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Index >> Protein Synthesis >> Activation of Amino Acids

Activation of Amino Acids

Activation of Amino Acids - The first step in translation is the activation of amino acids. The 20 amino acids commonly found in proteins are first screened to eliminate the D isomers. Only the L amino acids take part in protein synthesis. Many of the other common amino acids which are not used in protein synthesis, e.g. citrulline, alanine, β alanine, etc. are also rejected.

The activation of amino acids takes place through their carboxyl groups. Each amino acid is catalysed by its own specific activating enzyme, called aminoacyl tRNA synthetase, to form an aminoacyl adenylate (aaa) (aminoacyl AMP) in the presence of ATP. A high energy acyl bond is formed between the α-phosphate of A TP and the carboxyl group of the amino acid.

 

aa + ATP + E----> E.aa-- AMP + PPi
Amino acid + ATP + Aminoacyl tRNA synthetase---->
(Activating enzyme)
Aminoacyl adenylate synthetase +
(Aminoacyl AMP)
Inorganic pyrophosphate

The β and γ phosphates of A TP break away as inorganic pyrophosphates (PPi). The aminoacyl AMP remains bound to the activating enzymeThe activation of amino acids by activating enzymes has a large degree of specificity, each amino acid being activated by a specific enzyme. However, some activating enzymes can activate more than one amino acid, e.g. isoleucine tRNA synthetase can also activate valine.

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