lecture 31 - amino acids as fuel molecules Flashcards

1
Q

what is the deamination of amino acids

A

removal of the nitrogen group from amino acid

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2
Q

what does deamination of amino acids generate and what occurs to them

A

carbon skeleton = can be used for energy capture

a free amino acid = generally excreted

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3
Q

what are the two ways to deaminate an amino acid

A
  1. releasing their amino acid groups to solution
  2. transferring their amino acid group to a keto acid
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4
Q

what is the transferring of amino acid to keto acid catalysed by

A

aminotransferase enzymes (transmainases)
- requires co enzyme

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4
Q

what is transferring amino acid group to keto acid called (deamination)

A

transamination

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5
Q

how is an amino acid deaminated by releasing amino group to solution

A

enzyme catalysed reaction where amino groups is chopped off and released to solution

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6
Q

what is the co enzyme required for transamination reactions and what does it do

A

pyridoxal phosphate (PLP) = carries amino acid group from amino acid to keto acid

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7
Q

what forms does the co enzyme that is required for transamination reactions exist in

A

pyridoxal phosphate (no amino acid) and pyridoxamine phosphate (with amino group)

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8
Q

what is the first step of transamination

A

amino group is transferred from the amino acid to the pyridoxal phosphate (becomes pyridoxamine phosphate)

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9
Q

what is the second step of transamination

A

amino group is transferred from pyridoxamine phosphate (becomes pyridoxal phosphate) to the keto acid

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10
Q

what is the keto acid of aspartate

A

oxaloacetate

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11
Q

what is the keto acid of alanine

A

pyruvate

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12
Q

what is the keto acid of glutamate

A

a-ketoglutarate

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13
Q

can all keto acids be feed into metabolic pathways

A

some can directly enter and some require modification first

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14
Q

how is excess nitrogen removed from the body

A

via the liver = also requires transamination reactions

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