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Literature summary extracted from

  • Mort, J.S.; Chan, W.W.C.
    Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits (1975), J. Biol. Chem., 250, 653-660.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 aspartate
-
 Escherichia coli
2.1.3.2 CTP competitive vs. carbamoyl phosphate Escherichia coli
2.1.3.2 L-aspartate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 7.9
-
 L-aspartate complex of catalytic and regulatory subunits, C3R6 Escherichia coli
2.1.3.2 44.7
-
 L-aspartate complex of catalytic subunits, C3 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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.3.2 More characterization of a complex between catalytical and regulatory subunit Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.3.2 10
-
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.3.2 7.9
-
 L-aspartate substrate inhibition, complex of catalytic and regulatory subunits, C3R6 Escherichia coli
2.1.3.2 80
-
 aspartate substrate inhibition, complex of catalytic subunits, C3 Escherichia coli