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How are amino acids converted to other amino acids?

Published in Amino Acid Conversion 2 mins read

Amino acids are primarily converted to other amino acids through a process called transamination.

Transamination: The Key to Amino Acid Conversion

Transamination is a chemical reaction that involves the transfer of an amino group from one amino acid to an α-keto acid. This process is crucial for synthesizing non-essential amino acids and catabolizing amino acids.

How Transamination Works:

  1. Amino Group Transfer: An amino acid donates its amino group (-NH2) to an α-keto acid.
  2. Formation of New Compounds: The original amino acid becomes the corresponding α-keto acid, and the receiving α-keto acid is converted into a new amino acid.

Key α-keto Acids and Their Corresponding Amino Acids:

The reference states that the main α-keto acids involved in these reactions are:

α-Keto Acid Corresponding Amino Acid
Pyruvate Alanine
Oxaloacetate Aspartate
α-Ketoglutarate Glutamate

Important Exception: The reference also notes that lysine and threonine are not involved in transamination reactions. This indicates that these amino acids use other metabolic pathways for conversion and degradation, which are not covered in the given reference.

Simplified Explanation:

Imagine you have an amino acid that's not needed in its current form. To convert it, it trades its amino group with a specialized helper molecule (α-keto acid). This trade results in the original amino acid becoming its corresponding α-keto acid and the helper molecule becoming a new amino acid, ready to perform its function.

Practical Implications:

  • Amino Acid Synthesis: Transamination is used to synthesize non-essential amino acids that the body can create on its own.
  • Amino Acid Degradation: When amino acids are broken down, transamination is the first step. This process removes the amino group, which is further processed in urea cycle, and prepares the remaining carbon skeletons for other metabolic pathways.
  • Metabolic Flexibility: It allows the body to adapt to different nutritional and physiological needs by shifting which amino acids are made and used.

In conclusion, transamination is the primary method for interconverting amino acids, involving the transfer of an amino group to different α-keto acids. This allows for the production of various amino acids, with lysine and threonine being notable exceptions, requiring other metabolic routes.