Literature summary for 2.1.3.2 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.

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Protein Variants

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