Amino Acid Metabolism Flashcards

1
Q

What are nitrogen assimilation and nitrogen fixation and how are they different? Which is more costly?

A

2 ways for nitrogen to enter biosphere

Fixation most costly and difficult, assimilation = predominant strategy

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2
Q

What enzymes and substrates bring nitrogen into the biosphere?

A

Fixation: nitrogenase + reductase
Assimilation: glutamate dehydrogenase (GDH) + glutamine synthetase + glutamate synthase

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3
Q

What are the reactants and products of a transaminase reaction?

A

amino acid and keto acid

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4
Q

Alpha ketoacid

A

Deaminated form of AAs

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5
Q

What cofactor is involved in transamination reactions?

A

pyridoxal phosphate (Vitamin B6)

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6
Q

Why are transaminases important—what role do they play in amino acid metabolism?

A

Transferring the amino group from abundant AA (glutamate) to an alpha ketoacid acceptor, creating a new AA

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7
Q

Why is vitamin B6 important? What would be some consequences of B6 deficiency?

A

B6 deficiency causes changes in carbon skeleton of AAs, makes AA essential

Symptoms: skin rashes, mental changes

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8
Q

What makes an amino acid essential?

A

Not made by the body (not via metabolic intermediates), comes from dietary source

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9
Q

Limiting amino acid

A

AA present in lowest amount in body

When runs out, synthesis of any proteins that require it will stop

Limits how much protein can be synthesized

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10
Q

Why are some amino acids considered “conditionally essential”?

A

AAs usually not essential, except in times of illness and stress

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11
Q

Why are proteins broken down in starvation– what are they used for?

A

Fuel source (glucose)

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12
Q

What are the major carriers of carbons derived from protein degradation to liver for gluconeogenesis?

A

ammonium, pyruvate

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13
Q

How is the NH4+ removed and where does this occur?

A

Removed in mitochondria by glutaminase

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14
Q

What is the glucose-alanine shuttle?

A

Purpose: transports nitrogen in a non-toxic form from peripheral tissues to the liver

Steps:
- Protein from muscle degraded for fuel
- Ammonium stripped from glutamate and then to alanine
- Alanine carries ammonium to liver
- Transferred back to glutamate and then detoxified in urea cycle
- Pyruvate generated by aminotransferase rxn used for gluconeogenesis

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15
Q

What’s the role of the Urea cycle? When is it active? What turns it on?

A

Eliminates toxic ammonium from the body

Active after a high protein meal and during a states of starvation

Turned on by N-acetyl-glutamate (a required allosteric activator)

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16
Q

Carbamoyl phosphate

A

Activated by N-acetyl-glutamate

Committed step of urea cycle

17
Q

What other pathway involves Carbamoyl-P synthesis?

A

pyrimidine synthesis

18
Q

What is the role of aspartate?

A

Nitrogen donor in urea cycle

Coupled w/ ammonium to transport citrulline

19
Q

Why is it so important to get rid of ammonia? What reactions does high [NH4+] drive that can be harmful to metabolism in the brain and why is this harmful?

A

Build up of ammonia in blood causes health problems (toxic - corrosive in body)

Build up activates glutamine synthetase, leading to depletion of glutamate
Glutamate = precursor for synthesis of GABA (essential neurotransmitter)