7303-50-6

Basic information

• Product Name: 7-AZATRYPTOPHAN
• Synonyms: DL-7-AZATRYPTOPHANE extrapure;7-Aza-DL-tryptophan;1H-Pyrrolo[2,3-b]pyridine-3-alanine;Aza-T;NSC 19495;DL-7-Azatryptophan hydrochloride;2-Amino-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)propanoic acid, 3-(2-Amino-2-carboxyethyl)-1H-pyrrolo[2,3-b]pyridine;1H-pyrrolo[2,3-b]pyridine (R)-2-aminopropanoate
• CAS NO: 7303-50-6
• Molecular Formula: C₁₀H₁₁N₃O₂
• Molecular Weight: 205.21
• Product Categories: Fluorescent Labels & Indicators;A - H;Amino Acids;Modified Amino Acids;Indole Derivatives;amino;Amino Acids 13C, 2H, 15N;Peptide;Amino Acids & Derivatives
• Mol File: 7303-50-6.mol

Chemical Properties

• Melting Point: 275°C dec.
• Boiling Point: 466.1 °C at 760 mmHg
• Flash Point: 235.7 °C
• Appearance: Slightly off-white/Crystalline Powder
• Density: 1.434 g/cm³
• Storage Temp.: −20°C
• PKA: 2.20±0.10(Predicted)
• CAS DataBase Reference: 7-AZATRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 7-AZATRYPTOPHAN(7303-50-6)
• EPA Substance Registry System: 7-AZATRYPTOPHAN(7303-50-6)

Safety Data

• WGK Germany: 3
• RTECS: UY8810000
• Hazardous Substances Data: 7303-50-6(Hazardous Substances Data)

Usage

Uses

Used in Biochemistry Research:
7-AZATRYPTOPHAN is used as a fluorescent probe for investigating the structure and dynamics of proteins and peptides. Its incorporation into these biomolecules enables researchers to gain insights into their conformational changes, folding mechanisms, and interactions with other molecules, which can be crucial for understanding their functions and potential applications in medicine and biotechnology.

InChI:InChI=1/C10H11N3O2/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)

Upstream product

• 211179-97-4 diethyl 2-((1H-pyrrolo[2,3-b]pyridin-3-yl)methyl)-2-acetamidomalonate 
• 87358-28-9 N,N,N-trimethyl-1-(1H-pyrrolo[2,3-b]pyridin-3-yl)methanaminium iodide 
• 271-63-6 7-Azaindole 
• 5654-92-2 7-azagramine 

Downstream Products

• 4649-12-1 2-(1H-pyrrolo[2,3-b]pyridin-3-yl)-ethylamine 
• 134235-82-8 (-)-(R)-7-azatryptophan 
• 49758-35-2 (S)-2-amino-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)propanoic acid 
• 737007-45-3 C₂₅H₂₁N₃O₄ 
• 1295647-38-9 (5aR,10R)-10-benzo[1,3]dioxol-5-yl-7-[(R)-1-benzylpyrrolidin-3-yl]-5,5a,7,8,10,11-hexahydro-1,7,9a,11-tetraaza-benzo[b]fluorene-6,9-dione 

Relevant articles and documents

MACROCYCLIC INHIBITORS OF THE PD-1/PD-L1 AND CD80 (B7-1)/PD-LI PROTEIN/PROTEIN INTERACTIONS

The present disclosure provides novel macrocyclic peptides which inhibit the PD-1/PD-L1 and PD-L1/CD80 protein/protein interaction, and thus are useful for the amelioration of various diseases, including cancer and infectious diseases.

Biosynthesis of violacein, structure and function of L-tryptophan oxidase VioA from chromobacterium violaceum

Violacein is a natural purple pigment of Chromobacterium violaceum with potential medical applications as antimicrobial, antiviral, and anticancer drugs. The initial step of violacein biosynthesis is the oxidative conversion of L-tryptophan into the corresponding α-imine catalyzed by the flavoenzyme L-tryptophan oxidase (VioA). A substrate-related (3-(1H-indol-3-yl)-2-methylpropanoic acid) and a product-related (2-(1H-indol-3-ylmethyl)prop-2-enoic acid) competitive VioA inhibitor was synthesized for subsequent kinetic and x-ray crystallographic investigations. Structures of the binary VioA?FADH2 and of the ternary VioA?FADH2 ?2-(1H-indol-3-ylmethyl)prop-2-enoic acid complex were resolved. VioA forms a "loosely associated" homodimer as indicated by small-angle x-ray scattering experiments. VioA belongs to the glutathione reductase family 2 of FAD-dependent oxidoreductases according to the structurally conserved cofactor binding domain. The substrate-binding domain of VioA is mainly responsible for the specific recognition of L-tryptophan. Other canonical amino acids were efficiently discriminated with a minor conversion of L-phenylalanine. Furthermore, 7-aza-tryptophan, 1-methyl-tryptophan, 5-methyl-tryptophan, and 5-fluoro-tryptophan were efficient substrates of VioA. The ternary product-related VioA structure indicated involvement of protein domain movement during enzyme catalysis. Extensive structure-based mutagenesis in combination with enzyme kinetics (using L-tryptophan and substrate analogs) identified Arg64 , Lys269 , and Tyr309 as key catalytic residues of VioA. An increased enzyme activity of protein variant H163A in the presence of L-phenylalanine indicated a functional role of His163 in substrate binding. The combined structural and mutational analyses lead to the detailed understanding of VioA substrate recognition. Related strategies for the in vivo synthesis of novel violacein derivatives are discussed.