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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
Research Papers that Mention the Interaction
“As neither of the branched chain amino acid transaminases proved to be inhibited by glycine, inhibition by glycine of the uptake of valine by the tissues became likely.”
“ Glycine was found to … competitive inhibitor of valine uptake, with a Ki of 4.9 mM. It is concluded that the tendency to a decreased rate of valine disappearance … blood in non-ketotic hyperglycinemia could be due to an inhibition of valine uptake by the high plasma glycine concentration.”
Studies on the valine sensitivity in non-ketotic hyperglycinemia.“HD causes a significant decrease in CSF/P ratios of branched chain AA (BCAA) and a significant increase in CSF Glycine/Valine ratio, suggesting an augmented brain uptake of Glycine at detriment of Valine.”
“Alpha-aminoisobutyric acid, valine , and thioproline are also shown to inhibit glycine uptake.”
“Replacing a glycine with valine in the turn between the last two β-strands (Gly121Val) slows the folding process by more than three orders of magnitude.”
Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR“In addition, glutamine (Q387), valine (V666), and serine (S669) substitutions were found to reduce glycine efficacy.”
“We show here that a single exchange of glycine 450 with a valine residue, or an internal deletion of amino acids 444-452, strongly interferes with the normal assembly of IFs under in vitro conditions.”
“Glycine, D- or L-serine, L-threonine, L-methionine, L-alanine, and L-valine all individually protected against the inactivation of glycine , L-serine, L-threonine, L-methionine, L-alanine, L-valine, L-proline, and beta-alanine transport, while L-proline, beta-alanine,”
“Substitution of phenylalanine for valine increased, and substitution of lysine or glycine for valine considerably decreased the rate of phosphorylation.”
“ Glycine and valine are partially competitive inhibitors and homoarginine, alanine and methionine are completely competitive.”
“Substitution of glycine 88 with valine (Gly88Val) destabilizes staphylococcal nuclease by 1.0 kcal mole-1 and reduces its sensitivity to the denaturant guanidine hydrochloride, a phenomenon which may indicate an increase in residual structure in the denatured state.”
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
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