33468-33-6

Basic information

• Product Name: (S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID
• Synonyms: 4-METHYL-L-TRYPTOPHAN;L-Tryptophan, 4-methyl-;L-4-METHYLTRYPTOPHAN;(S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID
• CAS NO: 33468-33-6
• Molecular Formula: C12H14N2O2
• Molecular Weight: 218.25
• Mol File: 33468-33-6.mol
• Article Data: 7

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID(33468-33-6)
• EPA Substance Registry System: (S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID(33468-33-6)

Safety Data

• Hazardous Substances Data: 33468-33-6(Hazardous Substances Data)

Usage

General Description

(S)-2-amino-3-(4-methyl-1H-indol-3-yl)-propionic acid is a chemical compound with the molecular formula C13H15N2O2. It is an amino acid derivative with a unique structure that includes an indole ring. (S)-2-AMINO-3-(4-METHYL-1H-INDOL-3-YL)-PROPIONIC ACID is commonly referred to as "methyltryptophan" and is often used in the study of serotonin signaling and metabolism in various biological systems. Methyltryptophan has been shown to have potential as a therapeutic agent for neurological disorders and cancer due to its ability to influence serotonin levels and inhibit tryptophan metabolism. Additionally, it has been implicated in the regulation of immune responses and inflammation.

Upstream product

• 1954-45-6 2-amino-3-(4-methyl-1H-indol-3-yl)propionic acid 
• 16096-32-5 4-methyl-1H-indole 
• 56-45-1 L-serin 
• 302-84-1 serin 
• 164119-68-0 acetylamino-(4-methyl-indol-3-ylmethyl)-malonic acid diethyl ester 
• 6639-59-4 N-(2,3-dimethylphenyl)formamide 
• 164119-81-7 N,N-dimethyl-1-(4-methyl-1H-indol-3-yl)methanamine 

Downstream Products

• 33468-33-6 (R)-2-amino-3-(4-methyl-1H-indol-3-yl)propanoic acid 

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.

De novo Biosynthesis of “Non-Natural” Thaxtomin Phytotoxins

Thaxtomins are diketopiperazine phytotoxins produced by Streptomyces scabies and other actinobacterial plant pathogens that inhibit cellulose biosynthesis in plants. Due to their potent bioactivity and novel mode of action there has been considerable interest in developing thaxtomins as herbicides for crop protection. To address the need for more stable derivatives, we have developed a new approach for structural diversification of thaxtomins. Genes encoding the thaxtomin NRPS from S. scabies, along with genes encoding a promiscuous tryptophan synthase (TrpS) from Salmonella typhimurium, were assembled in a heterologous host Streptomyces albus. Upon feeding indole derivatives to the engineered S. albus strain, tryptophan intermediates with alternative substituents are biosynthesized and incorporated by the NRPS to deliver a series of thaxtomins with different functionalities in place of the nitro group. The approach described herein, demonstrates how genes from different pathways and different bacterial origins can be combined in a heterologous host to create a de novo biosynthetic pathway to “non-natural” product target compounds.