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Literature summary for 2.1.3.2 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

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

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
-
?