canaline

Canaline is a non-proteinogenic amino acid found primarily in legumes such as the jack bean (Canavalia ensiformis). Structurally related to ornithine but distinguished by an aminooxy group in its side chain, canaline acts as an irreversible inhibitor of the mitochondrial enzyme ornithine aminotransferase (OAT), a key enzyme in the urea cycle. By forming a stable oxime with pyridoxal 5′-phosphate at the OAT active site, canaline disrupts normal enzymatic function and interferes with nitrogen metabolism. Its toxicity is attributed both to this inhibition and to its incorporation into proteins via arginyl-tRNA synthetase, resulting in dysfunctional "canavanyl proteins." Canaline also inhibits other pyridoxal-dependent enzymes and can disrupt polyamine metabolism and generate reactive nitrogen species. It plays a role as a plant metabolite involved in chemical defense against insects[1][2][5][6].

Other names

l-canalineo-amino-l-homoserine2-amino-4-(aminooxy)butanoic acidl-homoserine o-amino