module 2 - 2.1.4 - enzymes Flashcards

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1
Q

What are enzymes?

A

-globular proteins
-interact with substrates to make te reaction happen faster

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2
Q

meaning of activation energy?

A

the amount of energy needed to start a reaction

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3
Q

meaning of active site?

A

an area in the tertiary structure that has a specific shape that is complementary to the substrate.

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4
Q

What is the lock and key hypothesis?

A

1.only the specific substrate will fit into the complementary active site
2.this forms an enzyme-substrate complex
3.the substrate then reacts and forms products making a enzyme-product complex
4,products are then released leaving the enzyme unchanged

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5
Q

How does the enzyme hold the substrate to increase the rate of reaction?

A
  • held so the right atom groups are close enough to react
    -R groups of the active site will interact with the substrate forming temporary bonds
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6
Q

What is the induced fit hypothesis?

A

1, substrate enters active site with a weak interaction
2, forms an enzyme substrate complex
3,the weak interactions cause a change in the tertiary structure of the enzyme , this puts a strain on the substrates
4,this lowers the activation energy and products are released

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7
Q

How do enzymes increase the rate of reaction?

A

they lower the activation energy

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8
Q

What are intracellular enzymes?

A

enzymes that work in the cell

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9
Q

Two examples of intracellular enzymes?

A
  1. lactase= breaks down lactose into glucose and galactose

2.catalase= breaks hydrogen peroxide down into water and oxygen = found in plants and humans

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10
Q

Extracellular enzymes?

A

enzymes that work outside the cell that made them

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11
Q

Why are extracellular enzymes needed?

A

nutrients needs to enter cells but are too large so need to be broken down.
enzymes are released from the cell to break the nutrients down

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12
Q

Examples of extracellular enzymes?

A
  1. amylase= secreted by salivary glands, catalyses the hydrolysis of starch into maltose
    2.tryspin
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13
Q

Factors that impact enzymes?

A
  1. temperature
    2.PH
    3.enzyme concentration
  2. substrate concentration
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14
Q

What happens to the rate of reaction with enzymes when the temperature increases?

A

1,increases the kinetic energy of the particles
2,this makes the particles move more and collide more often
3,this will mean there are more successful collisions of substrates and enzymes
4,= an increased rate of reaction

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15
Q

What does temperature coefficient Q10 mean?

A

a measure of how much the rate of reaction increases with a 10 degree raise in temperature

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15
Q

What is denaturing?

A

1,at a high temp the bonds holding the protein (enzyme) together vibrate more
2,as the temp increases the bonds strain and eventually break
3, the breaking of the bonds change the shape of the tertiary structure
4,it is then denatured

16
Q

optimum temperature meaning?

A

the temperature where the enzyme has the highest rate of reaction

after the optimum temp enzyme denatures and rate of reaction decreases rapidly

17
Q

What are enzymes like that are meant to be in cold temps?

A
  • have more flexible structures
    = less stable
    -small temp changes can denature them
18
Q

What are enzymes like that are meant to be in hot temps?

A

=more stable
=more resistant to change of temps so less likely to denature

19
Q

What happens to the enzyme when the PH is not at the optimum?

A

active site is likely to change shape
=reduces rate of reaction

20
Q

What happens to rate of reaction if the conc of substrates or enzymes increases?

A

more successful collisions between the active sites and substrates so increase of rate of reaction

21
Q

What is the role of inhibitors?

A

To slow down a reaction so excess product is not made

22
Q

What are the two types of inhibitors?

A

1.competitive
2. non-competitive

23
Q

How does competitive inhibition work?

A

1.a similar shaped molecule to the active sire can fit into the active site
2.blocks the substrate from attaching to the active site
3.enzyme can not catalyse
4.substrates and inhibitors compete for the active site
5.reduce amount of substrates attaching to the active sire
=decrease in rate of reaction

24
Q

How do competitive inhibitors impact the rate of reaction?

A

=decreases rate of reaction

25
Q

Examples of competitive inhibitors?

A

-statins =reduces blood cholesterol levels
-aspirin=reduces chemical for pain

26
Q

How does non-competitive inhibition work?

A

1.the inhibitor binds to somewhere else other than the active site making a allosteric site
2.this causes tertiary of the enzyme to change changing the shape of the active site
3.substrates no longer complementary so cannot bind

27
Q

How do non-competitive inhibitors change the rate of reaction?

A

=decreases the rate of reaction as less available active sites

28
Q

examples of non-competitive inhibitors?

A

1.insectisides= needed for nerve impulses
2.proton pump= reduces production of excess acid in the stomach

29
Q

end - product inhibition?

A

This is when the products of an enzyme inhibit the enzyme that produced them

30
Q

Roles of cofactors?

A

transfer atoms/groups from one reaction to another by a pathway

31
Q

Whats a coenzyme?

A

when a cofactor is an organic molecule

32
Q

How are inorganic cofactors obtained?

A

via the diet through minerals
=iron,calcium,chloride

33
Q

How are coenzymes obtained?

A

via vitamins in the diet
=vitamin B3 , vitamin B5

34
Q

What are prosthetic groups?

A

=cofactors
=required for certain enzymes to carry out catalytic functions

35
Q

Are cofactors essential?

A

no

36
Q

are coenzymes essential?

A

yes

37
Q

whats a precursor activator?

A

an inactive enzyme

38
Q

What do precursor activators do?

A

temporarily bind to an enzyme and alter its active site