2280-01-5

Basic information

• Product Name: N-ACETYL-D-TRYPTOPHAN
• Synonyms: D-N-ACETYL-2-AMINO-3-(3-INDOLYL)PROPIONIC ACID;H-N-ACETYL-D-TRP-OH;ACETYL-D-TRYPTOPHAN;AC-D-TRP-OH;AC-D-TRYPTOPHAN;N-ALPHA-ACETYL-D-TRYPTOPHAN;N-ACETYL-D-TRYPTOPHAN;N-Acetyl-D-tryptaophan
• CAS NO: 2280-01-5
• Molecular Formula: C₁₃H₁₄N₂O₃
• Molecular Weight: 246.26
• EINECS: 218-912-4
• Product Categories: Amino Acids Derivatives;Tryptophan [Trp, W];Amino Acids and Derivatives;Ac-Amino Acids;Amino Acids;Amino Acids (N-Protected);Biochemistry;Indoles;Tryptophans;N-Acetyl-Amino acid series;A - H;Amino Acids;Modified Amino Acids
• Mol File: 2280-01-5.mol

Chemical Properties

• Melting Point: 186°C
• Boiling Point: 586.6°Cat760mmHg
• Flash Point: 308.6°C
• Appearance: /
• Density: 1.33g/cm³
• Storage Temp.: −20°C
• PKA: 3.65±0.10(Predicted)
• Water Solubility: Practically insoluble in water
• CAS DataBase Reference: N-ACETYL-D-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: N-ACETYL-D-TRYPTOPHAN(2280-01-5)
• EPA Substance Registry System: N-ACETYL-D-TRYPTOPHAN(2280-01-5)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 2280-01-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
N-ACETYL-D-TRYPTOPHAN is used as an intermediate in the synthesis of peptide drugs for various therapeutic applications. Its unique chemical properties allow for the development of novel drug candidates with improved pharmacokinetic and pharmacodynamic profiles.
Used in Food and Feed Industry:
N-ACETYL-D-TRYPTOPHAN is used in the preparation of enzymes, such as Bordetella petri D-acylated tryptophan hydrolase, which catalyzes the hydrolysis of N-ACETYL-D-TRYPTOPHAN to generate D-tryptophan. This process is essential for the production of food, feed, and peptide drugs, as D-tryptophan is a valuable building block for various bioactive compounds.
Used in Chemical Synthesis:
N-ACETYL-D-TRYPTOPHAN is used as a versatile building block in the synthesis of various organic compounds, including pharmaceuticals, agrochemicals, and other specialty chemicals. Its unique structure and reactivity make it a valuable component in the development of new and innovative products.

InChI:InChI=1/C13H14N2O3/c1-8(16)15-12(13(17)18)6-9-7-14-11-5-3-2-4-10(9)11/h2-5,7,12,14H,6H2,1H3,(H,15,16)(H,17,18)

Upstream product

• 1218-34-4 N-acetyl-DL-tryptophan 
• 62-53-3 aniline 
• 2824-57-9 AcTrpOMe 
• 70082-70-1 (Z)-2-acetamido-3-(3-indolyl)-2-propenoic acid 
• 830-03-5 4-nitrophenol acetate 
• 153-94-6 D-tryptophan 
• 73-22-3 L-Tryptophan 
• 42717-06-6 acetyltryptophan ethylester 
• 120-72-9 indole 

Downstream Products

• 153-94-6 D-tryptophan 
• 1329602-51-8 C₃₂H₄₂N₄O₁₀ 
• 1402723-37-8 C₂₄H₂₇N₅O₄ 

Relevant articles and documents

Synthesis of tripeptides containing d-Trp substituted at the indole ring, assessment of opioid receptor binding and in vivo central antinociception

The noncationizable tripeptide Ac-d-Trp-Phe-GlyNH2 was recently proposed as a novel minimal recognition motif for μ-opioid receptor. The introduction of different substituents (methyl, halogens, nitro, etc.) at the indole of d-Trp significantly influenced receptor affinities and resulted in serum stability and in a measurable effect on central antinociception in mice after ip administration.

Resolution of N-protected amino acid esters using whole cells of Candida parapsilosis ATCC 7330

Whole cells of Candida parapsilosis ATCC 7330 were used for the resolution of N-acetyl amino acid esters. Excellent enantioselectivities (E = 40 to >500) were achieved for the resolution of N-protected protein and non-protein amino acid esters giving good yields (28-50%) and high enantiomeric excesses (up to >99%) for both enantiomers.

The biosynthetic pathway of crucifer phytoalexins and phytoanticipins: De novo incorporation of deuterated tryptophans and quasi-natural compounds

Although several biosynthetic intermediates in pathways to cruciferous phytoalexins and phytoanticipins are common, questions regarding the introduction of substituents at N-1 of the indole moiety remain unanswered. Toward this end, we investigated the potential incorporations of several perdeuterated d- and l-1′-methoxytryptophans, d- and l-tryptophans and other indol-3-yl derivatives into pertinent phytoalexins and phytoanticipins (indolyl glucosinolates) produced in rutabaga (Brassica napus L. ssp. rapifera) roots. In addition, we probed the potential transformations of quasi-natural compounds, these being analogues of biosynthetic intermediates that might lead to "quasi-natural" products (products similar to natural products but not produced under natural conditions). No detectable incorporations of deuterium labeled 1′-methoxytryptophans into phytoalexins or glucobrassicin were detected. l-tryptophan was incorporated in a higher percentage than d-tryptophan into both phytoalexins and phytoanticipins. However, in the case of the phytoalexin rapalexin A, both d- and l-tryptophan were incorporated to the same extent. Furthermore, the transformations of both 1′-methylindolyl-3′-acetaldoxime and 1′-methylindolyl-3′-acetothiohydroxamic acid (quasi-natural products) into 1′-methylglucobrassicin but not into phytoalexins suggested that post-aldoxime enzymes in the biosynthetic pathway of indolyl glucosinolates are not substrate-specific. Hence, it would appear that the 1-methoxy substituent of the indole moiety is introduced downstream from tryptophan and that the post-aldoxime enzymes of the glucosinolate pathway are different from the enzymes of the phytoalexin pathway. A higher substrate specificity of some enzymes of the phytoalexin pathway might explain the relatively lower structural diversity among phytoalexins than among glucosinolates.

Heat-stable D-aminoacylase

The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective, the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Catalysis by β-cyclodextrin in the reaction of p-nitrophenyl acetate with α-amino acids

The reactions of p-nitrophenyl acetate, 1, with both enantiomers of the following α-amino acids: alanine (2a), methionine (2b), leucine (2c), and tryptophan (2d), were studied in the presence of β-cyclodextrin (β-CD).All the reactions were catalyzed by β-

Efficient Asymmetric Hydrogenations of (Z)-2-Acetamidoacrylic Acid Derivatives with the Cationic Rhodium Complex of (2S,4S)-MOD-BPPM

The preparation of (2S,4S)-MOD-BPPM ((2S,4S)-N-(t-butoxycarbonyl)-4-phosphino>-2-phosphino>methyl>pyrrolidine) and its application to highly effective asymmetric hydrogenations of (Z)-2-acetamidoacrylic acid derivatives are described.