Enzyme Flashcards

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1
Q

What are enzymes

A
  • tertiary structuere proteins and so are a very specific 3d shape
  • includes active site held by peptide , hydrogen, ionic and disulphide bonds
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2
Q

What is the locke and key theory

A
  • in this theory of enzyme action a successful collision has the substrate fit exactly into active site of the enzyme forming an enzyme subtrate complex
  • reaction occurs and products are release
  • enzyme remains unchanged at the end of the reaction
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3
Q

What is the induced fit theory

A
  • alternative theory of enzyme action
  • lysozyme is propoed to function in this way
  • active site and substrate are not fully complementary in shape
  • reactive groups in theses areas align and the substrate forces it way into the active site
  • both areas change structure slightly the bonds in the substrate weakens ad the reaction occurs at a lower activation energy
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4
Q

What are intracellular enzymes

A
  • these work inside cells
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5
Q

What are extracellular enzymes

A
  • secreted from cells for use outside the cell
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6
Q

How does low temperature affect enzymes

A
  • at low temperatures there is a low kinetic energy and so few successful collisions where the substrate i able to enter the active site of the enzyme and form products
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7
Q

How does high temperatures till opimum affect enzymes

A
  • as the temperature increases the kinetic energy increases
  • more collissions and the enzyme subsstrate complexes formed per unit of time leading to increased producct
  • continues up to an optimum temperature
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8
Q

How does temperatures above optimum affect enzymes

A
  • kinetic energy increases
  • vibrations in enzymes weaken some bonds holding tertiary structure of active site together
  • active site loses the shape and substrate is no longer complementary to active site no further enzyme substrate complexes can be made and enzyme said to be denatured
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9
Q

How does substrate concentration affect enzymes

A
  • as enzyme reaction relies on successful collissions between enzymes any increase in substrate concentration will increases collisions and rate of reaction
  • low substrate concentrations it is this factor that is limiting the rate of reaction increaseing the substrate concentration increase the rate of raction
  • at some point any further increase in substrate concentration has no effect as it platus as all the enzymes have full active sites at any one time
  • enzyme concentration is now the limiting factor
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10
Q

What are competitive inhibitors

A
  • are complementary in shape to the active site of the enzyme
  • therfore prevent the formation of enzyme substrate complexes by blocking the active site
  • do not bind permanently
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11
Q

What are non competitive inhibitors

A
  • bind to the enzyme away from the active site at the allosteric site
  • alters the shape of the active site so no enzyme substrate complexes can be formed
  • some inhibitors bind reversible others bind irreversibly
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12
Q

What do enzymes do

A
  • enzymes are catalysts whcih mean they lower the activation energy of reactions but remain unchanges in the reaction
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13
Q

How does pH affect enzymes

A
  • most enzymes have an optimum pH
  • small changes from the optimum either above or below optimum pH make small reversible changes in the enzyme reducing efficiency
  • large changes in ph can disrupt ionic and hydrogen bonds in the enzyme causing permanenet changes to the shape of the active site
  • prevent the formation of enzyme substrate complexes
  • denaturing the enzyme
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14
Q

How does enzyme concentration affect enzymes

A
  • assuming excess substrate any increase in enzyme concentration increases the rate of reaction as more active sites are available for reactions
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15
Q

What is metabolism

A
  • anabolic reactions - building up molecule
  • catabolic reaactions - breaking down of molecules
  • catalysed by enzymes
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16
Q

What are immobolised enzymes

A
  • enzymes can be attatched to an inert matrix such as cellulose microfibrils or sodium alginate beads
  • used in bioensors and to create lactose free milk
17
Q

What are advantages of immobolised enzymes

A
  • increased stability so will denature high temperature and can be used efficiently over a wider range of pH
  • products uncontaminated with enzyme
  • enzymes easily added and removed therefore giving control over reactions alternativley recovered for reuse
18
Q

How do inhibitors affect the rate of reaction of enzymes

A
  • as competitive inhibitors compete with substrate for the active site any increase in substrate concentreation will decrease the effect of the inhibitor as the substrate will collide more often than the inhibitor with the active site of the enzyme
  • increasing the substrte concentration increases the rate of reaction but some of the enzyme is always affected so rate is lower than it would be without the inhibitor