N-acetylornithine carbamoyltransferase (AOTC)

N-acetylornithine carbamoyltransferase (AOTC, EC 2.1.3.9) is an enzyme found in several eubacteria that catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to N(2)-acetyl-L-ornithine, resulting in the formation of N-acetyl-L-citrulline and phosphate[1][2][4][6]. It is part of an alternative arginine biosynthesis pathway that substitutes for ornithine carbamoyltransferase (EC 2.1.3.3) in specific bacterial species and displays no catalytic activity toward L-ornithine[4][7]. The enzyme's activity and unique substrate specificity make it a potential antimicrobial target, especially as it defines a different arginine biosynthetic route compared to canonical pathways in most organisms[3][5][7]. Currently, no well-characterized drugs interact with this target, but inhibitors such as N-acetyl derivatives and related compounds have been used experimentally to study its function and mechanisms[5].

Other names

Acetylornithine transcarbamylaseN-acetylornithine transcarbamylaseAOTCaseCarbamoyl-phosphate:2-N-acetyl-L-ornithine carbamoyltransferase

Enzyme inhibition (possible mechanism: blocking arginine biosynthesis in microbes by inhibiting AOTC) Substrate competition (in experimental contexts)