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Last Updated: 3 years ago

Possible Interaction: Adenosine Triphosphate and Aspartic Acid

Research Papers that Mention the Interaction

In contrast, mutation of Glu to Asp markedly increases the affinity of NBD2 for ATP while decreasing its ability to hydrolyze ATP and to release ADP.
Journal of Biological Chemistry  •  2003  |  View Paper
In Raf-1 the phosphorylation or mutation to aspartic acid of two key tyrosine residues upstream of the ATP binding site has been demonstrated to significantly potentiate catalytic activity.
Oncogene  •  1997  |  View Paper
The ATP decrease was suppressed by either the D or M treatment, such that after 5 minutes ATP levels were 63% and 64% of each basal level, respectively.
Journal of neurosurgical anesthesiology  •  2015  |  View Paper
Mutation Thr-204 ->Asp resulted in a 8-fold increase in the ATP binding constant and in a 2-fold increase in the kcat, thus indicating that Thr-204 may be located in the ATP-binding region of luciferase.
Biokhimiia  •  1996  |  View Paper
The size of products synthesized by the A and D forms on poly(dA) x oligo(dT)10 increased by a factor of 3-6 in the presence of ATP.
The Journal of biological chemistry  •  1983  |  View Paper
In the valine and aspartic acid systems, ATP induced a modification of the tRNA-enzyme complex leading to differences in the hydrolysis pattern of the 3'-accepting region.
European journal of biochemistry  •  1982  |  View Paper
A body of data has been … which appears to demonstrate that ATP synthesis is considerably more sensitive to inhibition by aurovertins B and D than are reactions that rely on the hydrolysis of ATP (Lardy et al., 1964; Lenaz, 1965; Lee & Ernster, 1968; Roberton et al., 1968; Bertina etal.,
Biochemical Society transactions  •  1977  |  View Paper
In the presence of Na + and ATP the high affinity of the enzyme for K + became reduced by d,l -aspartic acid , lowering at the same time the K 0.5 value.
Biochemical pharmacology  •  1975  |  View Paper
Both AMP and ATP inhibit the oxidation of aspartic acid by kidney homogenate.
Biochimica et biophysica acta  •  1954  |  View Paper
Interactions between these Asp and ATP are observed in all structures available for members of the superfamily, consistent with a critical role in substrate binding and catalysis for this invariant residue.
Archaea  •  2012  |  View Paper
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