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Literature summary extracted from

  • Kantrowitz, E.R.; Lipscomb, W.N.
    Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition (1990), Trends Biochem. Sci., 15, 53-59.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 X-ray structure of the holoenzyme in the presence of the substrate analog N-phosphonoacetyl-L-aspartate, carbamoylphosphate and succinate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 CTP
-
Escherichia coli
2.1.3.2 UTP
-
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
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.2 additional information
-
specific activity of the catalytic subunit alone is about 50% higher than that of the holoenzyme 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
-
?

Subunits

EC Number Subunits Comment Organism
2.1.3.2 More model for homotrophic cooperativity Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.2 ATP activates Escherichia coli