Enzymes Flashcards

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1
Q

What are enzymes?

A

Large, globular proteins which act as Catalysts in metabolism

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2
Q

What 2 theories are used to explain how enzymes work?

A

Lock and key
Induced fit

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3
Q

What does induced fit suggest about the active site of an enzymes?

A

The active site alters its shape to be complement to the substrate

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4
Q

What is an enzyme substrate complex?

A

When the tertiary structure of the active site successfully binds to the substrate

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5
Q

How many reactions can an enzyme catalise and why?

A

Many as they are not permenantly damaged

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6
Q

What are intracellular enzymes? Give an example

A

Enzymes that work inside cells.
Catalase breaks down into hydrogen peroxide and water in the liver

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7
Q

What are extra cellular enzymes? Give an example

A

Enzymes that work outside of cells.
Trypsin breaks down proteins in the small intestine

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8
Q

How does temperature effect enzyme reactivity?

A

Enzymes and substrates gain kinetic energy and so collide more creating more enzyme substrate complexes

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9
Q

What happens if the temperature is above optimum on enzymes?

A

The enzymes tertiary structure denatures

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10
Q

What is the temperature coefficient and what is the equation?

A

The increase in rate of reaction as a result of increasing the temperature by 10 degrees celsius.

Q10 = R2 ÷ R1

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11
Q

What graph shape is made during enzyme reactions?

A

Bell curve

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12
Q

Describe the effect of PH on enzyme reactivity

A

Any movement away from optimum PH causes their to be an unbalanced level of H+ ions which causes the tertiary structure of the active site to denature

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13
Q

What is the PH of HCl

A

1 or 2

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14
Q

What does pepsin break down?

A

Large proteins in the stomach

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15
Q

What does pancreatic juice contain?

A

Trypsin madd in the gall bladder is alkali of 7.8

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16
Q

What is a limiting factor?

A

Something which prevents a reaction from continuing

17
Q

What does inhibition mean?

A

Stop / prevent

18
Q

What does inhibition mean?

A

Stop / prevent

19
Q

What is a competitive inhibitor?

A

Something that is also complementary to the active site but is not the substrate. They slow reactions but eventually reach v-max

20
Q

What is a non competitive inhibitor?

A

Something which binds to an alloseric site on the enzyme altering the shape of the active site so it is no longer complementary to the substrate. Doesn’t reach v-max

21
Q

What is end product inhibition?

A

When the product can stop or enhance production based on how much has already been produced

22
Q

What is a cofactor, coenzyme and prosthetic group?

A

Cofactor: inorganic protein bound to substrate

Coenzyme: organic protein bound to substrate

Prosthetic group: can be co factors or co enzymes

23
Q

What is a holoenzyme?

A

An enzyme containing a co factor or co enzymes

24
Q

What is a holoenzyme?

A

An enzyme containing a co factor or co enzymes