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Last Updated: 3 years ago

Possible Interaction: Lysine and Vitamin B 6

supplement:

Lysine

supplement:

Vitamin B 6

Research Papers that Mention the Interaction

Covalent modification of lysines 212 and 191 with pyridoxal phosphate results in a decreased affinity of the enzyme for erythrocyte membranes if the enzyme-linked pyridoxal phosphate is not reduced prior to binding.
Biochemical and biophysical research communications  •  1983  |  View Paper
These results suggest that pyridoxal 5′-phosphate modified a lysine residue in the adenosine 3′-phosphate 5′-phosphosulfate-recognizing site of the sulfotransferase.
Glycoconjugate Journal  •  2004  |  View Paper
A specific lysine was found to stoichiometrically react with pyridoxal 5'-phosphate forming a reversible Schiff base which could be reduced with NaBH4.
The Journal of biological chemistry  •  1981  |  View Paper
Class C reagents finally, like pyridoxal phosphate or diethyl pyrocarbonate, modified the active-site lysine or histidine, respectively, and blocked antiport and uniport activity.
European journal of biochemistry  •  1992  |  View Paper
Limited proteolysis of the enzyme modified with [3H]PLP by trypsin suggests that PLP specifically modifies the lysine residue located in the 16-kDa fragment of the enzyme cleaved by trypsin.
These results suggested that PLP binds to a specific lysine residue in the nucleotide-binding site or a region in its vicinity and inhibits the substrate binding or phosphorylation step of (H+ + K+)-ATPase.
The Journal of biological chemistry  •  1988  |  View Paper
The effect of PLP was readily reversed by the addition of lysine.
Endocrinology  •  1985  |  View Paper
It is noteworthy that pyridoxal phosphate and NaSCN increased the number of sites when added directly to nuclear KCl extract, and the effect of pyridoxal phosphate and NaSCN was reversed by treatment with L-lysine and dialysis against KCl, respectively.
Biochimica et biophysica acta  •  1983  |  View Paper
The stabilization afforded by binding of the aldehyde form pyridoxal phosphate ) which exists as an internal Schiff's base with Lys 258 is diminished when this bond is chemically reduced or when the aldehyde is replaced by an amine (pyridoxamine phosphate).
The Journal of biological chemistry  •  1981  |  View Paper
All of these results strongly suggest that pyridoxal phosphate inhibited fatty acid synthetase by forming a Schiff base with the ϵ-amino group of lysine in the enoyl-CoA reductase domain of the enzyme.
Archives of biochemistry and biophysics  •  1980  |  View Paper
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