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Last Updated: 2 years ago

Possible Interaction: Adenosine Triphosphate and Lysine

Research Papers that Mention the Interaction

These residues probably interact with the triphosphate tail of ATP , positioning it for nucleophilic attack by the active site lysine.
The Journal of Biological Chemistry  •  1999  |  View Paper
As this lysine is essential for the interaction with ATP , acetylation of this residue inhibits cdk2 activity.
Nucleic acids research  •  2009  |  View Paper
Substituting a lysine for H319 reduced the EC50 for ATP 40‐fold.
The Journal of physiology  •  2002  |  View Paper
In other ATP binding cassette transporters, mutations of the lysine have been shown to reduce or abrogate the ATP hydrolysis activity and in some cases impair nucleotide binding.
The Journal of Biological Chemistry  •  2001  |  View Paper
ATP blocks the reaction with the lysine residue, but at higher concentrations compared with those for the native pump, in agreement with the lower ATP-binding affinity found previously.
European journal of biochemistry  •  1998  |  View Paper
ATP also inhibited the active uptake of lysine , alanine, valine, and isoleucine.
Biochimica et biophysica acta  •  1971  |  View Paper
With increasing pH, the interaction efficiency between the phosphate group of ATP and the protonated ammonium group of Lys increased significantly, while that with carboxyl group in Lys decreased.
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy  •  2011  |  View Paper
These findings suggest that Lys 306 is not essential for ATP binding, but does play a role in bringing about the conformational changes that mediate interactions between the ATP and UTP sites, and between the ATP-binding site and the glutamine amide transfer domain.
Biochimica et biophysica acta  •  2006  |  View Paper
However, alteration of Lys 782 increased the Km value for ATP 28-fold, indicating a role for Lys 782 in binding ATP.
Archives of biochemistry and biophysics  •  1999  |  View Paper
This lysine is known to interact with the substrate ATP , but otherwise its role is not well understood.
Biochemistry  •  1996  |  View Paper
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