Literature summary for 2.1.3.2 extracted from

Velyvis, A.; Schachman, H.K.; Kay, L.E.
Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase (2009), J. Mol. Biol., 387, 540-547.

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Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model	Escherichia coli
CTP	the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)