Enzymes Flashcards

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1
Q

What are enzymes?

A

Biological catalysts

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2
Q

What does an enzyme do?

A

Increase rate of reaction by providing a pathway of lower activation energy to get reactants to products

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3
Q

What does lysozyme do?

A

Catalyses the cutting of polysaccharide chains

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4
Q

What happens when you increase substrate concentration?

A

Reaction velocity increases

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5
Q

What is the maximum rate of reaction called?

A

Vmax

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6
Q

What is Km?

A

The substrate concentration required for half maximum velocity

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7
Q

What is PHOSPHO1?

A

Found in osteoblasts and chondrocytes

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8
Q

What are the two classifications of enzyme inhibitors?

A

Irreversible and reversible

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9
Q

What are irreversible enzyme inhibitors called?

A

Inactivators

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10
Q

What are reversible enzyme inhibitors called?

A

Competitive and allosteric

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11
Q

Describe irreversible inhibition?

A

React with the enzyme and form a covalent adduct with the proteins

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12
Q

What is the primary mechanism of action of diisopropyl fluorophosphate?

A

Inhibition of acetylcholinesterase (AChE)

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13
Q

What does AChE do?

A

Degrades the neurotransmitter ACh

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14
Q

What happens if there is too many ACh?

A

Overstimulation of receptors ion the post synaptic membrane

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15
Q

What is aspirin?

A

Antipyretic, anti-inflammatory and analgesic

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16
Q

What does aspirin do?

A

Irreversibly inhibiting cylooxygenase-1 (COX-1)

17
Q

What does COX-1 do?

A

Catalyses the conversion of arachidonic to prostaglandin H2 (precursor for synthesis of inflammatory mediators)

18
Q

Where does aspirin bind?

A

On the serine residue close to the active site preventing the substrate arachidonic acid from binding

19
Q

Describe competitve inhibition

A

Competes for active site of the enzyme

Like a key that gets through the keyhole but cannot unlock the door

20
Q

What is 4-aminobenzoic caid?

A

What folic acid is synthesized from

21
Q

What is used to competitively inhibit the synthesis of folic acid?

A

Sulphonamides

22
Q

What happens to Km when you introduce a competitive inhibitor?

A

Km increases

23
Q

Describe allosteric inhibition

A

Never bind to the active site

Change in conformation, substrate can longer bind

24
Q

What happens to Vmax and Km in allosteric inhibition?

A

Vmax decreases

Km often (but not always) increases

25
Q

What are the two types of allosteric inhibition?

A

Mixed and non-competitive

26
Q

What happens to the Vmax and Km in mixed allosteric inhibition?

A

Vmax decreases

Km increases

27
Q

What happens to the Vmax and Km in non-competitive allosteric inhibition?

A

Vmax decreases

Km is unchanged

28
Q

What does phophofructokinase do?

A

Catalyses transfer of phosphate from ATP to fructose 6-phosphate

29
Q

What happens when ATP is not needed?

A

The inhibitory site of PFK will be filled