Seminar 8: Enzymes & Energy Flashcards

1
Q

what is the catalytic unit

A

polypeptide in quaternary structure with the active site

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2
Q

what is the regulatory unit?

A

polypeptide in quaternary structure with the allosteric site

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3
Q

why does reaction rate speed up as sites become sequentially activated? (Enzymes w/ subunits w/ own active sites)

A

when enzymes have multiple subunits w/ active sites:
1. binding to 1 active site causes ALLOSTERIC effects (slight change in protein structure)
2. this influences the adj subunit, making it MORE LIKELY to bind to substrate

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4
Q

how does a cell stop a metabolic pathway if they no longer need a product?

A
  1. have the final product of the pathway inhibit the enzyme that catalyses the commitment step (often allosterically, non-competitive inhibitor)

AKA feedback inhibition/end-product inhibition

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5
Q

the synthesis of cholesterol involves a biochemical pathway that begins w/ HMG-CoA reductase. Statins are drugs that are widely used to inhibit cholesterol synthesis/ How do you suppose statins work?

A
  • statins bind to the enzyme, inhibiting it
  • substrate can no longer bind, prevents enzyme from catalysing the reaction
  • pathway to synthesise cholesterol cannot progress, decreases synthesis
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6
Q

how to inactivate most enzymes after they’ve been activated?

A
  • reverse phosphorylation
  • protein phosphatase catalyse hydrolysis & removal of phosphate grp so that enzyme is inactive again
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7
Q

inside the cell, pH of cytosol ~ 7.2, but in lysosome ~ 4.8. A protease which catalyses hydrolysis of proteins is active w/in lysosome but inactive in cytosol. How can this occur?

A
  1. Due to compartmentalisation, different parts of a cell can have different internal environ
  2. protease has an optimal pH range w/in acidic conditions therefore it can only func in pH<7
  3. in the cytosol, protease would denature, there would be a change in its 3D tertiary shape due to change in ionisation of R-grps &/or carboxyl & amino grps
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8
Q

what happens to carboxyl grps in neutral/basic pH?

A

COOH looses H+ & becomes COO-

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9
Q

what happens to amino grps in neutral/acidic pH?

A

NH2 accepts H+ & becomes NH3+

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10
Q

how are polysaccharides broken down for energy?

A
  1. hydrolysed to glucose
  2. glucose passes through glycolysis & cellular respiration
  3. energy captured as ATP
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11
Q

how are lipids broken down for energy?

A
  1. hydrolysed into F.A & glycerol
  2. Glycerol converted to dihydroxyacetone phosphate (DHAP) - intermediate in glycolysis
  3. F.A reduced to molecules that are converted to acetyl CoA - in mitochondrion, by series of oxidation enzymes (beta-oxidation)
  4. Acetyl CoA enters citric acid cycle, catabolised to CO2
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12
Q

how are proteins broken down for energy?

A
  1. hydrolysed into A.A
  2. feed into glycolysis or citric acid cycle @ diff points depending on their structures
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13
Q

what is gluconeogenesis

A

metabolic process that creates glucose from non carbohydrate sources (A.A, glycerol etc)

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14
Q

what is Acetyl CoA form?

A
  • pigments
  • plant growth substances
  • steroid hormones
  • rubber
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15
Q

how to regulate each step in a biochemical pathway?

A
  1. changing amount of active enzyme : cell can increase expression of gene encoding an enzyme
  2. changing enzyme activity by covalent modifications : adding phosphate grps by kinase can alter enzyme activity
  3. feedback inhibition : final product allosterically binds to enzyme, inhibits it
  4. substrate availability : if substrate used by another enzyme, 1st one can’t function anymore, pathway shuts down
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