Arginine N-succinyltransferase (AST)

Arginine N-succinyltransferase is the primary enzyme in the arginine succinyltransferase (AST) pathway, a major catabolic route for L-arginine in bacteria such as Pseudomonas aeruginosa and Escherichia coli (UniProt P09050, P0A9M0). It catalyzes the transfer of a succinyl group from succinyl-CoA to the alpha-amino group of L-arginine, producing N2-succinyl-L-arginine (EC 2.3.1.109). This metabolic process allows the bacteria to utilize arginine as a source of carbon, nitrogen, and energy, which is vital for survival in diverse environments (PubMed: 10411748). In pathogens like P. aeruginosa, the AST pathway is involved in the regulation of virulence and adaptation to the host environment. Although there are currently no clinical drugs targeting this enzyme, it is considered a viable target for novel antibacterial strategies due to its absence in human metabolic pathways. Inhibiting this enzyme could potentially disrupt bacterial growth and reduce the fitness of the pathogen during infection.

Other names

Arginine succinyltransferaseL-arginine N2-succinyltransferaseSuccinyl-CoA:L-arginine N2-succinyltransferaseAruAAstA

Inhibition of the arginine succinyltransferase pathway to disrupt bacterial nitrogen utilization and growth.