Enzymes I Flashcards

1
Q

what is the role of enzymes?

A

to catalyse specific chemical reactions

eg blood clotting, nerve conduction

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2
Q

what can enzyme defects lead to?

A

disease

eg glycogen storage disease

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3
Q

how are enzymes utilised?

A

they are targets for therapeutic drugs

  • antibiotics inhibit enzymes
  • anti inflammatory agents
  • anti cancer drugs
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4
Q

what are the properties of enzymes?

A
  • increase rate of reaction by 10 billion folds
  • shows specificity
  • unchanged at end of reaction
  • does not alter reaction eqm
  • lowers activation energy so less ΔG required
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5
Q

describe the structure and function of active sites

A
  • 3D cavity/cleft that binds to substrate w specificity through hydrophobic, H, electrostatic bonding and van de waal forces
  • formation of ES complex is first step of enzyme catalysis
  • seen through x ray crystallography and kinetic studies of enzymes
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6
Q

what is the michaelis constant?

A

measures the enzyme substrate affinity

-Vmax/2

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7
Q

what is Vmax?

A

the maximum velocity of saturation at the active sites

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8
Q

what is the michaelis-menton equation?

A

V = Vmax + ([S]/ ([S] + Km))

  • will give a exponential graph
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9
Q

what is the double reciprocal plot?

A

1/V = 1/Vmax + ((Km/Vmax) x (1/[S]))

  • gives a linear graph
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10
Q

What is the turnover number?

A
  • max number of substrate molecules handled per active site
  • also called Kcat:

Vmax/[enzyme]

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11
Q

what is a competitive inhibitor?

A

molecule that competes with substrate by binding to the active site of the enzyme

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12
Q

what happens in the presence of a competitive inhibitor?

A
  • Km increases
  • more substrate required to reach Km
  • Vmax stays same
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13
Q

what is a non competitive inhibitor

A

a molecule that binds to a different site to the active site

  • causes a conformation on enzyme
  • Vmax reduced but Km stays same
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14
Q

how is enzyme activity regulated?

A
  • control of gene expression
  • compartimentation: sequence of enzyme polypeptide chain target enzyme to ER to ensure that enzyme activity occurs in particular part of cell
  • allosteric regulation: regulatory molecule causes conformational change to reduce enzyme activity
  • covalent modification of an enzyme: changes enzyme shape
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