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Last Updated: 2 years ago

Possible Interaction: Glutamine and Tryptophan

supplement:

Glutamine

supplement:

Tryptophan

Research Papers that Mention the Interaction

In particular, the substitution of Trp for the hydrophobic amino acids, Gln and Asp at positions 17 and 19 of HP (2-20) (Anal 3), caused a dramatic increase in antibiotic activity without a hemolytic effect.
Biochimica et biophysica acta  •  2002  |  View Paper
TRP and LEU decreased intake more than PHE (reductions relative to control, ~219 ± 68, ~170 ± 48 and ~12 ± 57 kcal, respectively), and TRP decreased intake more than GLN (~31 ± 82 kcal).
Physiological reports  •  2017  |  View Paper
It is postulated that the increased transport of tryptophan at the BBB occurs in exchange with glutamine.
Enzyme  •  1987  |  View Paper
The reduction in glutamine levels in the hypothalamus when NH3 and tryptophan are infused together may be explained either by an inhibition of synthesis or by an intercellular influx of neutral amino acids and an efflux of glutamine as suggested by James et al.
Hepatology  •  1986  |  View Paper
The uptake of L-tryptophan into isolated porcine microvessels is increased by preincubation with L-glutamine as well as with D-glutamine.
Brain Research  •  1986  |  View Paper
Thus, interaction between glutamine and tryptophan transport into nerve terminals may be one of the factors regulating the rate of serotonin synthesis in vivo.
Brain Research  •  1983  |  View Paper
A decrease in fluorescence life time of tryptophan residues from 3.31 ns in Hb to 2.89 ns in presence of Q at pH 5.0; surmises efficient binding of Q at the hydrophobic core housing tryptophan.
Journal of biomolecular structure & dynamics  •  2021  |  View Paper
Charged and polar residues (D, H, K, N, Q , R, S) are more incident in the immediate surrounding of tryptophan (-6, -5, -2, -1, 1, 2, 4) and hydrophobic residues (A, F, I, L, V, Y) are more rare than in remote positions.
Molekuliarnaia genetika, mikrobiologiia i virusologiia  •  2001  |  View Paper
Inhibition by tryptophan was competitive with chorismate and noncompetitive with glutamine and showed positive cooperativity.
The Journal of biological chemistry  •  1970  |  View Paper
Tryptophan acted as a noncompetitive inhibitor with respect to glutamine , one of the substrates for anthranilate synthetase, and as a competitive inhibitor of the reaction when chorismate, the other substrate, was varied.
Journal of bacteriology  •  1968  |  View Paper
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