139393-02-5

Basic information

• Product Name: 5-CYANO-DL-TRYPTOPHAN
• Synonyms: DL-2-AMINO-3-(5-CYANOINDOLYL)PROPIONIC ACID;H-5-CYANO-DL-TRP-OH;5-CYANO-DL-TRYPTOPHAN;RARECHEM AH BS 0097;5-Cyano-L-tryptophan;(S)-2-Amino-3-(5-cyano-1H-indol-3-yl)propanoic acid;-2-Amino-3-(5-cyano-1H-indol-3-yl)
• CAS NO: 139393-02-5
• Molecular Formula: C₁₂H₁₁N₃O₂
• Molecular Weight: 229.23
• Mol File: 139393-02-5.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• Storage Temp.: under inert gas (nitrogen or Argon) at 2–8 °C
• CAS DataBase Reference: 5-CYANO-DL-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 5-CYANO-DL-TRYPTOPHAN(139393-02-5)
• EPA Substance Registry System: 5-CYANO-DL-TRYPTOPHAN(139393-02-5)

Safety Data

• Hazardous Substances Data: 139393-02-5(Hazardous Substances Data)

Usage

Description

5-CYANO-DL-TRYPTOPHAN, also known as (S)-2-Amino-3-(5-cyano-1H-indol-3-yl)propanoic Acid, is an organic compound derived from the amino acid tryptophan. It is characterized by the presence of a cyano group (-CN) at the 5-position of the indole ring, which distinguishes it from the natural tryptophan. This modification grants 5-CYANO-DL-TRYPTOPHAN unique properties and potential applications in various fields.

Uses

Used in Pharmaceutical Industry:
5-CYANO-DL-TRYPTOPHAN is used as a building block for the synthesis of tryptophan analogues, which are essential in the development of new pharmaceutical compounds. These analogues can have altered biological activities or improved pharmacological properties compared to the native tryptophan, making them valuable for the treatment of various diseases and medical conditions.
Used in Research and Development:
In the field of research, 5-CYANO-DL-TRYPTOPHAN serves as an important tool for studying the structure and function of proteins and enzymes that interact with tryptophan. By incorporating this modified amino acid into proteins, researchers can gain insights into the role of tryptophan in protein folding, stability, and function, as well as its involvement in various biological processes.
Used in Chemical Synthesis:
5-CYANO-DL-TRYPTOPHAN can also be utilized as a starting material or intermediate in the chemical synthesis of various compounds, including pharmaceuticals, agrochemicals, and other specialty chemicals. Its unique structural features make it a versatile building block for the development of novel molecules with potential applications in various industries.

Upstream product

• 15861-24-2 1H-indole-5-carbonitrile 
• 56-45-1 L-serin 
• 79465-82-0 L-(2β,3aα,8aα)-1,2,3,3a,8,8a-hexahydro-1,2-dimethoxycarbonylpyrrolo<2,3-b>indole 
• 66377-68-2 N-(methoxycarbonyl)-L-tryptophan methyl ester 
• 79465-85-3 L-(2β,3aα,8aα)-8-acetyl-1,2-dimethoxycarbonyl-1,2,3,3a,8,8a-hexahydropyrrolo<2,3-b>indole 
• 139393-04-7 5-Cyano-L-tryptophan methyl ester 
• 544-92-3 copper(I) cyanide 
• 139393-00-3 (2S,3aR,8aR)-8-Acetyl-5-bromo-3,3a,8,8a-tetrahydro-2H-pyrrolo[2,3-b]indole-1,2-dicarboxylic acid dimethyl ester 

Relevant articles and documents

A Panel of TrpB Biocatalysts Derived from Tryptophan Synthase through the Transfer of Mutations that Mimic Allosteric Activation

Naturally occurring enzyme homologues often display highly divergent activity with non-natural substrates. Exploiting this diversity with enzymes engineered for new or altered function, however, is laborious because the engineering must be replicated for each homologue. A small set of mutations of the tryptophan synthase β-subunit (TrpB) from Pyrococcus furiosus, which mimics the activation afforded by binding of the α-subunit, was demonstrated to have a similar activating effect in different TrpB homologues with as little as 57 % sequence identity. Kinetic and spectroscopic analyses indicate that the mutations function through the same mechanism: mimicry of α-subunit binding. From these enzymes, we identified a new TrpB catalyst that displays a remarkably broad activity profile in the synthesis of 5-substituted tryptophans. This demonstrates that allosteric activation can be recapitulated throughout a protein family to explore natural sequence diversity for desirable biocatalytic transformations.

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.

Unlocking Reactivity of TrpB: A General Biocatalytic Platform for Synthesis of Tryptophan Analogues

Derivatives of the amino acid tryptophan (Trp) serve as precursors for the chemical and biological synthesis of complex molecules with a wide range of biological properties. Trp analogues are also valuable as building blocks for medicinal chemistry and as tools for chemical biology. While the enantioselective synthesis of Trp analogues is often lengthy and requires the use of protecting groups, enzymes have the potential to synthesize such products in fewer steps and with the pristine chemo- and stereoselectivity that is a hallmark of biocatalysis. The enzyme TrpB is especially attractive because it can form Trp analogues directly from serine (Ser) and the corresponding indole analogue. However, many potentially useful substrates, including bulky or electron-deficient indoles, are poorly accepted. We have applied directed evolution to TrpB from Pyrococcus furiosus and Thermotoga maritima to generate a suite of catalysts for the synthesis of previously intractable Trp analogues. For the most challenging substrates, such as nitroindoles, the key to improving activity lay in the mutation of a universally conserved and mechanistically important residue, E104. The new catalysts express at high levels (>200 mg/L of Escherichia coli culture) and can be purified by heat treatment; they can operate up to 75 °C (where solubility is enhanced) and can synthesize enantiopure Trp analogues substituted at the 4-, 5-, 6-, and 7-positions, using Ser and readily available indole analogues as starting materials. Spectroscopic analysis shows that many of the activating mutations suppress the decomposition of the active electrophilic intermediate, an amino-acrylate, which AIDS in unlocking the synthetic potential of TrpB.