Enzymes Flashcards

1
Q

What is an important enzyme for exercise?

A

Nitric oxide synthase: NO drives relaxation of arterial smooth muscle

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2
Q

How does the induced fit model work?

A

Enzyme puts pressure on bonds in substrate, and a slight conformational change of activation site is needed

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3
Q

What are cofactors?

A

Enable the enzyme to catalyse reaction; can be bound tightly or loosely

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4
Q

What are types of cofactors?

A

Coenzymes, metals, and vitamin derivatives (e.g. B vitamins)

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5
Q

What is the difference between loose and tight cofactors?

A

Loose bind to enzyme before reaction and are released after the reaction; tight remain bound all the time (e.g. Haem in Hb)

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6
Q

How do enzymes allow catalysis?

A

Enzyme reduces Eact of reaction; enzyme stabilises transition state

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7
Q

What type of enzyme reaction is more common: reversible or irreversible?

A

Reversible

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8
Q

Which type of enzyme reaction is a non-equilibrium reaction?

A

Irreversible

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9
Q

Why are irreversible enzymatic reactions important?

A

Essential to regulation of cell

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10
Q

What are five groups of enzymes?

A

Transferases; hydrolases; oxidoreductases; kinases; phosphotases

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11
Q

How can enzymes be classified?

A

By the group they fall under, and/or the specific reaction they catalyse

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12
Q

What do transferases do?

A

Catalyse group transfer

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13
Q

What do hydrolases do?

A

Catalyse hydrolysis

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14
Q

What do oxidoreductases do?

A

Catalyse redox

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15
Q

What do kinases do?

A

Catalyse phosphate addition

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16
Q

What do phosphotases do?

A

Catalyse phosphate removal

17
Q

What is initial velocity?

A

V0; the highest rate of an enzyme catalysed reaction; occurs when substrate is at its greatest and product at lowest; occurs at initiation of reaction

18
Q

What is maximal velocity?

A

Vmax; maximum possible initial rate of reaction

19
Q

What is Michaelis Constant?

A

Km; concentration of substrate which allows enzye to work at half Vmax; is a measure of substrate-enzyme affinity

20
Q

What is the significance of a higher Km?

A

Has lower affinity, so larger substrate is need to get Km

21
Q

Why do cells normally have substrate concentration lower than Km?

A

Enzymes are working below saturation/ Vmax; enables enzymes to respond to changes easily, increasing or decreasing velocity as needed

22
Q

What happens to Vmax and Km when enzyme concentration is increased?

A

Increases Vmax as Vmax is dependent on amount of enzyme; does not affect K as concentration of substrate is not affected as enzyme is in extreme excess

23
Q

What happens to Vmax and Km when substrate concentration is increased?

24
Q

How does temperature affect the rate of an enzymatic reaction?

A

Rate increases as temperature increases until denaturing; Q10 values quantify change in relation to temperature (typically is 2)

25
What is competitive inhibition?
Competitive chemcial occupies active site and prevents ESC formation
26
How can competitive inhibition be overcome?
Adding more substrate
27
How does competitive inhibition affect Vmax and Km?
No change in Vmax, but increases Km
28
What is non-competitive inhibition?
Binds to allosteric site of enzyme; interferes with ans stops enzyme function
29
How does non-competitive inhbition affect Vmax and Km?
Vmax decreases, but no change in Km
30
How can enzymes be regulated?
Covalent modification turns them on or off: addition and removal of molecules will change enzyme's conformation, causing increase or decrease in activity
31
What are common covalent modifications of enzymes?
Phosphorylation to a specific amino acid (~30%); acetylation; palmitoylation