Enzymes Flashcards

1
Q

enzymes

A

enzymes are molecules that act as catalysts to speed up the rate of biological reactions by reducing activation energy

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2
Q

key info

A
  • often end in ASE
  • enzymes are proteins
  • enzymes are not consumed during the reaction, they are reusable
  • the compound on which an enzyme acts to the substrate (a molecule that an enzyme reacts with)
  • when a substrate binds to an enzyme an enzyme-substrate complex is formed
  • enzymes are substrate specific
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3
Q

Biochemical pathways

A

chemical reactions in cells take place in a series of steps, called biochemical pathways. Each step is controlled and regulated by a specific enzyme

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4
Q

Catabolic

A

when enzymes break a single structure into compartments (big to small)

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5
Q

Anabolic

A

join two or more substrate molecules together (small to big)

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6
Q

enzyme-substrate complex

A

the structure is formed when an enzyme and substrate are bound together

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7
Q

Enzyme active site

A
  • The substrate binds to an enzyme’s active site.
  • The shape of the active site is complementary to its substrate
  • Enzymes are substrate specific meaning an enzyme active site will fit with one type of substrate
  • enzymes shape of the active site is determined by the molecule’s tertiary structure
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8
Q

endothermic (endergonic)

A
  • endothermic reactions absorb energy from the surroundings and convert it to stored chemical energy
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9
Q

exothermic (exergonic)

A
  • exothermic releases energy to the surroundings through the conversion of stored chemical energy
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10
Q

effect of temp on enzymes

A
  • enzymes catalyse reactions fastest at their optimum temperature
  • at low temperatures, molecules move around slowly and the rate of collisions between enzymes and substrates reduces
  • at increasing temps molecules move faster and the rate of collisions increases
  • above optimum temp, enzymes denaturation occurs, and the shape of the enzyme changes, meaning substrates can no longer bind to the active site
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11
Q

Effects on pH on enzymes

A
  • Enzymes catalyst reactions fastest at their optimum pH
  • Extremes of pH (very acidic or alkaline) away from enzyme optimum can result in enzyme denaturation
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12
Q

Enzyme concentration

A
  • Rate of reaction continues to increase in enzyme concentration
  • This relationship assumes unlimited amount of substrate
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13
Q

substrate concentration

A
  • the rate of reaction increases and then plateaus with increasing substrate concentration. At the plateau, enzymes become saturated and are catalysing reactions at their fastest rate
  • this relationship assumes a fixed amount of enzyme
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14
Q

enzyme inhibitors

A

prevent the substrate from binding to the enzyme’s active site, deactivating the enzyme e.g drugs and toxins

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15
Q

Reversible inhibitors

A

are used by cells to control enzyme activity

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16
Q

Irreversible inhibitors

A

bind tightly and permanently to the enzymes destroying their catalytic activity

17
Q

competitive inhibitors

A

inhibitors block the substrate’s access to the active site. The shape of the inhibitor complements the active site allowing it to bind

18
Q

non-competitive inhibitors

A

inhibitors bind to another region of the enzyme (allosteric site), causing a change in the shape of the active site. May slow down or stop enzyme active

19
Q

co-enzymes

A

Co-enzymes are small organic non-protein molecules. They assist enzyme activity by binding to enzymes or by functioning as carriers of energy, electrons and protons. E.G) may vitamins work as coenzymes, cofactors have similar functions