid essential for DNA synthesis

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14
Q

How can enzymes be controlled

A

(de)phosphorylation, negative feedback (often genetic control with TF), Activation of zymogens (inactive enzymes that can be switched on but not off unless destroyed), allosteric binding, compartmentalisation

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15
Q

Describe how haemoglobin is cooperative (draw diagram of the concerted and sequential model)

A

see notes

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16
Q

Which 2 lysozyme amino acids participate in stabilising the transition state?

A

Glutamic acid and aspartic acid lie either side of bond between D and E in active site
glutamic acid in non-polar enviroment, largely protonated and acts as base
Asp in polar environment, deprotonated and negativey charged
Once substrate bound glu donates H to O of glycosidic bond