Enzymes Flashcards

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1
Q

What are enzymes

A

biological catalysts

They speed up chemical reactions without being used up themselves

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2
Q

Why are enzymes so remarkable

A

They can be specific for really extreme environments

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3
Q

How do enzymes structure determine their function

A

Some enzymes need cofactors
Enzymes shape must be specific in order for it to function

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4
Q

What is the active site

A

A specific area that consists of about 6-10 amino acids.

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5
Q

What decides the shape of the active site

A

The tertiary structure of its amoino acids

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6
Q

What are intracellular enzymes

A

Enzymes that work within the cells of organisms

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7
Q

What is a metabolic pathway

A

a sequence of reactions each catalysed by a different enzyme that results ins. product

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8
Q

what are extracellular enzymes

A

Enzymes that work outside of the cell

eg:amylase and pepsin

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9
Q

That is a prosthetic group

A

A perementantly bound cofactor

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10
Q

What is a cofactor

A

A small non protein molecule that attaches to an enzyme and aids its function

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11
Q

What is an example of a prosthetic group

A

Zinc ions in carbonic anhydrase (found in red blood cells)

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12
Q

What is a coenzyme

A

Small ORGANIC non protein molecules that bind to en enzyme and aid its function

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13
Q

What is a common source of co enzymes

A

Vitamins

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14
Q

What is the lock and key hypothesis

A

The idea that only a certain enzyme and substrate work together
Just like how only one lock works with a key

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15
Q

How does the lock and key theory work ( enzyme action )

A

The substrate molecule fits into the complementary active site,
Temporary hydrogen bonds form between the enzyme and the substrate forming an enzyme substrate complex
The molecules that may have Been joined or split leave the active site, breaking the temp bonds

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16
Q

What is the induced fit hypothesis

A

When the substrate molecule’s fit into the active site, the active site changes shape slightly to mould its self to the substrate. Its like putting on a glove
A glove that’s too small or only has 4 fingers won’t fit but most gloves do

17
Q

How do enzymes speed up reactions

A

They lower the activation

18
Q

How does heat effect enzyme action

A

As heat increases, molecules have more Ke and therefore more successful collisions with sufficient energy occur

But after point the enzymes active site denatures and this stops reaction completely

An optimum temperature is just before denaturing occurs

19
Q

What is Q10

A

rate of reaction at t+10 / rate of reaction at t

Usually 2

20
Q

What is pH

A

indicates weather a substance is acidic or alkali

21
Q

What is a buffer

A

a substance that resists change to pH

22
Q

How can pH change enzyme action

A

pyramid shape, moving the pH away from the optimum reduces reaction rate because the conc of H+ ions affects the tertiary structure of the enzyme molecule

23
Q

How do different enzymes have different optimum temps

A

Differing amounts of disulphide bridges

24
Q

What is the effect of changing substrate conc on rate of reactions

A

increases rate until V max is reached (when each enzyme is filled) at this point adding more has no effect

25
Q

What is the effect of changing enzyme conc on rate

A

increases rate until V max is reached (when each substrate is used) at this point adding more has no effect

26
Q

What is enzyme degradation

A

When the enzyme molecules are degraded into their amino acids and used to synthesise new ones

27
Q

What is competitive inhibition

A

Substances whose molecules have similar shapes to substrate and therefore fir into the active site
This stops the enzyme from functioning

28
Q

What happens to the rate of reaction if you increase sub conc with competetive inhibition

A

Increases rate of reaction as there is higher proportion of substrate compared to inhibitor therefore increasing the probability of a substrate reaching the enzyme

29
Q

What is non competitive inhibition

A

They are molecules that bind alleosterically and prevent the enzyme from functioning by changing the active site shape

30
Q

What is end product inhibition

A

When one of the products of the enzyme substrate complex stays tightly bound and stops further action from occurring

31
Q

what is cyanide

A

KCN is a highly toxic poison as it inhibits aerobic respiration.

32
Q

Green mamba venom

A

Binds to neuromuscular synapses and causes muscles to stay contracted, leading to suffocation

33
Q

Aspirin

A

Salycidic acid binds to enzymes that catalyse the formation of prostoglandins. These are cell signalling molecules that are used on pain response.

34
Q

ATPase inhibitors (foxgloves)

A

Allow more calcium ions to enter muclular cells. This increases the strength of muscle contraction

35
Q

ACE inhibitor

A

lowers high blood pressure

36
Q

Protease inhibitor

A

Prevent the reproduction of virus’ within host cells

37
Q
A