Literature summary extracted from

Yuan, X.; LiCata, V.J.; Allewell, N.M.
Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase (1996), J. Biol. Chem., 271, 1285-1294.

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.1.3.2	Y165F	mutant enzyme shows greatly reduced affinity for aspartate and activity	Escherichia coli
2.1.3.2	Y240F	mutant enzyme shows higher affinity for aspartate and increased activity	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)