Final answer:
Aminoacyl tRNA synthetases have highly discriminating amino acid activation sites, ensuring the accuracy of protein synthesis.
Step-by-step explanation:
Aminoacyl tRNA Synthetases
Aminoacyl tRNA synthetases are enzymes that catalyze the attachment of amino acids to tRNA molecules during protein synthesis. Each amino acid has a specific aminoacyl tRNA synthetase that recognizes it. These enzymes have highly discriminating amino acid activation sites, meaning that they are able to accurately select and activate the correct amino acid for attachment to the corresponding tRNA molecule. This specificity is important for ensuring the fidelity of protein synthesis.
For example, if a leucine-tRNA synthetase accidentally attaches an incorrect amino acid, such as isoleucine, to a tRNA molecule, it will recognize the incorrect amino acid and remove it through a proofreading process, preventing the incorporation of the wrong amino acid into the growing protein chain.