Enzymes Flashcards

(41 cards)

1
Q

properties of enzymes:

A
  • biological catalysts
  • are precisely shaped 3D proteins made by protein synthesis (includes active site which is precisely shaped to bind with/be complementary to enzymes target molecule or substrate)
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2
Q

what can enzymes be specific to?

A
  • a single substrate molecule
  • or a group of similar reactions or substrates
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3
Q

example of how enzymes can be specific to a single molecule:

A

they can tell the difference between two isomers and only fit and have an effect on 1 of them
so glucose oxidase can recognise a-glucose but not b-glucose since they are different SHAPED molecules

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4
Q

example of how enzymes can be specific to a group of similar reactions or substrates:

A

'’group specificity’’ e.g. an enzyme may recognise and break any peptide bond

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5
Q

why are enzymes produced in small concentrations

A

because they are reusable

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6
Q

what is enzyme action effected by

A

extreme temperature and extreme pH - if their active site is changed, they will denature; will no longer fit with target substrate so no enzyme-substrate complex is formed - they won’t form a product

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7
Q

Are enzymes fast working?

A

Yes;1 enzyme molecule may catalyse 1000s reactions/second

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8
Q

are enzymes intracellular or extracellular

A

can be both

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9
Q

What is anabolism?

A

The sequences of reactions building larger molecules
(Enzymes catalyse reactions which turns smaller molecules into larger ones in condensation reactions)

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10
Q

What is catabolism?

A

Sequence of reactions producing smaller molecules - large molecules into smaller ones in hydrolysis reactions which turns

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11
Q

What is metabolism

A

Sequence of reactions that includes building up and breaking down steps

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12
Q

Enzyme substrate complex

A
  • binding of substrate to enzyme
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13
Q

What is activation energy?

A

Level of energy required for a reaction to occur- is the energy barrier that has to be overcome for the reaction to occur

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14
Q

What do enzymes do to activation energy?

A

Reduce the activation energy required
Frequency of reactions will increase as less energy is required

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15
Q

Sequence of events in an enzyme controlled reaction:

A
  • substrate binds to enzyme at active site to produce enzyme (substrate complex)
  • whilst attached change occurred to the the substrate to produce the product
  • enzyme and product will separate
  • active site is now empty and available again (enzymes are reusable)
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16
Q

Why might the enzyme and product separate?

A

The changed product isn’t strongly attached to the enzyme as the substrate was

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17
Q

Why may the substrate change?

A
  • fitting active site - slightly change shape of substrate (breaks bonds) produces small molecules from larger ones
  • AS may contain charged areas - changes in charge distribution
  • when 2 molecules enter active site - pressed together - forms bonds between molecules - producing larger molecules from smaller ones
18
Q

Lock and key hypothesis

A

Substrate and active site are complementary and they fit or bind to make the enzyme - substrate complex

19
Q

Induced fit hypothesis

A

Substrate and active site aren’t complementary but when they come together the active site changes shape to become complementary and fit or bind

20
Q

What are the two types of enzyme inhibition

A

non competitive and competitive inhibitors

21
Q

what are competitive inhibitors

A

molecules that are structurally similar to normal substrate of the enzyme, so they can enter the active site

22
Q

what happens if the active site is occupied by a competitive inhibitor?

A

normal substrate cannot enter the active site

23
Q

what happens if the competitive inhibitor binds permanently?

A

enzyme activity is lost since the substrate cannot bind to the active site
if it binds temporarily, the enzyme activity is reduced

24
Q

what do non-competitive inhibitors do, and what happens?

A

do not bind to active site so they do not compete with the substrate
instead they bind to the allosteric site, causing the active site to change shape
substrate cannot fit active site, so the enzyme will not work

25
examples of non-competitive inhibitors
heavy metals such as mercury and silver
26
examples of competitive inhibitors
- statins: competitive inhibitors of an enzyme in cholesterol synthesis so reduce blood cholesterol - aspirin: binds permanently and irreversible inhibits enzymes involved in the sensation of pain, so aspirin reduces pain
27
how does temperature effect enzyme activity?
as temp increases, particles have more energy, move faster, collide more frequently - rate of reaction increases
28
how does pH effect enzyme activity?
as pH moves away from optimum, enzymes denature and rate of reaction decreases lower pH (acidic) = more H+ present = R groups interact = bonds break = active site changes shape = > denature
29
why do some enzyme groups need a non-protein component
because amino acids can't perform all necessary catalytic tasks
30
what is a cofactor
organic OR inorganic non-protein substance required for an enzyme to work e.g Fe2+
31
what is a coenzyme?
specific organic molecule often derived from vitamins, and acts as a carrier for chemical groups or electrons between molecules
32
example of a coenzyme in action
vitamin B3 used to form NAD, a coenzyme in transfer of H+ between molecules in respiration and NADP
33
what are prosthetic groups?
non-protein and more tightly bound to enzymes to allow them to carry out their function - Zn2+ is part of carbonic anhydrase, found in RBC's in carbon dioxide carriage
34
why do precursor enzymes don't work until activated
don't work until activated as they may damage the site of synthesis
35
what might the change in precursor activation might be triggered by (examples)?
another enzyme e.g. protease that breaks bonds and changes 3D shape pH temperature tertiary structure
36
what does vitamin K do?
vitamin K activates factor X - factor X activates prothrombin to thrombin - thrombin breaks the soluble fibrinogen into fibrin monomers - fibrin then creates fibrin threads and this creates blood clots
37
active transport definition:
movement of molecules or ions from low concentration to high concentration against the concentration gradient. Therefore it requires energy as ATP. Requires carrier proteins
38
ATP def
Adenosine triphosphate - is a high-energy molecule that stores and provides energy for cellular processes in all living organisms.
39
Is active transport selective?
The carrier protein only binds to a specific molecule to be transported e.g. Na+ and glucose are transported together by a specific carrier protein
40
Why do cells that highly rely on active transport have more mitochondria than expected?
because they make ATP/release energy
41
What is end product inhibition?
- respiration of glucose requires the enzyme PFK and produces ATP - ATP completely inhibits PFK - high ATP means more can bind to allosteric site of PFK - second phosphate cannot be added to the glucose (glucose isn't broken down as fast - less ATP is made - low ATP as it is used up - less binds to the allosteric site of PFK - second phosphate can be added to the glucose - more glucose is broken down and more ATP is made