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16 Cards in this Set

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What are the essential amino acids?
Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Histidine
Arginine
Leucine
Lysine
What are the non-essential amino acids?
Glycine
Alanine
Serine
Cysteine
Aspartate
Asparagine
Proline
Glutamate
Glutamine
Arginine
Tyrosine
Which amino acids become essential if Methionine and Phenolalanine become low in diet?
Cysteine
Tyrosine
What are the 3 sources and 2 utilizations of the amino acid pool?
1. Tissue Protein Catabolism
2. Dietary Protein
3. Non-Essential Fatty Acid synthesis

1. Amino Acid catabolism
2. Nitrogen cmpd synthesis
What are the two maor kinds of protein degradation?
Lysosomal Pathway - degrades proteins from outside the cell

Ubiquitin Proteosome pathway - degrades proteins from inside the cell.
1. Polyubiquitination
2. Proteosome recognition
3. Protein degraded in proteosome
4. Ubiquitin recycled
5. AAs released to pool
Which 3 parts of Nitrogen Metabolism take place in the liver?
1. AAs release amino groups as ammonia
2. Ammonia is detoxified to urea
3. AA carbon skeletons are used for:
- gluconeogenesis
- TCA cycle
- ketone bodies
Which 4 non-protein substances are excreted by the kidneys?
1. Urea made in the liver
2. Ammonia as ammonium ions
3. Uric acid from purine degradation
4. Creatinine from creatine degradation
How are amino acids transported in the renal tubule and GIT?
Brush border membrane absorms them through a Na+/K+ ATPase secondary transport. They follow their own gradient in the portal vein.
What two pathologies are related to AA transport?
Cystinuria - Deficiency of cystine transporter.
- Cystine is excreted in urine rather than reabosorbed.
- Cystine stones form in renal tubules

Hartnup's disease - neutral AA (tryptophan) transport defect.
- increased excretion
- NAD deficiency (pellagra)
- because niacin is not synthesized from tryptophan, you get the 4 Ds.
Provide an overview of AA catabolism
1. Tissue proteins are broken down to AAs
2. AAs lose their amino groups becoming keto acids
3. Glucogenic AAs are
- turned into pyruvate and enter the TCA cycle as intermediates
- used in gluconeogenesis
4. Ketogenic AAs are made into acetyl CoA or Ketone bodies.
Which amino acids are Ketogenic? Glucogneic? Which are both?
Ketogenic - leucine, lysine

Both - threonine, isoleucine, phenylalanine, tryptophan,
tyrosine

Glucogenic - all others - Glycine, Serine, Valine, Histidine, Arginine, Cysteine, Proline, Alanine, Glutamate, Glutamine, Aspartate, Asparagine, Methionine
Link the important TCA cycle intermediates formed from amino acids
Pyruvate - alanine
Acetoacetyl CoA/Acetyl CoA - leucine, lysine
a-Ketoglutarate - Glutamate, glutamine
Succinyl CoA - isoleucine, valine
Fumarate - phenylalanine
Oxaloacetate - asparagine, aspartate
Discuss alanine metabolism
Alanine is turned into Pyruvate
1. Alanine transaminase (ALT) takes an amino group from a-ketoglutarate
2. The a-ketoglutarate becomes glutamate
3. The left over alanine becomes pyruvate

COENZYME = B6
Discuss glutamate metabolism
A-ketoglutarate is converted to either glutamate (1 N) or glutamine (2 Ns)

Glutamate - glutamate dehydrogenase
Glutamine - glutamine synthetase

Both reactions are fully reversible
Discuss aspartate metabolism
Asparagine is turned into oxaloacetate.
1. Asparagine ↔ Aspartate
- enzyme: Asparaginase
- frees one ammonia
2. Aspartate ↔ oxaloacetate
- enzyme: Aspartate transaminase (AST)
- coenzyme: a-ketoglutarate ↔ glutamate when it gains an ammonia, B6

Oxaloacetate is turned into asparagine.
1. Oxaloacetate ↔ Aspartate
- enzyme: aspartate transaminase (AST)
- coenzyme: glutamate ↔ a-ketoglutarate when it loses its ammonia, B6
2. Aspartate ↔ Asparagine
- enzyme: asparagine synthetase
- co-enzyme: glutamine ↔ glutamate when it loses its ammonia