Literature summary extracted from

Kurtin, W.E.; Bishop, S.H.; Himoe, A.
Ornithine transcarbamylase: steady-state kinetic properties (1971), Biochem. Biophys. Res. Commun., 45, 551-556.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.1.3.3	5-hydroxy-2-aminovaleric acid	competitive vs. ornithine, uncompetitive vs. carbamoylphosphate	Enterococcus faecalis
2.1.3.3	DL-2-Amino-5-hydroxypentanoic acid	-	Enterococcus faecalis
2.1.3.3	L-norvaline	competitive vs. ornithine, uncompetitive vs. carbamoylphosphate	Enterococcus faecalis
2.1.3.3	phosphate	competitive vs. carbamoylphosphate, uncompetitive vs. ornithine	Enterococcus faecalis

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.3.3	Enterococcus faecalis	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.1.3.3	carbamoyl phosphate + L-ornithine = phosphate + L-citrulline	mechanism	Enterococcus faecalis	a
2.1.3.3	carbamoyl phosphate + L-ornithine = phosphate + L-citrulline	ping pong mechanism	Enterococcus faecalis	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.3.3	carbamoyl phosphate + L-ornithine	-	Enterococcus faecalis	phosphate + L-citrulline	-	?

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Release 2023.1 (January 2023)