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Literature summary for 2.1.3.2 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

Activating Compound Comment Organism Structure
ATP
-
Escherichia coli

General Stability

General Stability Organism
thermal denaturation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
CTP
-
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
-
-
-

Reaction

Reaction Comment Organism Reaction ID
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate reaction mechanism Escherichia coli
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

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
-
?