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Literature summary for 2.1.3.2 extracted from

  • West, J.M.; Xia, J.; Tsuruta, H.; Guo, W.; ODay, E.M.; Kantrowitz, E.R.
    Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor (2008), J. Mol. Biol., 384, 206-218.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
ATP addition of ATP along with the substrates increases the rate of the transition from the low activity T to the high activity R state and also decreases the duration of the R-state steady-state phase Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
CTP addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations Escherichia coli
N-phosphonoacetyl-L-aspartate after addition of N-phosphonacetyl-L-aspartate to the enzyme, the transition rate is more than 1 order of magnitude slower than with the natural substrates Escherichia coli
UTP addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information concerted transition between structural and functional states of either low affinity, low activity or high affinity, high activity for aspartate. Addition of ATP along with the substrates increases the rate of the transition from the T to the R state and also decreases the duration of the R-state steady-state phase. Addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the T-R transition and causes a shift in the enzyme population towards the T state even at saturating substrate concentrations Escherichia coli ?
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