BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Aminoacyl-tRNA synthetases (aaRSs) are universally distributed enzymes that catalyze the esterification of a tRNA to its cognate amino acid (i.e., the amino acid corresponding to the anticodon triplet of the tRNA according to the genetic code) (Ibba and Soll 2000; Pang et al.

Detailed explanation-2: -One end of the tRNA binds to a specific amino acid (amino acid attachment site) and the other end has an anticodon that will bind to an mRNA codon. One end of the L shape has the anticodon, while the other has the attachment site for the amino acid.

Detailed explanation-3: -Aminoacylation, the attachment of an amino acid to a tRNA, is typically a two-step process catalyzed by aminoacyl-tRNA synthetases (aaRSs). The first step, termed “activation”, is the formation of an aminoacyl-AMP (aminoacyl-adenylate) on the enzyme through the hydrolysis of adenosine triphosphate (ATP).

Detailed explanation-4: -The enzyme binds ATP to the amino acid to form an amino acid–AMP complex linked by a high energy bond (PP released) The amino acid is then coupled to tRNA and the AMP is released – the tRNA molecule is now “charged” and ready for use.

Detailed explanation-5: -Aminoacyl-tRNA synthetases attach amino acids to tRNAs The attachment of amino acids to tRNAs-‘charging’ in molecular biology jargon-is the function of the group of enzymes called aminoacyl-tRNA synthetases.