Frequently Asked Question

Transamination reactions are crucial for amino acid synthesis and involve the transfer of an amino group (-NH2) from an amino acid to an α-keto acid. Here's a breakdown of the reaction using alanine as an example:
1. Reactants:
Alanine (amino acid): CH3-CH(NH2)-COOH
α-Ketoglutarate (α-keto acid): HOOC-CH2-CH2-CO-COOH
2. Enzyme:
Transaminase (aminotransferase): A specific enzyme catalyzes the reaction.
3. Mechanism:
The amino group from alanine is transferred to α-ketoglutarate.
The carbon skeleton of alanine becomes pyruvate (an α-keto acid).
α-Ketoglutarate is converted to glutamate (an amino acid).
4. Products:
Pyruvate (α-keto acid): CH3-CO-COOH
Glutamate (amino acid): HOOC-CH2-CH2-CH(NH2)-COOH
Overall Reaction:
Alanine + α-Ketoglutarate ⇌ Pyruvate + Glutamate
Structures:
Alanine: [Image of Alanine]
α-Ketoglutarate: [Image of α-Ketoglutarate]
Pyruvate: [Image of Pyruvate]
Glutamate: [Image of Glutamate]
Key Points:
Transaminases require the cofactor pyridoxal phosphate (PLP), a derivative of vitamin B6.
This reaction is reversible, allowing for the synthesis and degradation of amino acids.
Transamination is an essential process for amino acid metabolism and nitrogen balance in the body.