L-Arginine is an amino acid involved in numerous essential metabolic pathways. It is catabolized by several enzymes to some important metabolites. Arginine is very important for mammals, and to ensure their supplies, mammalian cells can synthesize this amino acid from citrulline.This study deals with a series of arginine analogues and the activity of seven different enzymes of arginine metabolic pathway (nitric oxide synthases (inducible and endothelial), arginases, arginine:glycineamidinotransferase, arginine decarboxylase, arginine deiminase, and argininosuccinate synthase) in those analogues. The compounds were biologically tested and their in vitro effects are explained using docking. All investigated compounds inhibited five from the total of seven assessed enzymes, with norsulfoarginine (NsArg) and sulfoarginine (sArg) being more potent than the norcanaline (NCan) and norcanavanine (NCav) analogues due to the availability of more enzyme interactions sites in the first two compounds. Modifications with bis-(2-chloroetylhydrazine) and phenylhydrazine increased binding potential of the compounds. Computational methods can help in design of arginine mimetics, and are very useful for predicting the biological activities of newly synthesized compounds.
