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Last Updated: 2 years ago

Possible Interaction: Adenosine Triphosphate and Phenylalanine

Research Papers that Mention the Interaction

Binding of ATP to the protein induced an increase in beta-structure and perturbed tryptophan, tyrosine, and phenylalanine signals observed by aromatic CD and UV difference spectroscopy.
Biochemistry  •  2001  |  View Paper
The phenylalanine of this motif sticks into the ATP binding pocket and blocks ATP binding as observed with inhibitor bound and, thus, inactive p38 kinase.
Structure  •  2005  |  View Paper
In the in vitro studies, a biphasic effect of phenylalanine on both enzyme substrates ( ATP and ADP) was observed, with maximal inhibition at 2.0 mM and maximal activation at 5.0 mM. Inhibition of the enzyme activity was not due to calcium chelation.
Neurochemical Research  •  2004  |  View Paper
The effect of inhibition by Phe on ATP hydrolysis appeared only at a concentration of 5.0 mM. PP had no significant effect upon nucleotide hydrolysis.
Amino Acids  •  2003  |  View Paper
ATP altered markedly the kinetics of phenylalanine inhibition.
By adopting this approach (Fig. l), it was shown, for example, that at pH 8.0 and 0.2 mM-Mgk inhibition by phenylalanine (1.25 mM) in the presence of ATP (5 mM) was sigmoidal (h 1.6).
Whereas the mechanism of coupled ATP and phenylalanine inhibition remains to be elucidated, it is clear that the interaction might have a regulatory function in uiuo.
Biochemical Society transactions  •  1980  |  View Paper
Differences in inhibition by ATP and the amino acids l-alanine and l-phenylalanine were found.
The Journal of biological chemistry  •  1973  |  View Paper
Accompanied by the key amino acids (proposed to be crucial for ATP-Mg2+ coordination), we … have noticed that some additional conserved residues (including ‘Trp’ of the PhhCW motif, and Phe ’ and ‘Tyr’ of the GFxxxxRxxYF motif) are potentially interacting with ATP during dynamics; which require further experimentation for legitimacy.
PloS one  •  2018  |  View Paper
Replacement of either Trp residue of the ATP binding pocket with Phe or Leu destabilizes the complex formed with ATP by approximately 1 kcal/mol, indicating that both Trp residues participate in interactions with ATP.
The Journal of organic chemistry  •  2005  |  View Paper
ATP , both in the absence (in case of modification with pyridoxal-5'-phosphate) and in- the presence of Mg2+ and phenylalanine (in case of modification with o-ATP) exhibits a pronounced protective effect.
Biokhimiia  •  1981  |  View Paper
Here, we report on quenched flow experiments which confirm this finding for high substrate concentrations but show that activation of phenylalanine becomes rate limiting at low concentrations of ATP and phenylalanine.
FEBS letters  •  1981  |  View Paper
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