Literature summary extracted from

Lee, B.H.; Ley, B.W.; Kantrowitz, E.R.; O'Leary, M.H.; Wedler, F.C.
Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism (1995), J. Biol. Chem., 270, 15620-15627.

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.1.3.2	E50A	mutant enzyme shows a low activity, low affinity state, only 2fold activation with N-(phosphonoacetyl)-L-aspartate, kinetic mechanism is changed	Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.1.3.2	carbamoylphosphate + L-aspartate	Escherichia coli	-	phosphate + N-carbamoyl-L-aspartate	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.3.2	Escherichia coli	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.3.2	carbamoyl phosphate + L-aspartate	-	Escherichia coli	phosphate + N-carbamoyl-L-aspartate	-	?
2.1.3.2	carbamoylphosphate + L-aspartate	-	Escherichia coli	phosphate + N-carbamoyl-L-aspartate	-	?

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Release 2023.1 (January 2023)