Leyland 6 stage 2 Flashcards

1
Q

LIPIDS

A

• Structurally diverse
• Generally insoluble in water (hydrophobic)
• Most only contain C, H, O
(phospholipids contain P, N)
• More reduced than carbohydrates release more energy when oxidised

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2
Q
  1. Fatty acid derivatives:
A
  • Fatty acids – fuel molecules.
  • Triacylglycerols – fuel storage and insulation
  • Phospholipids – components of membranes and plasma lipoproteins
  • Eicosanoids – local mediators
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3
Q
  1. Hydroxy-methyl-glutaric acid derivatives (C6 compound):
A
  • Ketone bodies (C4) – water soluble fuel molecules
  • Cholesterol (C27) – membranes and steroid hormone synthesis
  • Cholesterol esters – cholesterol storage
  • Bile acids and salts (C24) – lipid digestion
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4
Q
  1. Vitamins
A

• A, D, E and K.

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5
Q

What are triacylglycerols?

A

(triglycerides, TAG)
• major dietary and storage lipid
• consist of 3 fatty acids esterified to glycerol
• hydrophobic

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6
Q

Fatty Acids

A

CH3(CH2)nCOOH
where n = 14 - 18 (ie 16 - 20 C in total)
• saturated or unsaturated ( ie one or more double bonds C=C)
• amphipathic (contain hydrophilic & hydrophobic groups)
• certain polyunsaturated FA are essential (ie cannot be synthesized) (because mammals cannot introduce a double bond beyond C9) eg linolenic acid 18 : 3 (9,12,15)

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7
Q

Dietary lipids

1. Lipids are emulsified in the small intestine

A
  • bile salts
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8
Q
  1. Digestion of lipids by lipases
A
  • TAGs - digested by pancreatic lipase
  • cholesterol esters - digested by cholesterol esterase
  • phospholipids - digested by phospholipases
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9
Q
  1. Absorption by intestinal mucosal cells
A

lumen: triacyglycerides + lipases -> fatty acids & monoacylglycerols

to

Mucosal cell

-> tiracyglycerides

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10
Q
  1. Transportation to tissues
A
  • consumer tissues - fatty acid oxidation
    • adipose tissue - storage
  • consumer tissues
    TAG broken down by lipases to release free FA and glycerol
  • fatty acid oxidation
  • adipose tissue
  • storage
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11
Q

Fatty acid catabolism (b-oxidation)

A
  • occurs in mitochondria
  • FA cycles through sequence of reactions
  • C2 removed at each cycle
  • 1 NADH, 1 FADH2 produced in each cycle
  • all intermediates linked to coenzymeA (FA activation)
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12
Q

Fatty acid catabolism (b-oxidation)

1. Activation of fatty acids

A
  • Occurs in the cytoplasm
  • FA activated by linkage to coenzyme A
  • Catalysed by acyl CoA synthetase

fatty acid + coenzyme A -> fatty acyl CoA

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13
Q

Fatty acid catabolism (b-oxidation)

2. Transport of fatty acyl CoA into mitochondria

A
  • fatty acyl group linked to carnitine
  • transported across the membrane by a translocase protein
  • fatty acyl CoA reformed in the matrix
  • Rate limiting step for fatty acid oxidation

Carnitine (carnitine acyltransferase I) -> acyl carnitine

across to matrix side
(carnitine acyltransferace II) -> carnitine

back to cytoplasmic side

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14
Q

Fatty acid catabolism (b-oxidation)

3. Oxidation of fatty acyl CoA

A
  • a series of 4 reactions
  • 1 NADH, 1 FADH2 and 1 acetyl CoA are generated in each round
  • each round shortens the chain by 2 carbon atoms
  • cycle continues until only acetyl CoA remains
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15
Q

Summary

Fatty acid catabolism (b-oxidation)

A

• Oxidative process that release a large amount of energy
e.g. palmitate C16
8 acetyl CoA, 7FADH2, 7NADH

106 molecules of ATP
• unsaturated FAs need additional steps for degradation
isomerase / reductase

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16
Q

Glycerol metabolism

A
  • transported to the liver

* used for glycolysis / gluconeogenesis

17
Q

Protein catabolism (Stages I & II)

A
  • dietary proteins are a source of amino acids
  • 9 essential amino acids – those that cannot be synthesised; histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine
18
Q

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 – pancreas aminopeptidase
• Transport into intestinal cells and into blood

19
Q

Degradation of amino acids:

A

• Excess amino acids cannot be stored so have to be degraded

20
Q

Degradation of amino acids

1Transfer of amino group to a-ketoglutarate

A

aminotransferases

aspartate + a-ketoglutarate produces oxaloacetate + glutamate
alanine + a-ketoglutarate produces pyruvate + glutamate

21
Q

Degradation of amino acids

  1. Dehydrogenation to produce ammonium ion
    - glutamate dehydrogenase
A
  • glutamate dehydrogenase

e.g.
aspartate + a-ketoglutarate produces oxaloacetate + glutamate
alanine + a-ketoglutarate produces pyruvate + glutamate

22
Q

Degradation of amino acids

Overall

equation

A

Amino acid + NAD(P)+ +H2O a-ketoacid + NH4+ + NAD(P)H

23
Q

Removal of ammonium ion - the urea cycle

A

Toxic NH4+ is converted to urea and excreted

24
Q

Carbon skeletons of amino acids

A

• Deamination of amino acids produces carbon skeletons that are used in many other pathways

25
Q

Protein Metabolism

A
  • Proteins contain > 90% of the nitrogen in the body
  • Proteins are produced for a specific function NOT synthesised as a store of excess amino acids
  • Muscle protein can be broken down to provide energy during starvation
  • Proteins are continuously being broken down and resynthesised
26
Q

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