496930-10-0

Basic information

• Product Name: 6-broMo-D-tryptophan
• Synonyms: 6-broMo-D-tryptophan;(R)-2-Amino-3-(6-bromo-1H-indol-3-yl)propanoic acid;D-Tryptophan, 6-bromo-;D-6-Bromotryptophan
• CAS NO: 496930-10-0
• Molecular Formula: C₁₁H₁₁BrN₂O₂
• Molecular Weight: 283.12124
• EINECS: -0
• Mol File: 496930-10-0.mol
• Article Data: 8

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 6-broMo-D-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-broMo-D-tryptophan(496930-10-0)
• EPA Substance Registry System: 6-broMo-D-tryptophan(496930-10-0)

Safety Data

• Hazardous Substances Data: 496930-10-0(Hazardous Substances Data)

Usage

General Description

6-bromo-D-tryptophan is a chemical compound belonging to the class of chemical entities called bromobenzenes. Bromobenzenes are compounds containing a monocyclic benzene moiety that carries one or more bromine atoms. Specifically, 6-bromo-D-tryptophan is a tryptophan derivative, essentially composed of a tryptophan molecule that is substituted by a bromine atom at the 6-position. Tryptophan is a standard amino acid that is found in most proteins. The 'D' in 6-bromo-D-tryptophan signifies that it is a D-isomer, a term relating to its stereochemistry or spatial arrangement of its atoms. 6-broMo-D-tryptophan does not have significant industrial use, but it may be used in scientific research, specifically in the study of proteins.

Upstream product

• 85515-06-6 N^α-acetyl-6-bromo-D,L-tryptophan 
• 33599-61-0 6-bromo-tryptophan(Ref_.7.) 
• 153-94-6 D-tryptophan 
• 99474-21-2 (E)-2-(4-bromo-2-nitrophenyl)-N,N-dimethylethyleneamine 
• 60956-26-5 4-bromo-2-nitrotoluene 
• 52415-29-9 6-bromo-1H-indole 

Downstream Products

• 753504-16-4 Fmoc-D-6Br-Trp 
• 774181-71-4 C₁₂H₁₃BrN₂O₂ 
• 496930-12-2 6'-bromo-N-carbobenzyloxy-D-tryptophan 

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.

General synthesis of unnatural 4-, 5-, 6-, and 7-bromo-D-tryptophans by means of a regioselective indole alkylation

A general two-step approach to enantiopure bromotryptophans from unprotected bromoindoles has been developed. Indole nucleophiles prepared with MeMgCl in the presence of CuCl reacted with cyclic sulfamidates derived from enantiopure D-serine to form 4-, 5-, 6-, or 7-bromo-D-tryptophan and some other halogenated tryptophans in moderate yields but with complete regioselectivity. The bromotryptophan derivatives were deprotected using mild conditions.

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.