Aminoacyltransferases () are

acyltransferase Acyltransferase is a type of transferase enzyme that acts upon acyl In chemistry, an acyl group is a moiety derived by the removal of one or more hydroxyl groups from an oxoacid, including inorganic acids. It contains a double-bonded oxygen ...

enzymes which act upon an

amino group In chemistry, amines (, ) are organic compounds that contain carbon-nitrogen bonds. Amines are formed when one or more hydrogen atoms in ammonia are replaced by alkyl or aryl groups. The nitrogen atom in an amine possesses a lone pair of elec ...

. For instance,

aminoacyl tRNA synthetase An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its pre ...

s attach an aminoacid through esterification to the corresponding tRNA. The activation of amino acids it aminoacyl-tRNA synthetase requires

hydrolysis Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water ...

of Adenosine triphosphate, ATP to Adenosine monophosphate, AMP plus Pyrophosphate, PP_i. The aminoacyl-tRNA molecule has close relationships with elongation facts like EF-Tu. Peptidyl transferases are also a type of aminoacyltransferase that catalyze the formation of peptide bonds, as well as the hydrolytic step that leads to the release of newly synthesized proteins off the tRNA.

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