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Literature summary extracted from

  • Allewell, N.M.
    Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms (1989), Annu. Rev. Biophys. Biophys. Chem., 18, 71-92.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.3.2 ATP
-
 Escherichia coli

General Stability

EC Number General Stability Organism
2.1.3.2 thermal denaturation Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 CTP
-
 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
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.2 carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate reaction mechanism Escherichia coli
a
2.1.3.2 carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP Escherichia coli
a

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
-
 ?