product name
DL-7-Azatryptophan hydrate,
检测方案
≥98% (TLC)
形式
powder
颜色
white to off-white
储存温度
−20°C
SMILES字符串
O.NC(Cc1c[nH]c2ncccc12)C(O)=O
InChI
1S/C10H11N3O2.H2O/c11-8(10(14)15)4-6-5-13-9-7(6)2-1-3-12-9;/h1-3,5,8H,4,11H2,(H,12,13)(H,14,15);1H2
InChI key
PXDRHYQAIUZKHN-UHFFFAOYSA-N
生化/生理作用
DL-7-Azatryptophan is a racemic mixture of D- and L-7-azatryptophan which together with L-tryptophan is a synergistic inducer of tryptophan oxygenase of Pseudomonas acidovorans. DL-7-Azatryptophan inhibits photosynthetic carbon assimilation, photosynthetic oxygen evolution and nitrogen metabolism in Anabaena sp. Strain 1F, a marine filamentous, heterocystous cyanobacterium.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
Biochemical and biophysical research communications, 219(2), 388-392 (1996-02-15)
The amino acid analogue 7-azatryptophan has attracted significant recent attention as a novel optical probe for protein structure, function and dynamics. We report here, for the first time, its fluorescence emission behavior in a membrane mimetic model system, namely reverse
Journal of peptide science : an official publication of the European Peptide Society, 16(10), 589-595 (2010-07-16)
Aequorea victoria green fluorescent protein and its widely used mutants enhanced green fluorescent protein and enhanced cyan fluorescent protein (ECFP) are ideal target proteins to study protein folding. The spectral signals of their chromophores are directly correlated with the folding
Biophysical chemistry, 48(2), 159-169 (1993-12-01)
The tryptophan analogs 5-hydroxytryptophan (5HW) and 7-azatryptophan (7AW) are capable of being biosynthetically incorporated into bacterial proteins and can be used as intrinsic fluorescence probes of protein structure, function and dynamics. A prerequisite for analog incorporation is their recognition by
Chembiochem : a European journal of chemical biology, 11(3), 305-314 (2010-01-09)
In vivo expression of colored proteins without post-translational modification or chemical functionalization is highly desired for protein studies and cell biology. Cell-permeable tryptophan analogues, such as azatryptophans, have proved to be almost ideal isosteric substitutes for natural tryptophan in cellular
Journal of bacteriology, 97(2), 697-704 (1969-02-01)
The process of induction of tryptophan oxygenase in Pseudomonas acidovorans is typical of many microbial enzyme induction systems, in that it (i) requires cell multiplication and de novo protein synthesis, (ii) is subject to catabolite repression, (iii) results in the
Chromatograms
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