Disease relevance of NSC9363

• The protein was derived from E. coli grown on a medium containing a 50:50 mixture of 5-fluorotryptophan and [2,4,6,7-2H4]-5-fluorotryptophan [1].
• Employing an optimized incorporation strategy, the small cold shock protein from the bacterium Thermotoga maritima (TmCsp) was labeled with 5-fluorotryptophan [2].
• A 5-fluorotryptophan-resistant mutant, termed 1041, was isolated from Brevibacterium lactofermentum AJ12036 [3].
• The average survival time after the diagnosis of advanced metastatic carcinoid disease was made and prior to the initiation of treatment with 5-fluorotryptophan in these patients was 5.5 years, varying from one to eight years [4].
• Isolation and characterization of the Bacillus subtilis tryptophanyl-tRNA synthetase gene (trpS) conferring 5-fluorotryptophan resistance and temperature sensitivity [5].

High impact information on NSC9363

• The fluorine nucleus was biosynthetically incorporated into the lac repressor with either 5-fluorotryptophan or 3-fluorotyrosine [6].
• In the presence of 5-fluorotryptophan a relatively stable oxyferroheme enzyme complex was generated with the fully reduced form of pseudomonad tryptophan oxygenase [7].
• This work reports an explanation for the unusual monoexponential fluorescence decay of 5-fluorotryptophan (5FTrp) in single-Trp mutant proteins [Broos, J.; Maddalena, F.; Hesp, B. H. J. Am. Chem. Soc. 2004, 126, 22-23] and substantially clarifies the origin of the ubiquitous nonexponential fluorescence decay of tryptophan in proteins [8].
• Of all the compstatin analogues, peptides containing 1-methyltryptophan at position 4 exhibited the highest binding affinity (Kd = 15 nM) and activity (IC50 = 0.205 microM), followed by a peptide containing 5-fluorotryptophan at position 7 [9].
• Biosynthetic incorporation of 5-fluorotryptophan (5F-Trp) into wild-type PAI-1 (5FW wtPAI-1) and the single tryptophan mutants (5FW86, 5FW139, 5FW175, and 5FW262) was achieved, allowing a (19)F NMR spectroscopic study of PAI-1 in its active and cleaved forms and in complex with t-PA [10].

Chemical compound and disease context of NSC9363

• 19F NMR relaxation studies on 5-fluorotryptophan- and tetradeutero-5-fluorotryptophan-labeled E. coli glucose/galactose receptor [1].
• Growth of Escherichia coli in the presence of glyphosate, an inhibitor of aromatic amino acid biosynthesis, has permitted the production of proton translocating ATPase that is specifically labelled with 5-fluorotryptophan [11].
• Life in patients with advanced metastatic carcinoid disease has been extended with good to excellent quality by the simple oral administration of the tryptophan analog, 5-fluorotryptophan [4].
• 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues [12].

Biological context of NSC9363

• A derepressed mutant selected by resistance to 5-fluorotryptophan was found to have elevated basal levels of trp gene expression; these basal levels were increased only two- to threefold by tryptophan limitation [13].
• Site-specific information on the protein conformation has been obtained by biosynthetic incorporation of an unnatural amino acid, 5-fluorotryptophan (5FW), into the recombinant protein [14].

Anatomical context of NSC9363

• The mechanism of killing of A9 fibroblasts by 5-fluorotryptophan has been studied [15].
• 5-fluorotryptophan resistant mutants affecting the A and L transport systems in the mouse L cell line A9 [16].
• Protoplasts of this organism made novel products when they were incubated with DL-5-fluorotryptophan or DL-6-fluorotryptophan [17].

Associations of NSC9363 with other chemical compounds

• Lactose permease activity is 35% of the control in the presence of 4- and 6-fluorotryptophan, less than 10% in the presence of 5-fluorotryptophan [18].
• Mutant strains, resistant against the amino acid analogues 5-methyltryptophan, 5-fluorotryptophan and canavanine were isolated, starting with a trp2 leaky auxotrophic strain [19].

Gene context of NSC9363

• Three glycolytic enzymes, hexokinase, phosphoglycerate kinase, and pyruvate kinase, were fluorine labeled in the yeast Saccharomyces cerevisiae by biosynthetic incorporation of 5-fluorotryptophan [20].
• By biosynthetic incorporation of 5-fluorotryptophan, we obtained an inhibitor of MMP-2 and MMP-9 gelatinases that showed a 6-fold enhancement in serum stability in comparison to the wild-type peptide [21].
• Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study [22].
• Yeast phosphoglycerate kinase was selectively fluorine-labeled in vivo by inducing enzyme synthesis in stationary phase cells in the presence of 5-fluorotryptophan [23].
• Wild-type D-lactate dehydrogenase and mutants in which an additional tryptophan is substituted in selected areas by site-specific oligonucleotide-directed mutagenesis have been labeled with 5-fluorotryptophan [24].

Analytical, diagnostic and therapeutic context of NSC9363

• Twenty-two patients with advanced metastatic carcinoid disease, most of whom were moribund were subjected to oral administration of 200 mg of 5-fluorotryptophan three times daily [4].

References