C4: Enzymes Flashcards

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1
Q

what are cofactors

A
  • an additional non protein molecule is an enzyme that doesn’t take part in the reaction
  • so it isn’t used up
  • allows for EZ-SS reaction to occur by keeping the EZ and SS bonded together
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2
Q

one group of cofactors are called PROSTHETICS. explain what they are.

A

_ tightly bound together and a permanent part of the enzyme

  • contributes to the 3D structure of the enzyme = it’s a vital property
  • can be organic (eg. vitamins) or inorganic (eg. metal ions)
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3
Q

one group of cofactors are called COENZYMES

A
  • theyre cofactors with organic molecules (eg. vitamins) only in their structure
  • they only bond for a short period of time = loosely bound and easily released
  • they’re changed in some way after the reaction but can be reused again
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4
Q

what are inactive precursor enzymes

A

enzymes that are made in an inactive form and can either cause damage within the cells, or can only be activated under certain conditions and needs to be controlled.

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5
Q

to activate a precursor enzyme ….. by …

A

.. they need to undergo a change in their shape (tertiary) by adding a cofactor

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6
Q

define enzymes

A

biological catalysts that speed up chemical/metabolic reactions by lowering the Ea

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7
Q

levels of temperature on enzyme activity (on a graph)

A

(A/N: should memorise/do the graph)

  • peak of graph = optimum temperature, the maximum rate of reaction
  • low temp, aka inactive = EZ don’t have much KE so they move very slowly.
  • too high temp = EZ are denatured, so the active site is destroyed and SS no longer fits.
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8
Q

how temperature rise affects enzyme activity

A
  • temperature rise = rise in KE, so particles collide more frequently = more successful collisions between SS and EZ = higher reaction rate
  • but TOO HIGH temperature = molecules vibrate more = H bonds and ionic bonds break down = changes the active site of the EZ and less EZ SS complexes form = rate lowers and EZ completely denatures
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9
Q

on an enzyme graph Q10 = how rate increases with a 10ºc increase. what is the formula for this

A

Q10 = rate of reaction @ (x+10)º/ rate of reaction @ (x)º

Q10 is usually 2-3

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10
Q

how pH affects enzyme activity

A
  • all enzymes have different optimum pH
  • TOO MANY H+ ions (protons) interact with the polar groups in the amino acids and the H bonds + ionic bonds holding the tertiary structure = active site of EZ changes = SS can’t fit anymore
  • NOT ENOUGH H+ ions means there aren’t enough interactions = loses the shape of active site
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11
Q

how enzymes catalyse intracellular and extracellular reactions

A

intracellular: occurs inside the cell that produces the enzyme, eg.
extracellular: nutrients in the form of proteins and polysaccharides need to be broken down to enter the cells

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12
Q

describe the lock & key theory

A
  • only a specific substrate will fit into the active site of an EZ b/c they’re exactly complementary
  • when the SS binds to the EZ it forms a EZ-SS complex, the SS reacts and products are formed in a product-SS complex, lowering the activation energy
  • the products are released, leaving the EZ unchanged so it can react again
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13
Q

describe induced fit theory

A
  • SS collides with complementary active site. EZ is flexible and conforms to the shape of SS so the active site fits closer
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14
Q

what part of the enzyme mechanism lowers the activation energy

A

the formation of an enzyme substrate complex

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15
Q

what 5 factors affect the rate of enzyme reactions

A
  1. pH
  2. substrate concentration
  3. enzyme concentration
  4. temperature
  5. inhibitors concentration
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