56632-86-1

Basic information

• Product Name: 6-CHLORO-D-TRYPTOPHAN
• Synonyms: 6-CHLORO-D-TRYPTOPHAN;H-6-CHLORO-D-TRP-OH;D-2-AMINO-3-(6-CHLOROINDOLYL)PROPIONIC ACID;RARECHEM AH BS 0091;6-Chloro-(r)-Tryptophan;D-Tryptophan, 6-chloro-;D-6-Chlorotryptophan
• CAS NO: 56632-86-1
• Molecular Formula: C₁₁H₁₁ClN₂O₂
• Molecular Weight: 238.67
• Product Categories: Amino Acids 13C, 2H, 15N;Amino Acids & Derivatives;Chiral Reagents;Heterocycles
• Mol File: 56632-86-1.mol
• Article Data: 9

Chemical Properties

• Melting Point: 264-265°C
• Boiling Point: 476.9oC at 760 mmHg
• Flash Point: 242.2oC
• Appearance: /
• Density: 1.474g/cm3
• Vapor Pressure: 6.66E-10mmHg at 25°C
• Refractive Index: 1.701
• Storage Temp.: -20°C Freezer
• Solubility: Aqueous Acid, Aqueous Base, DMSO
• CAS DataBase Reference: 6-CHLORO-D-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 6-CHLORO-D-TRYPTOPHAN(56632-86-1)
• EPA Substance Registry System: 6-CHLORO-D-TRYPTOPHAN(56632-86-1)

Safety Data

• Hazardous Substances Data: 56632-86-1(Hazardous Substances Data)

Usage

Description

6-CHLORO-D-TRYPTOPHAN is an unnatural enantiomer of Chlorotryptophan, a derivative of the naturally occurring amino acid tryptophan. It is characterized by the presence of a chlorine atom at the 6th position of the tryptophan molecule. This modification can lead to unique properties and potential applications in various fields.

Uses

Used in Pharmaceutical Industry:
6-CHLORO-D-TRYPTOPHAN is used as an intermediate in the synthesis of various pharmaceutical compounds. Its unique structural features make it a valuable building block for the development of new drugs with specific therapeutic properties.
Used in Research and Development:
6-CHLORO-D-TRYPTOPHAN is utilized as a research tool in the study of protein structure, function, and interactions. Its incorporation into proteins can help researchers understand the effects of specific amino acid substitutions on protein stability, folding, and activity.
Used in Chemical Synthesis:
6-CHLORO-D-TRYPTOPHAN can be used as a starting material for the synthesis of various organic compounds, including those with potential applications in the fields of materials science, agrochemistry, and environmental science.
Used in Enzyme Inhibition Studies:
6-CHLORO-D-TRYPTOPHAN can be employed in the study of enzyme inhibition, particularly for enzymes that utilize tryptophan as a substrate. Its unnatural configuration may provide insights into the mechanisms of enzyme specificity and selectivity.
Used in Chiral Pool Synthesis:
6-CHLORO-D-TRYPTOPHAN can serve as a chiral building block in the synthesis of enantiomerically pure compounds. Its unique stereochemistry can be exploited to create novel chiral molecules with potential applications in various industries, including pharmaceuticals, agrochemicals, and fragrances.

InChI:InChI=1/C11H11ClN2O2/c12-7-1-2-8-6(3-9(13)11(15)16)5-14-10(8)4-7/h1-2,4-5,9,14H,3,13H2,(H,15,16)/t9-/m1/s1

Upstream product

• 57233-87-1 dl-N-formyl-6-chlorotryptophan 
• 56777-76-5 N^α-acetyl-6-chloro-D-tryptophan 
• 50517-10-7 N^α-acetyl-6-chloro-D,L-tryptophan 
• 17422-33-2 6-chloroindole 
• 56-45-1 L-serin 
• 153-94-6 D-tryptophan 
• 17808-21-8 6-chloro-tryptophan 

Downstream Products

• 1219168-45-2 Fmoc-D-6Cl-Trp 

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.

Targeted Enzyme Engineering Unveiled Unexpected Patterns of Halogenase Stabilization

Halogenases are valuable biocatalysts for selective C?H activation, but despite recent efforts to broaden their application scope by means of protein engineering, improvement of thermostability and catalytic efficiency is still desired. A directed evoluti

Biosynthesis of l-4-Chlorokynurenine, an Antidepressant Prodrug and a Non-Proteinogenic Amino Acid Found in Lipopeptide Antibiotics

l-4-Chlorokynurenine (l-4-Cl-Kyn) is a neuropharmaceutical drug candidate that is in development for the treatment of major depressive disorder. Recently, this amino acid was naturally found as a residue in the lipopeptide antibiotic taromycin. Herein, we report the unprecedented conversion of l-tryptophan into l-4-Cl-Kyn catalyzed by four enzymes in the taromycin biosynthetic pathway from the marine bacterium Saccharomonospora sp. CNQ-490. We used genetic, biochemical, structural, and analytical techniques to establish l-4-Cl-Kyn biosynthesis, which is initiated by the flavin-dependent tryptophan chlorinase Tar14 and its flavin reductase partner Tar15. This work revealed the first tryptophan 2,3-dioxygenase (Tar13) and kynurenine formamidase (Tar16) enzymes that are selective for chlorinated substrates. The substrate scope of Tar13, Tar14, and Tar16 was examined and revealed intriguing promiscuity, thereby opening doors for the targeted engineering of these enzymes as useful biocatalysts.