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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
Research Papers that Mention the Interaction
“Mutagenesis of either of the cysteines to glycine increased the resistance of the enzyme, which retained 46% of activity in presence of 150 microM Cu(2+), compared to only 27% of the activity retained by the wild type enzyme (WT).”
“Replacement of both the cysteines with glycines resulted in retention of over 65% activity.”
Importance of the free sulfhydryl groups of lecithin-cholesterol acyltransferase for its sensitivity to oxidative inactivation.“Insertion of an extra glycine between the vicinal cysteines in either D domain inhibited multimerization of dimers, whereas alteration of lysine to glycine in both domains (residues 157 and 519) had no effect.”
“The sequence specific thermal stability calculations shed some light on why some mutations of cysteine for glycine have greater effects on the thermal stability than others.”
“Without formal statistic testing, the authors concluded that the ‘‘more aggressive’’ glycine and serine substitutions for the cysteine at codon 609 entailed a higher risk than arginine and tyrosine substitutions.”
“Retained N was not affected by Cys in the absence of Gly, but was increased by Cys when Gly was supplemented (interaction, p = 0.01).”
“Supplemental Gly improved responses to supplemental Met and Cys.”
Effect of glycine and vitamin supplementation on sulphur amino acid utilization by growing cattle.“Replacement of the respective cysteine with glycine in the skeletal RLC has markedly changed the regulatory properties of the molecule.”
“Phenylalanine and tyrosine inhibit one site; proline and the straight-chain amino acids, alanine, methionine and cysteine inhibit another; and glycine and the branched-chain valine, leucine, and isoleucine inhibit a 3rd.”
“The solution structure of DxM1 exists, like wild type Dx, as a dimer in solution although the single glycine inserted between the adjacent cysteines disrupts the stability of the dimer resulting in exchange between a dimer state and a small population of another, probably monomeric, state.”
NMR solution structures of two mutants of desulforedoxin.“Unexpectedly, substitution of the cysteine with glycine results in the inhibition of cell growth and the mutant allele can be maintained in the cells only when it is poorly expressed.”
“The mutagenicity of allyl glycine is relieved by cysteine , and to a lesser extent by homocysteine, methionine, or alpha-amino-n-butyric acid.”
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