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Protein Metabolism

Comprehensive overview of amino acid anabolism (synthesis) and catabolism (degradation)

Protein Anabolism (Amino Acid Synthesis)

Essential vs Non-Essential Amino Acids

Essential Amino Acids (9 total - must be consumed in diet):

Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine

Non-Essential Amino Acids (11 total - synthesized in body):

Alanine
Arginine
Asparagine
Aspartate
Cysteine
Glutamate
Glutamine
Glycine
Proline
Serine
Tyrosine

Carbon Skeleton Sources

Non-essential amino acids are synthesized from intermediates of glycolysis and the TCA cycle:

  • 3-Phosphoglycerate: → Serine → Glycine, Cysteine
  • Pyruvate: → Alanine
  • α-Ketoglutarate: → Glutamate → Glutamine, Proline, Arginine
  • Oxaloacetate: → Aspartate → Asparagine

Glutamate: Central Hub of Amino Acid Synthesis

Glutamate Dehydrogenase:

α-Ketoglutarate + NH₄⁺ + NADH → Glutamate + NAD⁺

Glutamine Synthetase:

Glutamate + NH₄⁺ + ATP → Glutamine + ADP + Pi

Glutamate and glutamine serve as nitrogen donors for the synthesis of other amino acids, purines, and pyrimidines.

Transamination

Key Reaction: Transfer of amino group from one amino acid to an α-keto acid

Amino Acid 1 + α-Keto Acid 1 ⇌ α-Keto Acid 2 + Amino Acid 2

Important Transaminases:

  • AST (Aspartate Aminotransferase):
    Glutamate + Oxaloacetate ⇌ α-KG + Aspartate
  • ALT (Alanine Aminotransferase):
    Glutamate + Pyruvate ⇌ α-KG + Alanine

Note: Elevated AST and ALT in blood are clinical markers for liver damage

Methylation Pathway

Methionine, serine, and cysteine metabolism are interconnected:

  1. Methionine + ATP → SAM (S-adenosylmethionine)
  2. SAM → Transmethylation (methyl group transfer to DNA, proteins, lipids)
  3. SAM → SAH → Homocysteine
  4. Homocysteine + Serine → Cystathionine → Cysteine

Protein Catabolism (Amino Acid Degradation)

When organismal carbohydrate levels are low or excess amino acids are consumed, amino acids are oxidized for energy.

Removing the Amino Group

Two types of reactions remove nitrogen from amino acids:

1. Transamination (most common):

Amino Acid + α-Keto Acid → α-Keto Acid + Amino Acid

Example: Alanine + α-KG → Pyruvate + Glutamate

2. Deamination (releases free ammonia):

Asparagine + H₂O → Aspartate + NH₄⁺

Via Asparaginase enzyme

Glucogenic vs Ketogenic Amino Acids

Glucogenic (14 AAs)

Can become glucose

Yields: Pyruvate or Oxaloacetate

Aspartate, Asparagine
Glutamate, Glutamine
Alanine, Arginine
Glycine, Proline
Serine, Histidine
Threonine, Valine
Cysteine, Methionine

Both (4 AAs)

Can become glucose or ketones

Yields: Both types of intermediates

Phenylalanine
Tyrosine
Tryptophan
Isoleucine

Ketogenic (2 AAs)

Cannot become glucose

Yields: Acetyl-CoA or Acetoacetyl-CoA

Leucine
Lysine

Why Can't Acetyl-CoA Become Glucose?

Acetyl-CoA requires oxaloacetate to enter the TCA cycle. Two carbons are lost as CO₂ in reactions 3 and 4 of the TCA cycle, so there is no net gain of carbon. A ≥4 carbon intermediate is required to enter the TCA cycle for gluconeogenesis.

Entry Points into Energy Metabolism

  • Pyruvate: Alanine, Cysteine, Glycine, Serine, Threonine, Tryptophan
  • Acetyl-CoA: Leucine, Lysine, Phenylalanine, Tryptophan, Tyrosine
  • Acetoacetyl-CoA: Leucine, Lysine, Phenylalanine, Tryptophan, Tyrosine
  • α-Ketoglutarate: Arginine, Glutamate, Glutamine, Histidine, Proline
  • Succinyl-CoA: Isoleucine, Methionine, Valine
  • Fumarate: Aspartate, Phenylalanine, Tyrosine
  • Oxaloacetate: Asparagine, Aspartate

Nitrogen Disposal: The Urea Cycle

Why Remove Nitrogenous Waste?

  • Ammonia is toxic: NH₃ is a weak base (pKa = 9.4). At physiological pH (~7.4), it becomes protonated to NH₄⁺, which can cause metabolic alkalosis at high concentrations.
  • High [NH₄⁺] disrupts metabolism: Drives excess glutamate and glutamine synthesis, which depletes α-ketoglutarate from the TCA cycle.
  • Glutamine as neurotransmitter: Excess glutamine can act as a stimulatory neurotransmitter, leading to neurological problems.

Nitrogen Excretion Strategies

Ammonia (NH₃)

Aquatic animals

Highly soluble, easily diffuses into water

Urea

Mammals

Non-toxic, soluble, excreted in urine

Uric Acid

Birds, reptiles

Low solubility, conserves water

The Urea Cycle

Location: Mitochondria (first 2 steps) and Cytosol (remaining steps)

Function: Converts toxic ammonia into urea for excretion

Two Nitrogen Sources for Urea:

  1. First Nitrogen (from free ammonia):

    NH₄⁺ + CO₂ + 2 ATP → Carbamoyl phosphate (Carbamoyl phosphate synthetase I)

    Carbamoyl-P + Ornithine → Citrulline (in mitochondria)

    Citrulline exported to cytosol

  2. Second Nitrogen (from aspartate):

    Citrulline + Aspartate + ATP → Arginosuccinate + AMP + PPi (= 2 ATP)

    Arginosuccinate → Arginine + Fumarate

    Arginine + H₂O → Urea + Ornithine

Energy Cost:

  • 2 ATP → Carbamoyl phosphate
  • 2 ATP (ATP → AMP + PPi) → Arginosuccinate
  • Total: 4 ATP per urea molecule

Linking Urea Cycle and TCA Cycle

The two cycles are energetically linked through fumarate:

  1. Arginosuccinate → Arginine + Fumarate
  2. Fumarate enters TCA cycle
  3. Fumarate → Malate → Oxaloacetate (produces 1 NADH → ~2.5 ATP)
  4. Oxaloacetate + Glutamate → Aspartate + α-KG (via AST)
  5. Aspartate provides the second nitrogen back to the urea cycle

The NADH produced (~2.5 ATP) helps offset the energy cost of the urea cycle (~4 ATP per urea).

Protein Metabolism Pathways

PathwayLocationEnergyKey Enzyme
TransaminationCytosol / MitochondriaNo ATP requiredAST, ALT
Glutamine SynthesisCytosol1 ATP consumedGlutamine synthetase
Glutamate SynthesisMitochondria1 NADH consumedGlutamate dehydrogenase
Urea CycleMitochondria + Cytosol4 ATP consumedCPS I, Arginosuccinate synthetase