154-06-3

Basic information

• Product Name: 5-Methyl-L-tryptophan
• Synonyms: 5-Methyl-L-tryptophan;(S)-5-Methyl-α-amino-1H-indole-3-propionic acid;(αS)-α-Amino-5-methyl-1H-indole-3-propionic acid;(2S)-2-amino-3-(5-methyl-1H-indol-3-yl)propionic acid;(2S)-2-azanyl-3-(5-methyl-1H-indol-3-yl)propanoic acid;L-5-Methyltryptophan;L-Tryptophan, 5-Methyl-;(S)-2-Amino-3-(5-methyl-1H-indol-3-yl)propanoic acid
• CAS NO: 154-06-3
• Molecular Formula: C₁₂H₁₄N₂O₂
• Molecular Weight: 218.25176
• EINECS: 213-453-6
• Mol File: 154-06-3.mol
• Article Data: 11

Chemical Properties

• Boiling Point: 358.94°C (rough estimate)
• Flash Point: 229.1°C
• Appearance: /
• Density: 1.313
• Vapor Pressure: 4.48E-09mmHg at 25°C
• Refractive Index: 1.6660 (estimate)
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: 5-Methyl-L-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 5-Methyl-L-tryptophan(154-06-3)
• EPA Substance Registry System: 5-Methyl-L-tryptophan(154-06-3)

Safety Data

• Hazardous Substances Data: 154-06-3(Hazardous Substances Data)

Usage

General Description

5-Methyl-L-tryptophan is a naturally occurring amino acid that is structurally similar to the essential amino acid tryptophan. It is a derivative of tryptophan and is produced through a specific enzymatic reaction in the body and can also be obtained through dietary sources. This chemical has been studied for its potential therapeutic applications, particularly in the treatment of certain types of cancer. 5-Methyl-L-tryptophan has been shown to inhibit the activity of indoleamine 2,3-dioxygenase (IDO), an enzyme involved in immune suppression, and has demonstrated anti-tumor properties in preclinical studies. Research into the potential health benefits and applications of this chemical is ongoing, with a focus on its ability to modulate the immune response and inhibit tumor growth.

InChI:InChI=1/C12H14N2O2/c1-7-2-3-11-9(4-7)8(6-14-11)5-10(13)12(15)16/h2-4,6,10,14H,5,13H2,1H3,(H,15,16)/t10-/m0/s1

Upstream product

• 312-84-5 D-Serine 
• 614-96-0 5-methyl-1H-indole 
• 71953-90-7 2-acetamido-3-(5-methyl-1H-indol-3-yl)propanoic acid 
• 56-45-1 L-serin 
• 951-55-3 5-methyl-DL-tryptophan 
• 355839-53-1 (2R,5S)-3,6-diethoxy-2-isopropyl-5-[5-methyl-2-(trimethylsilyl)-3-indolyl]methyl-2,5-dihydropyrazine 
• 220906-01-4 (2R,5S)-3,6-diethoxy-2-isopropyl-5-[3-(trimethylsilyl)prop-2-ynyl]2,5-diydropyrazine 
• 29289-13-2 2-iodo-4-methylaniline 
• 355839-74-6 5-methyl-L-tryptophan ethyl ester 
• 74761-41-4 (S)-1-(methoxycarbonyl)pyrrolidine-2-carboxylic acid 
• 1148-11-4 N-Benzyloxycarbonyl-L-proline 
• 147-85-3 L-proline 
• 93299-30-0 N-methoxycarbonyl-L-glutamine methyl ester 
• 93271-96-6 (2S,5RS)-1,2-dimethyl-5-hydroxypyrrolidine-1,2-dicarboxylate 

Downstream Products

• 1401863-33-9 N-(2-aminoethyl)-6-methyl-1-(4-methoxyphenyl )-9H-pyrido[3,4-b]indole-3-carboxamide hydrochloride 
• 1401863-37-3 C₂₂H₂₂N₄O₂ 
• 952200-85-0 C₂₁H₁₈N₂O₃ 
• 114873-09-5 N-(tert-butoxycarbonyl)-DL-5-methyltryptophan 

Relevant articles and documents

Biocatalysts from cyanobacterial hapalindole pathway afford antivirulent isonitriles against MRSA

Abstract: The emergence of resistance to frontline antibiotics has called for novel strategies to combat serious pathogenic infections. Methicillin-resistant Staphylococcus aureus [MRSA] is one such pathogen. As opposed to traditional antibiotics, bacteriostatic anti-virulent agents disarm MRSA, without exerting pressure, that cause resistance. Herein, we employed a thermophilic Thermotoga maritima tryptophan synthase (TmTrpB1) enzyme followed by an isonitrile synthase and Fe(II)-α-ketoglutarate-dependent oxygenase, in sequence as biocatalysts to produce antivirulent indole vinyl isonitriles. We report on conversion of simple derivatives of indoles to their C3-vinyl isonitriles, as the enzymes employed here demonstrated broader substrate tolerance. In toto, eight distinct L-Tryptophan derived α-amino acids (7) were converted to their bioactive vinyl isonitriles (3) by action of an isonitrile synthase (WelI1) and an Fe(II)-α-ketoglutarate-dependent oxygenase (WelI3) yielding structural variants possessing antivirulence against MRSA. These indole vinyl isonitriles at 10 μg/mL are effective as antivirulent compounds against MRSA, as evidenced through analysis of rabbit blood hemolysis assay. Based on a homology modelling exercise, of enzyme-substrate complexes, we deduced potential three dimensional alignments of active sites and glean mechanistic insights into the substrate tolerance of the Fe(II)-α-ketoglutarate-dependent oxygenase. Graphic abstract: [Figure not available: see fulltext.]

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.

Chiral ligand-exchange resolution of underivatized amino acids on a dynamically modified stationary phase for RP-HPTLC

The synthesis of Spi(τ-dec), derived from the selective alkylation of L-spinacine (4,5,6,7-tetrahydro-1H-imidazo[4,5-c]pyridine-6-carboxylic acid) at the τ-nitrogen of its heteroaromatic ring, with a linear hydrocarbon chain of 10 carbon atoms, is described here for the first time. Spi(τ-dec) was successfully employed in the past to prepare home-made chiral columns for chiral ligand-exchange high-performance liquid chromatography. In the present article a new method is described, using Spi(τ-dec) as a chiral selector in high-performance thin-layer chromatography (HPTLC): commercial hydrophobic plates were first coated with Spi(τ-dec) and then treated with copper sulfate. The performance of this new chiral stationary phase was tested against racemic mixtures of aromatic amino acids, after appropriate optimization of both the conditions of preparation of the plates and the mobile phase composition. The enantioselectivity values obtained for the studied compounds were higher than those reported in the literature for similar systems. The method employed here for the preparation of chiral HPTLC plates proved practical, efficient, and inexpensive. Chirality 26:313-318, 2014. 2014 Wiley Periodicals, Inc.