UNIT 1 (topic 4) proteins and enzymes Flashcards

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1
Q

what is a enzyme

A
  • a biological catalyst that lowers the activation energy of a reaction to speed up reactions
  • they are proteins, globular shaped
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2
Q

define the active site

A

specific 3D shape because of the tertiary structure that binds to the substrate

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3
Q

define the substrate

A

the reactants that are complementary to an enzyme

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4
Q

what is the lock and key theory

A
  • substrate and active site are complementary
  • when they bind, E-S complex is formed
  • reaction occurs and products are released from the active site
  • active site is free to bind to other complementary substrate
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5
Q

what is the induced fit theory

A
  • the binding of substrate causes the active site to change shape
  • active site becomes complementary forming E-S complexes
  • places stress on the bonds within the substrate - lowering the active site
  • forces a reaction to take place
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6
Q

what are the factors effecting enzymes

A
  • temperature
  • pH
  • concentration of enzymes
  • concentration of substrate
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7
Q

why does temperature increase enzyme rate

A
  • increases kinetic energy of enzymes and substrate
  • more collisions between substrate and active site
  • more E-S complexes formed
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8
Q

why does temperature decrease enzyme rate

A
  • high temperature causes the H-bonds in the tertiary structure to break
  • change shape of the active site meaning substrate no longer complementary
  • E-S complexes no longer form
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9
Q

how is rate affected at the optimum pH

A

more E-S complexes formed, increased rate

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10
Q

what is the rate above and below the optimum pH

A
  • changing pH affects concentration of H+ / OH-
  • Disrupts H-bonds and ionic bonds in the tertiary structure
  • changes shape of the active site
  • no longer complementary so E-S complexes can’t be formed
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11
Q

why does the rate increase as the concentration of enzyme/ substrate increases

A
  • more substrate/ active sites so higher chance of collisions
  • more E-S complexes formed
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12
Q

why does the rate plateaus as the concentration increases

A
  • enzyme/ substrate becomes the limiting factor
  • all is occupied so rate cannot increase further
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13
Q

define an enzyme inhibitor

A

substances that prevent the active site from binding to the substrate to prevent E-S complexes

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14
Q

how does competitive inhibitors prevent E-S complexes

A
  • inhibitor has similar shape to the substrate and bind to active site
  • physically prevents the binding of substrate and active site
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15
Q

how does the non- competitive inhibitors prevent E-S complexes

A
  • the inhibitor binds to an allosteric site in the enzyme
  • this alters the tertiary structure
  • changes shape of the active site
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16
Q

why does the non-competitive have decreased rate

A
  • increasing substrate concentration has no effect
  • inhibitor altered shape of the active site
  • no longer complementary
17
Q

why does the competitive have an increased rate

A
  • substrate and inhibitor are competing for the active site
  • increased collision for substrate at high concentration
18
Q

explain the primary structure of a protein

A
  • sequence of amino acids in a polypeptide chain
  • peptide bonds between the carboxyl group and amino group
19
Q

explain the secondary structure of a protein

A

folding of the polar peptide bonds creating a-helices or b-pleated sheets
- hydrogen bonds between the peptide bonds

20
Q

explain the tertiary structure of a protein

A

more folding of the a-helices and b-pleated sheets
- ionic, hydrogen and disulphide bonds between the R-groups

21
Q

explain the quaternary structure in a protein

A

multiple polypeptide chains bonded together or a polypeptide chain bonded to a prosthetic group
- ionic, hydrogen and disulphide bonds between the chain’s R-groups

22
Q

what is a prosthetic group

A

a non protein e.g. iron

23
Q

how do you find the rate of reaction on a graph

A

Change in y (amount of product) /
Change in x (time)