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Merck

A1632

Sigma-Aldrich

DL-7-Azatryptophan hydrate

≥98% (TLC)

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About This Item

Fórmula empírica (notación de Hill):
C10H11N3O2 · H2O
Número de CAS:
Peso molecular:
223.23
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26

product name

DL-7-Azatryptophan hydrate,

assay

≥98% (TLC)

form

powder

color

white to off-white

storage temp.

−20°C

SMILES string

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

Biochem/physiol Actions

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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C H Chen et al.
Journal of bacteriology, 169(3), 1107-1113 (1987-03-01)
The addition of DL-7-azatryptophan (AZAT), a tryptophan analog, to continuous cultures of Anabaena sp. strain CA grown with 10 mM nitrate as the nitrogen source resulted in the differentiation of heterocysts. Analysis of the intracellular amino acid pools of Anabaena
H Rosenfeld et al.
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
Fernando Formaggio et al.
Advances in experimental medicine and biology, 527, 731-737 (2004-06-23)
Aal and 7-Atrp, quasi-isosteric with Trp, have been inserted together with a TOAC residue in two 3(10)-helical, model hexapeptides. The interaction of photoexcited AA1 and 7-Atrp with the nitroxide group of TOAC was investigated by time resolved EPR. Both peptides
Arnaldo L Serrano et al.
The journal of physical chemistry. B, 116(35), 10631-10638 (2012-08-16)
The villin headpiece subdomain (HP35) has become one of the most widely used model systems in protein folding studies, due to its small size and ultrafast folding kinetics. Here, we use HP35 as a test bed to show that the
Julie M G Rogers et al.
Analytical biochemistry, 399(2), 182-189 (2009-12-29)
Fluorescence resonance energy transfer (FRET) provides a powerful means to study protein conformational changes. However, the incorporation of an exogenous FRET pair into a protein could lead to undesirable structural perturbations of the native fold. One of the viable strategies

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