ML6: Stage I & II catabolism Flashcards

1
Q

What are the classes of lipids?

A
  • Fatty acid derivatives
    • Fatty acids – fuel molecules
    • Triacylglycerols – fuel storage and insulation
  • Hydroxy-methyl-glutaric acid derivatives
    • Ketone bodies (C4) – water soluble fuel molecules
  • Vitamins
    • A, D, E, and K
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2
Q

What are triacylglycerides (TAGs)? Are they (overall) hydrophobic, amphipathic, or hydrophilic?

A

Major dietary and storage lipids

Consist of three fatty acids esterified to glycerol

Overall hydrophobic

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3
Q

What happens to dietary lipids?

A
  1. Lipids are emulsified in the small intestine
    Bile salts
  2. Digestion of lipids by lipases
    TAGs – digested by pancreatic lipase
    Cholesterol esters – digested by cholesterol esterase
    Phospholipids – digested by phospholipases
  3. Absorption by intestinal mucosal cells
  4. Transportation to tissues
    Consumer tissues – fatty acid oxidation
    Adipose tissue – storage
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4
Q

Give an overview of fatty acid catabolism (β-oxidation).

A
  • Occurs in mitochondria
  • FA cycles through sequence of reactions
  • C2 removed at each cycle
  • 1 NADH and 1 FADH2 produced in each cycle
  • All intermediates linked to coenzyme-A
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5
Q

Give the stages of fatty acid catabolism (β-oxidation).

A
  1. Activation of fatty acids
    Occurs in the cytoplasm
    FA actiated by linkage to coenzyme-A
    Catalysed by acyl CoA synthetase
    fatty acid + coenzyme A → fatty acyl CoA
  2. Transport of fatty acyl CoA into mitochondria
    Fatty acyl group linked to carnitine
    Transported across the membrane by translocase protein
    Fatty acyl CoA reformed in the matrix
    Rate limiting step for faty acid oxidation
  3. Oxidation of fatty acyl CoA
    A series of four reactions
    1 NADH, 1 FADH2 and 1 acetyl-CoA are generated in each round
    Each round shortens the chain by two carbon atoms
    Cycle continues until only acetyl-CoA remains

Overall: released 106 molecules of ATP

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6
Q

What are essential amino acids? Name them.

A

Amino acids that cannot be synthesised

His, Ile, Leu, Lys, Met, Phe, Thr, Trp, Val

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7
Q
A
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8
Q

What are the stages of digestion and absorption of proteins?

A
  • Dietary protein digestion begins in the stomach
    • Denaturation
    • Pepsin
  • Further digestion in the lumen of the intestine
    • Chymotrypsin, trypsin, carboxypeptidase – pancrease aminopeptidase
  • Transport into intestinal cells and into blood
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9
Q

What happens to excess amino acids? Why and how?

A

They cannot be stored so have to be degraded

  • Transfer of amino group to α-ketoglutarate
    Uses aminotransferases
  • Dehydrogenation to produce ammonium ion
    Uses glutamate dehydrogenase

e. g. aspartate + α-ketoglutarate produces oxaloacetate and glutatamate
e. g. alanine + α-ketoglutarate produces pyruvate + glutatamate

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10
Q

How are ammonium ions removed?

A

The urea cycle

Toxic NH4+ is converted to urea and excreted

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11
Q

Are proteins produced for a specific function or synthesised as a store of excess amino acids?

A

They are produced for a specific function

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12
Q

How can energy be provided during starvation?

A

By breaking down muscle

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13
Q

Explain the nitrogen balance.

A

Positive nitrogen balance
Intake of nitrogen (protein) > loss
During active growth, pregnancy, tissue repair

Negative nitrogen balance
Intake of nitrogen (protein) < loss
During starvation

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