Degradation of aminoacids

Cards (34)

  • Nonpolar Aliphatic R Groups
    • Glycine
    • Alanine
    • Valine
    • Leucine
    • Isoleucine
    • Methionine
    • Proline
  • Aromatic R Groups
    • Phenylalanine
    • Tyrosine
    • Tryptophan
  • Polar Uncharged R Groups
    • Serine
    • Threonine
    • Cysteine
    • Asparagine
    • Glutamine
  • Positively Charged R Groups
    • Lysine
    • Arginine
    • Histidine
  • Negatively Charged R Groups
    • Aspartate
    • Glutamate
  • Branched Amino Acids

    • Valine
    • Leucine
    • Isoleucine
  • Mixed Amino Acids
    Can undergo deamination or transamination depending on the pathway and energy needs
  • Transaminases (Aminotransferases)
    1. Catalyze the transfer of an amino group from an amino acid to an α-keto acid
    2. Cofactor: Pyridoxal phosphate (PLP) is the prosthetic group
    3. Mechanism: Involves the formation of a Schiff base (internal aldimine) with the enzyme, which then forms an external aldimine with the substrate amino acid
  • Glutamate-pyruvate transaminase

    Transfers the amino group from glutamate to pyruvate, forming α-ketoglutarate and alanine
  • Glutamate Dehydrogenase
    1. Catalyzes the oxidative deamination of glutamate to α-ketoglutarate and ammonia (NH3)
    2. Regulation: Allosterically activated by ADP/GDP and inhibited by ATP/GTP, reflecting the cell's energy state
  • Urea Cycle
    1. Converts toxic ammonia to urea for excretion
    2. Carbamoyl Phosphate Synthetase I: Converts NH3 and CO2 to carbamoyl phosphate
    3. Ornithine Transcarbamylase: Forms citrulline from carbamoyl phosphate and ornithine
    4. Argininosuccinate Synthetase: Combines citrulline with aspartate to form argininosuccinate
    5. Argininosuccinate Lyase: Splits argininosuccinate into arginine and fumarate
    6. Arginase: Hydrolyzes arginine to urea and ornithine, completing the cycle
  • Ketogenic Amino Acids
    • Leucine
    • Lysine
  • Glucogenic Amino Acids
    • Alanine
    • Glutamine
  • Mixed Amino Acids
    • Isoleucine
    • Phenylalanine
    • Tyrosine
  • Transaminases
    1. Role: Key enzymes in amino acid catabolism and nitrogen metabolism
    2. Reaction: Amino group transfer from an amino acid to an α-keto acid
  • Glutamine Dehydrogenase
    1. Reaction: Converts glutamate to α-ketoglutarate and NH3
    2. Importance: Plays a crucial role in nitrogen metabolism
  • Urea Cycle

    Reaction Pathway: Converts ammonia to urea for safe excretion
  • Epinephrine (Adrenaline)

    Derived from tyrosine, acts as a hormone and neurotransmitter
  • GABA (Gamma-Aminobutyric Acid)

    Derived from glutamate, functions as an inhibitory neurotransmitter
  • Glutathione
    Composed of glutamate, cysteine, and glycine, acts as an antioxidant
  • Nitric Oxide (NO)

    Produced from arginine, functions as a signaling molecule
  • Histamine
    Derived from histidine, involved in immune responses and gastric acid secretion
  • Serotonin
    Derived from tryptophan, acts as a neurotransmitter and regulator of mood
  • Phenylalanine Metabolism

    1. Initial Reaction: Conversion to tyrosine via phenylalanine hydroxylase
    2. Further Reactions: Tyrosine is further metabolized to fumarate and acetoacetate
  • Branched Amino Acids
    Example: Isoleucine, leucine, and valine are initially transaminated and then undergo oxidative decarboxylation
  • Asparagine and Glutamine Metabolism
    1. Asparagine: Hydrolyzed by asparaginase to aspartate and NH4+
    2. Glutamine: Hydrolyzed by glutaminase to glutamate and NH4+
  • Alanine, Aspartate, and Glutamate Metabolism
    Transamination: Conversion to pyruvate, oxaloacetate, and α-ketoglutarate, respectively
  • Nitric Oxide Synthase (NOS)

    Converts arginine to nitric oxide (NO) and citrulline
  • Catabolic Pathways for Specific Amino Acids
    1. Alanine, Glycine, Serine, Cysteine, Tryptophan, and Threonine: Each amino acid follows a specific pathway leading to key metabolic intermediates like pyruvate, oxaloacetate, and α-ketoglutarate
    2. Color-Coding of Carbon Atoms: Used to trace the fate of carbon atoms through these pathways
  • Central Reactions: Involving transaminases, glutamine dehydrogenase, and the urea cycle
  • Fate of Degradation: Ketogenic, glucogenic, or mixed pathways
  • Pathways of Degradation: Normal degradation pathways of amino acids
  • Active Molecules: Examples include epinephrine, GABA, glutathione, nitric oxide, histamine, and serotonin
  • Ammonia Excretion: Via the urea cycle in mammals