Allen Institute for Artificial Intelligence
supp.ai logo
supp.ai

Discover Supplement-Drug Interactions

Disclaimer: The information contained herein should NOT be used as a substitute for the advice of an appropriately qualified and licensed physician or other health care provider. The tool is not a substitute for the care provided… (more)
Last Updated: 2 months ago

Possible Interaction: Threonine and Valine

supplement:

Threonine

supplement:

Valine

Research Papers that Mention the Interaction

Among amino acids, glycine, lysine, and total amino acids were positively correlated with birth weight, whereas valine and threonine showed a negative correlation.
American journal of obstetrics and gynecology  •  1975  |  View Paper
Threonine was most effective in increasing the degree of parasitaemia but its effect was further enhanced when it was combined with dietary excess of certain other amino acids, notably valine , isoleucine and methionine.
Transactions of the Royal Society of Tropical Medicine and Hygiene  •  1984  |  View Paper
Hydroxynorvaline DL-alpha-amino-beta-hydroxyvaleric acid ) was shown to competitively inhibit the activation of threonine and valine when tested with tRNA and synthetases prepared from whole chick embryos.
The Journal of biological chemistry  •  1975  |  View Paper
In fact, dual supplementation with Thr and Val showed synergy on the 2HB fraction of the polymer.
Journal of bioscience and bioengineering  •  2019  |  View Paper
Our work shows the crucial role of the cis-Pro loop, as changing valine to threonine in this motif completely abolishes the protein function in vivo.
Front. Microbiol.  •  2016  |  View Paper
This analysis suggests that isoleucine is a negative effector, and valine is a very weak positive effector, but that at high concentrations valine inhibits activity by competing with threonine for binding to the active site.
Biochemistry  •  2008  |  View Paper
Substitution of residue 42 with alanine and residue 58 with alanine or valine in the presence of threonine 195 results in trypsin variants that are 102–104‐fold less active than wild type in kcat/KM but >106‐fold more active than the Ser 195 → Thr single variant.
Protein science : a publication of the Protein Society  •  2006  |  View Paper
Two additional threonines are located near the canonical start of the kinase domain, and their individual mutation to valine strongly inhibits receptor phosphorylation and signaling activity.
The EMBO journal  •  1995  |  View Paper
L-Valine at high concentration acts as a substrate analogue and competitively inhibits L-threonine binding at the active site; the K1 is 1.6 x 10(-2) M.
Canadian journal of microbiology  •  1980  |  View Paper
These results suggest that threonine inhibits B. subtilis by causing valine starvation.
Journal of bacteriology  •  1979  |  View Paper
Show More