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Discover Supplement-Drug Interactions

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Possible Interaction: Aspartic Acid and Lysine


Aspartic Acid



Research Papers that Mention the Interaction

Substitution of arginine and lysine with negatively charged aspartic acid residues blocked nuclear localization.
PloS one  •  2011  |  View Paper
The placing of aspartic acid and histidine residues at interacting positions with lysine modulates the steps involved in early peptide glycation (reversible Schiff base formation and its subsequent irreversible conversion to a ketoamine product, the Amadori rearrangement).
Chemistry & biology  •  2001  |  View Paper
On the other hand, canavanine (45% of maximum activity) and lysine (13%) stimulated the incorporation of aspartic acid , whereas aspartic acid beta-methyl ester (53%) and asparagine (9%) stimulated the incorporation of arginine.
Applied and environmental microbiology  •  2001  |  View Paper
Here, we show … negatively charged aspartic acid situated close … positively charged lysine can attenuate both of these effects in a position-specific manner, suggesting that intra- or intermolecular charge pairing can … interactions between positively charged residues in the nascent chain and parts of the secretory machinery or membrane phospholipids.
The Journal of biological chemistry  •  1993  |  View Paper
Substitution of the P2 lysine to aspartic acid decreased processing and little or no processing was detected when both the P4 and P2 were mutated to lysine and aspartic acid, respectively.
  •  1992  |  View Paper
Either aspartic acid or glutamic acid further enhanced LT synthesis in the presence of methionine and lysine , with aspartic acid being more stimulatory for porcine strains and glutamic acid more stimulatory for human strains.
Infection and immunity  •  1979  |  View Paper
Preloading with lysine, arginine, glutamic acid, or aspartic acid inhibited lysine transport activity; preloading with glutamine, glycine, methionine, phenylalanine, or valine had little effect; however, preloading with histidine stimulated lysine transport activity.
Journal of bacteriology  •  1976  |  View Paper
Threonine, lysine , and uracil exert a reversing effect on biotin sulfone inhibition in the presence of a moderate concentration of aspartic acid.
Archives of biochemistry and biophysics  •  1955  |  View Paper
The conservative substitutions of lysine for arginine, alanine for glycine, or glutamic acid for aspartic acid each resulted in abrogation of the cell attachment-promoting activity characteristic of the natural sequence.
Proceedings of the National Academy of Sciences of the United States of America  •  1984  |  View Paper