2.4 enzymes Flashcards

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1
Q

Definition of an intracellular enzyme

A

they are produced and function inside the cell

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2
Q

Definition of an extracellular enzyme

A

secreted by cells and catalyse reactions outside of the cell

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3
Q

Induced fit hypothesis

A
  • the enzyme and the active site change shape slightly as the substrate molecules begins to enter the enzyme
  • these changes are known as conformational changes
  • they ensure an ideal binding arrangement is achieved
  • this maximises the ability of it to catalyse reactions
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4
Q

Why at high levels of pH do enzymes become denatured?

A
  • hydrogen and ionic bonds hold together the tertiary structure of the protein together
  • below or above optimum pH an excess of H+ ions or OH- ions can build up causing the bonds to break
  • the broken bonds change the shape of the active site so eventually enzyme substrate complex’s can no longer form
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5
Q

Why are buffer solutions used in experiments

A
  • they maintain a specific pH even if the reaction would otherwise change the pH
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6
Q

What is the temperature coefficient

A

the ratio between the rates of that reaction at two different temperatures

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7
Q

Equation for the temperature coefficient

A

Q10= rate of reaction at x+10 / rate of reaction at x

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8
Q

What is a competitive inhibitor

A

they have a similar shape to that of the substrate molecule

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9
Q

What is a non-competitive inhibitor

A

bind to the allosteric site which alters the shape of the active site preventing the substrate from binding to it

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10
Q

How to reverse increased competitive inhibitor concentration

A

increasing the substrate concentration as that means they are more likely to collide with enzymes

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11
Q

How to reverse increased non-competitive inhibitor concentration

A

increasing substrate concentration will NOT do anything as the active site has already changed shape

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12
Q

Process of end-product inhibition

A
  1. as the enzymes convert the substrate into product, the process is slowed down as the end-product of the reaction chain binds to an allosteric site
  2. the end product can then detach and be used elsewhere allowing the active site to reform
  3. this means as the product falls the enzyme catalyses the reaction once again in a CONSTANT FEEDBACK LOOP
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13
Q

How to inhibitors form irreversible reactions

A

form covalent bonds with the enzymes

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14
Q

Why are irreversible inhibitors dangerous

A

their biological reaction the enzyme is catalysing will be completely stopped

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15
Q

Definition of cofactor

A

inorganic ions that an enzyme needs in order to function
minerals
non-protein

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16
Q

Role of a cofactor

A

stabilise the structure of the enzyme or they may take part in the reaction at the active site

17
Q

Definition of coenzyme

A

large organic cofactors
vitamins

18
Q

Role of a coenzyme

A

carry electrons or chemical groups between enzymes, aiding catalysis
found at/in the active site (can be permanently bound to the active site)

19
Q

Definiton of a prosthetic group

A

permanent part of the enzyme structure to that they assist

20
Q

Role of a prosthetic group

A

help to form the final 3D shape of the enzyme