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

Uses

Different sources of media describe the Uses of 56632-86-1 differently. You can refer to the following data:
1. The unnatural enantiomer of Chlorotryptophan
2. The unnatural enantiomer of Chlorotryptophan.

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

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

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

One-Pot Biocatalytic Synthesis of Substituted d -Tryptophans from Indoles Enabled by an Engineered Aminotransferase

d-Tryptophan and its derivatives are important precursors of a wide range of indole-containing pharmaceuticals and natural products. Here, we developed a one-pot biocatalytic process enabling the synthesis of d-tryptophans from indoles in good yields and high enantiomeric excess (91% to >99%). Our method couples the synthesis of l-tryptophans catalyzed by Salmonella enterica tryptophan synthase with a stereoinversion cascade mediated by Proteus myxofaciens l-amino acid deaminase and an aminotransferase variant that we engineered to display native-like activity toward d-tryptophan. Our process is applicable to preparative-scale synthesis of a broad range of d-tryptophan derivatives containing electron-donating or -withdrawing substituents at all benzene-ring positions on the indole group.