Literature summary extracted from

Fetler, L.; Tauc, P.; Baker, D.P.; Macol, C.P.; Kantrowitz, E.R.; Vachette, P.
Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase (2002), Protein Sci., 11, 1074-1081.

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.1.3.2	D162A	7700fold reduction in specific activity, 2fold decrease in affinity for aspartate, loss of homotropic cooperativity and decreased activation by ATP	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)