55325-48-9

Basic information

• Product Name: 5-CHLORO-D-TRYPTOPHAN
• Synonyms: 5-CHLORO-D-TRYPTOPHAN;D-Tryptophan, 5-chloro-;D-5-ChloroTryptophan;(R)-2-Amino-3-(5-chloro-1H-indol-3-yl)propanoic acid
• CAS NO: 55325-48-9
• Molecular Formula: C11H11ClN2O2
• Molecular Weight: 238.67
• Mol File: 55325-48-9.mol

Chemical Properties

• Boiling Point: 476.906°C at 760 mmHg
• Flash Point: 242.224°C
• Appearance: /
• Density: 1.475g/cm3
• PKA: 2.21±0.10(Predicted)
• CAS DataBase Reference: 5-CHLORO-D-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 5-CHLORO-D-TRYPTOPHAN(55325-48-9)
• EPA Substance Registry System: 5-CHLORO-D-TRYPTOPHAN(55325-48-9)

Safety Data

• Hazardous Substances Data: 55325-48-9(Hazardous Substances Data)

Usage

Uses

Used in Scientific Research:
5-Chloro-D-tryptophan is utilized as a building block for the synthesis of various bioactive compounds, including antimicrobial peptides and drugs. Its structural modifications can lead to altered pharmacological properties, making it a valuable tool in drug design and development.
Used in Pharmaceutical Development:
The unique structural modifications of 5-chloro-D-tryptophan allow it to serve as a key component in the creation of new pharmaceuticals. Its ability to alter the pharmacological properties of synthesized compounds makes it an essential resource in the advancement of drug discovery and innovation.
Used in Cancer Therapy:
5-Chloro-D-tryptophan has been found to exhibit antitumor activity, which positions it as a potential candidate for cancer therapy. Its application in this field could contribute to the development of novel treatment options for various types of cancer.

InChI:InChI=1S/C11H11ClN2O2/c12-7-1-2-10-8(4-7)6(5-14-10)3-9(13)11(15)16/h1-2,4-5,9,14H,3,13H2,(H,15,16)

Upstream product

• 154-07-4 2-amino-3-(5-chloro-1H-indol-3-yl)propanoic acid 
• 74761-41-4 (S)-1-(methoxycarbonyl)pyrrolidine-2-carboxylic acid 
• 147-85-3 L-proline 
• 67811-44-3 5-chloro-N_b-methoxycarbonyl-L-tryptophan methyl ester 
• 93299-30-0 N-methoxycarbonyl-L-glutamine methyl ester 
• 93271-96-6 (2S,5RS)-1,2-dimethyl-5-hydroxypyrrolidine-1,2-dicarboxylate 
• 93271-98-8 N-methoxycarbonyl-4-cyano-L-2-aminobutyric acid methyl ester 
• 83541-81-5 (S)-dimethyl pyrrolidine-1,2-dicarboxylate 
• 93299-36-6 5-chloro-L-tryptophan methyl ester 
• 67811-39-6 8-Acetyl-3,3a,8,8a-tetrahydro-2H-pyrrolo[2,3-b]indole-1,2-dicarboxylic acid dimethyl ester 
• 67811-44-3 5-chloro-N_b-methoxycarbonyl-D-tryptophan methyl ester 
• 93299-36-6 5-chloro-D-tryptophan methyl ester 

Relevant articles and documents

METHODS FOR PRODUCING D-TRYPTOPHAN AND SUBSTITUTED D-TRYPTOPHANS

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism; and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. As disclosed herein, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted D-tryptophan analogs in high enantiomeric excess.

Complete Stereoinversion of l -Tryptophan by a Fungal Single-Module Nonribosomal Peptide Synthetase

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. Here, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of l-tryptophan to d-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes d-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted d-tryptophan analogs in high enantiomeric excess.

Syntheses of Substituted L- and D-Tryptophans

Several 5-substituted nb-methoxycarbonyl-L- and -D-tryptophan derivatives were synthesized from proline by a new route involving electrochemical oxidation, as well as by the known procedures.Removal of the Nb-methoxycarbonyl group was accomplished by treatment with Me3SiI in refluxing chloroform, then alkaline hydrolysis of the methyl esters afforded 5-substituted L- and D-tryptophans with high optical purities.Keywords - L-tryptophan 5-substituted; D-tryptophan 5-substituted; anodic oxidation; N-methoxycarbonyl group deprotection; Fischer indole synthesis; iodotrimethylsilane