ACIDIC AMINO ACIDS (Aspartate and Glutamate)

Introduction to ACIDIC AMINO ACIDS (Aspartate and Glutamate)


  • Aspartate and asparagine are interconvertible
  • L-asparaginase is used as an anticancer agent in the treatment of leukemias and lymphomas

Salient features of aspartate metabolism are given below

  • Asp contributes one amino group for the synthesis of urea
  • Malate- Aspartate shuttle transfers the reducing equivalents from the cytosol to the mitochondria
  • Aspartate contributes the synthesis of purines and pyrimidines
  • Aspartate along with glutamate depolarise neurons. Asp acts as a excitatory neurotransmitter in pyramidal cells and spiny stellate cells in the visual cortex.


  • Glutamine is synthesized from glutamate by glutamine synthetase and is converted to glutamate by glutaminase
  • Most AA transfer their amino group to – ketoglutarate to form glutamate (transamination)
  • Glutamate is also formed during the metabolism of histidine, arginine and proline
  • Gluatamate is glucogenic and non essential amino acid.

Synthesis of biologically important substances from glutamate

  • N- acetylglutamate
  • Glutathione
  • γ- carboxyglutamate
  • Glutamate as a neurotransmitter
  • γ-Aminobutyric acid

BASIC AMINO ACIDS (Lysine, Arginine, Histidine and Proline)


  • Ketogenic amino acid
  • Absent in the proteins of cereals.
  • Upon hydroxylation forms hydroxylysine
  • Lysine in histone proteins occur in the methylated form
  • Trimethyllysine serves as a precursor for the synthesis of carnitine.



  • The vasodilator
  • Formed from histidine by decarboxylation
  • Causes a lowering of blood pressure
  • Stimulates gastric secretions
  • In high concentration it causes allergic reactions


  • Semi-essential amino acid
  • Formed in the urea cycle
  • Arginine is catabolised to form glutamate which is transaminated to  α-KG.
  • Glycogenic amino acid
  • Arginine along with glycine and SAM takes part in the creatine formation
  • Arginine acts as the precursor of nitric oxide (NO)


  • Glycogenic amino acid
  • Proline is hydoxylated by the enzyme prolyl hydroxylase to hydroxyproline.
  • Important constituent of fibrous proteins –collagen, elastin and keratin
  • Increased levels of hydroxyproline excreted in urine is a diagnostic indicator of bone tumours.

Nitric oxide

  • It is a potent vasodilator. Plays important role in regulation of normal BP
  • Deficiency of NO may lead to hypertension
  • It acts as as inhibitor of platelet aggregation and adhesion
  • Acts as a neurotransmitter
  • It stimulates the release of hormones (GHRH, CRH) from the hypothalamus
  • It is involved with the potential bactericidal actions of macrophages including their ability to kill cancer cells
  • It causes smooth muscle relaxation resulting in reduced GI motility and relaxation of sphinctors.
  • Sildenafil (viagra) drug inhibits the degradation of cGMP by phosphodiesterase and is a popular drug in treating erectile dysfunction.

Therapeutic effects of NO

  • NO as nitroglycerine is used in the treatment of angina pectoris
  • Inhalation of NO gas is employed in the treatment of pulmonary hypertension


Phenylalanine, Tyrosine and Tryptophan

Conversion of Phenylalanine to tyrosine

Biologically Important Substances synthesized from phenylalanine and tyrosine

  • Synthesis of catecholamines
  • Synthesis of Thyroid hormones
  • Synthesis of melanin

Other Biochemistry Notes

Biochemistry of Proteins

Carbohydrate Metabolism


Vitamin A


Pyrimidine metabolism

Purine Metabolism

Cardiac Biomarkers

. Blood Metabolism (Heme synthesis and breakdown)


DNA Repair

Regulation of gene expression

DNA Replication


Protein synthesis and genetic code

Detoxification (Xenobiotics)

Liver Function Test

Transamination Deamination & Urea Cycle


Hydroxy amino acids

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