Literature summary for 2.1.3.2 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.

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Protein Variants

Protein Variants	Comment	Organism
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)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)