C1.1 Enzymes & Metabolism Flashcards

(32 cards)

1
Q

What are enzymes?

A

specialized, globular proteins which catalyse the chemical reaction by lowering its activation energy

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2
Q

Active site

A

region on the enzyme designed for only one other substance to fit

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3
Q

Catalytic site

A

where the catalysis happen

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4
Q

Binding site

A

recognizes substrate and ensures the correct subtrate fits into the active site

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5
Q

What is enzyme-substrate specificity?

A

ability of the enzyme to recognize and bind to specific substrate

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6
Q

What is induced fit bonding?

A

the active site changes its shape (conformational change) so substrate will fit better

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7
Q

What is transition state?

A

The point of energy that must be reached for reaction to happen

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8
Q

Activation energy

A

energy needed to reach transition state

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9
Q

What type of reaction is formation of bonds? (exo/endo)

A

exothermic

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10
Q

What type of reaction is breakdown of bonds? (exo/endo)

A

Endothermic

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11
Q

Metabolism

A

all chemical reactions taking place in the body that build or break the molecules

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12
Q

Anabolic reaction (e.g. peptide bond formation)

A

building molecules up, monomers build up to form polymers

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13
Q

Catabolic reaction (e.g. digestion)

A

breaking down the molecules

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14
Q

Active sites and substrates function via ______ and _____

A

molecular motion, collision

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15
Q

What factors affect the rate of enzyme activity?

A

temperature, pH, substrate concentration

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16
Q

How temperature affects the rate of enzyme activity?

A

in higher temperature (up to 37 C), molecules move faster and bump into each other more often

17
Q

How pH affects the rate of enzyme activity?

A

enzymes work better in different range of pH, but any shift from this range decreases the rate

18
Q

What are the main properties and structure of enzymes?

A
  • globular proteins
  • soluble
19
Q

What are extracellular enzymes and how are they produced?

A

used outside the cell, produced by ribosomes on rough ER and then modified and packed into vesicles in Golgi to be released through cell membrane

20
Q

What are intracellular enzymes and how are they produced?

A

used within the cell and produced by free ribosomes in cytoplasm

21
Q

What is non-competitive inhibition?

A

when a substance binds to the allosteric site and change the shape of the active site making it impossible for the substrate to bind

22
Q

What is an allosteric site?

A

regulatory site as binding there changes thr enzyme

23
Q

What is competitive inhibition?

A

when a competitor with similar shape to the substrate binds to active site, blocking it

24
Q

How do warm-blooded animals use heat generated from metabolic reactions?

A

to maintain body temperature

25
What are statins?
example of competitve inhibitor that inhibit the enzyme that produces cholesterol
26
What is end-product inhibition?
final product becomes a non-competitve inhibitor of the first enzyme in the chain
27
What's the function of end-product inhibition?
it prevents a build up of the final product
28
What's the example of end-product inhibition?
threonine (enzyme) to isoleucine (product)
29
Compare competitive and non-competitve inhibition
30
What is mechanism-based inhibition?
inhibitor binds permanently to the active site by covalent bond
31
What the example of mechanism-based inhibition?
- treatment for HIV (AZT) - penicillin
32
How penicilin works?
it binds to an enzyme transpeptidase in the bacterial cell wall that makes the cell wall and cause it to burst