Enzymes 1&2 Flashcards

(29 cards)

1
Q

How are enzymes different from chemicals?

A

Catalyse very high reaction rates
Regulated by homeostasis
Very specific

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2
Q

Ribozyme

A

Made from RNA not protein

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3
Q

Cofactor

A

Non protein component required for activity

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4
Q

Coenzyme

A

Complex organic molecule made from vitamins eg FAD

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5
Q

Prosthetic group

A

Cofactor covalently bound to enzyme

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6
Q

Apoenzyme

A

Protein component of enzyme containing cofactor

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7
Q

Holoenzyme

A

Whole enzyme apoenzyme + coenzyme

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8
Q

Substrate

A

Molecule added on by enzyme

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9
Q

Active site

A

Part of enzyme which substrate binds

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10
Q

How do enzymes reduce Ea

A

Entropy reduction
Desolvation
Induced fit

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11
Q

Entropy reduction

A

Molecules randomly come together

Enzyme forces them to collide

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12
Q

Desolvation

A

Shield of stable water removed

Weak bonds replace these

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13
Q

Km

A

Substrate concentration at which the initial reaction rate is half of the maximum reaction rate

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14
Q

What does a large km mean?

A

Unstable

More reversing back

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15
Q

Vmax

A

How fast a reaction proceeds when enzyme saturated with substrate

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16
Q

Isoenzyme

A

Different proteins but catalyse the same reaction

17
Q

Glucokinase

A

Found in liver

High km and vmax

18
Q

Hexokinase

A

Found in other tissues

Low km and vmax

19
Q

2 ternary examples

A

Ordered eg pyruvate=>lactate

Random eg creatine=>phosphocreatine

20
Q

No ternary examples

A

Amino acid=>keto acid

Ping pong ball

21
Q

Competitive inhibitors (km and Vmax)

A

Increased km and unchanged Vmax

22
Q

Non competitive inhibitors (km and vmax)

A

Unchanged km and decreased v max

23
Q

Transition state analogue

A

Make an inhibitor that mimics transition state

24
Q

Catalytic antibodies

A

Antibody with a specific to transition state molecule

25
Concerted model
Only 2 conformations | Switch between each
26
Sequential model
No flipping, binding at one subunit causes change in the other subunits
27
Kinase
Add phosphoryl
28
Phosphatase
Remove phosphoryl
29
Proteolytic cleavage
Enzyme exists as inactive precursor which is cleaved to become active