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Literature summary for 2.1.3.2 extracted from

  • Tsuruta, H.; Kihara, H.; Sano, T.; Amemiya, Y.; Vachette, P.
    Influence of nucleotide effectors on the kinetics of the quaternary structure transition of allosteric aspartate transcarbamylase (2005), J. Mol. Biol., 348, 195-204.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP allosteric effector, increases the apparent rate of unliganded T-state to substrate-bound R-state Escherichia coli
CTP allosteric effector, slightly shifts the dynamical equilibrium during steady state toward unliganded T-state Escherichia coli
UTP allosteric effector, makes steady state vanishingly short Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Reaction

Reaction Comment Organism Reaction ID
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate allosteric enzyme, in absence of effectors, two-state, concerted transition model Escherichia coli