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Literature summary extracted from

  • Xi, X.G.; De Staercke, C.; Van Vliet, F.; Triniolles, F.; Jacobs, A.; Stas, P.P.; Ladjimi, M.M.; Simon, V.; Cunin, R.; Herve, G.
    The activation of Escherichia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2' at the hydrophobic interface between the two domains of the regulatory chains (1994), J. Mol. Biol., 242, 139-149.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.2 L151Q strongly reduced stimulation by ATP, synergistic inhibition by UTP is decreased Escherichia coli
2.1.3.2 L151V stimulation by ATP is reduced by 50% Escherichia coli
2.1.3.2 L32A stimulation by ATP is reduced by 25% Escherichia coli
2.1.3.2 L76A synergistic inhibition by UTP is decreased Escherichia coli
2.1.3.2 Q73E stimulation by ATP is reduced by 80% Escherichia coli
2.1.3.2 V106A synergistic inhibition by UTP is decreased Escherichia coli
2.1.3.2 V106W strongly reduced stimulation by ATP Escherichia coli
2.1.3.2 V106W/Y77F strongly reduced stimulation by ATP Escherichia coli
2.1.3.2 Y77F synergistic inhibition by UTP is decreased 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
-
 ?