The process of protein synthesis involves the esterification of the amino acid (eg. arginine) to a specific tRNA (arginyl-tRNA) which tranfers the amino acid to the protein assembly site in the cytosol. Arginyl-tRNA synthetase is the enzyme which directs both the activation of arginine and its subsequent covalent linkage to tRNA.

Normally, this reaction is highly specific since there is a distinct aminoacyl-tRNA synthetase for linking each amino acid to its correct tRNA. Due to the structural similarity between arginine and canavanine, both amino acids are substrates for this enzyme. Arginyl-tRNA synthetase activates and then aminoacylates canavanine to the cognate tRNA for arginine. As a consequence, canavanine rather than arginine is transferred to the protein assembly site and erroneously incorporated into the nascent polypeptide chain. In this way, anomalous, structurally aberrant, canavanyl proteins are synthesized.