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Last Updated: 3 months ago

Possible Interaction: Aspartic Acid and Glutamic Acid

supplement:

Aspartic Acid

supplement:

Glutamic Acid

Research Papers that Mention the Interaction

The frequency of occurrence of glutamic acid (36.90%) was higher than that of aspartic acid (27.02%).
Molecular bioSystems  •  2015  |  View Paper
Parallel studies showed that glutamic acid and aspartic acid are relatively inefficient in metal ion binding.
Journal of Alzheimer's disease : JAD  •  2010  |  View Paper
Concentrations of aspartic and glutamic acids , Phe, and Tyr were positively correlated and 17 amino acids were negatively correlated with the interval between feeding and blood draw.
Journal of the American College of Nutrition  •  1999  |  View Paper
The intensity of intrinsic fluorescence of B decreased in the presence of aspartic acid and glutamic acid (Kd = 0.48 mM for aspartic acid and 0.24 mM for glutamic acid).
Complement  •  1987  |  View Paper
Cross-linking of glutamic acid and aspartic acid residues in proteins will greatly expand the scope of structural mass spectrometry.
Analytical chemistry  •  2018  |  View Paper
L-glutamic acid transport was found to be competitively inhibited by L-aspartic acid.
Journal of applied microbiology  •  2001  |  View Paper
When residues of both an aspartic acid and a glutamic acid of SF were methylated or amidated, the activity increased by 20%, although their water solubility was lost.
Biochimica et biophysica acta  •  2000  |  View Paper
Substitution at glutamic acid-86 or -177 with glutamine (Gln), aspartic acid (Asp), or glycine (Gly) inhibited the beta-1-4-endoxylanase activity.
Plant physiology  •  1999  |  View Paper
Substitution of an aspartic acid for glutamic acid 166 of the Slt-IIA subunit decreased the capacity of the polypeptides to inhibit protein synthesis at least 100-fold in a cell-free translation system.
Journal of bacteriology  •  1990  |  View Paper
Multiple inhibition of the glutaminase activity by L-glutamic acid and L-aspartic acid indicated that these ligands are mutually exclusive at the product-releasing site.
Biochemical pharmacology  •  1983  |  View Paper
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