Disease relevance of NSC19495

• Nitrogen starvation mediated by DL-7-azatryptophan in the cyanobacterium Anabaena sp. strain CA [1].
• Biosynthetic incorporation of 7-azatryptophan into the phage lambda lysozyme: estimation of tryptophan accessibility, effect on enzymatic activity and protein stability [2].
• Tropomyosin mutants containing either tryptophan (122W), 5-hydroxytryptophan (5OH122W) or 7-azatryptophan (7N122W) have been expressed in Escherichia coli and their fluorescence properties studied [3].

High impact information on NSC19495

• Replacement of 7-azatryptophan for tryptophan in two positions on the catalytic chain of aspartate transcarbamylase results in changes in the enzyme's homotropic and heterotropic interactions although there is no change in the enzyme's specific activity [4].
• Beta-Galactosidase was induced with isopropyl-beta-D-thiogalactopyranoside in the presence of 7-azatryptophan, a tryptophan analogue that is incorporated into proteins and renders the beta-galactosidase formed inactive [5].
• Replacement of the four tryptophans of plasminogen activator inhibitor type-1 (PAI-1) with the spectrally unique analogue 7-azatryptophan permitted observations of conformational changes in the serpin but not those of the proteinase [6].
• 5-Hydroxytryptophan and 7-azatryptophan have red-shifted absorbance spectra, and the latter has a red-shifted fluorescence, which is very sensitive to its environment (being heavily quenched in water) [7].
• The in vitro activity of carbamyl phosphate synthetase and glutaminase increased severalfold in the presence of azatryptophan [8].

Gene context of NSC19495

• Phosphorescence emission of 7-azatryptophan and 5-hydroxytryptophan in fluid solutions and in alpha2 RNA polymerase [9].
• In vivo properties of thiol inhibitors of the three vasopeptidases NEP, ACE and ECE are improved by introduction of a 7-azatryptophan in P2' position [10].

References