17028-03-4

Basic information

• Product Name: 3-METHYL-L-TYROSINE
• Synonyms: 3-METHYL-L-TYROSINE;(S)-2-AMino-3-(4-hydroxy-3-Methylphenyl)propanoic Acid
• CAS NO: 17028-03-4
• Molecular Formula: C₁₀H₁₃NO₃
• Molecular Weight: 195.21512
• Product Categories: Amino Acids & Derivatives;Aromatics;Chiral Reagents;Intermediates & Fine Chemicals;Pharmaceuticals
• Mol File: 17028-03-4.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 386.5±42.0 °C(Predicted)
• Appearance: /
• Density: 1.283±0.06 g/cm3(Predicted)
• PKA: 2.26±0.20(Predicted)
• CAS DataBase Reference: 3-METHYL-L-TYROSINE(CAS DataBase Reference)
• NIST Chemistry Reference: 3-METHYL-L-TYROSINE(17028-03-4)
• EPA Substance Registry System: 3-METHYL-L-TYROSINE(17028-03-4)

Safety Data

• Hazardous Substances Data: 17028-03-4(Hazardous Substances Data)

Usage

Description

3-METHYL-L-TYROSINE is a naturally occurring non-proteinogenic amino acid that is structurally similar to L-tyrosine, with the addition of a methyl group at the third carbon position. This modification results in distinct properties and potential applications in various fields, making it a valuable compound for research and development.

Uses

Used in Pharmaceutical Research:
3-METHYL-L-TYROSINE is used as a tyrosine analogue as an alternative substrate for protein tyrosine kinase Csk. This application provides valuable insights into substrate selectivity and the catalytic mechanism of the enzyme, which can contribute to the development of targeted therapies and a better understanding of kinase function in various biological processes.
Used in Biochemical Studies:
3-METHYL-L-TYROSINE can be utilized in biochemical studies to investigate the specificity and activity of enzymes that act on tyrosine residues. By comparing the behavior of this analogue with that of the natural amino acid, researchers can gain a deeper understanding of enzyme-substrate interactions and the factors that influence these processes.
Used in Drug Development:
As a structural analogue of L-tyrosine, 3-METHYL-L-TYROSINE may have potential applications in the development of new drugs targeting enzymes or pathways that involve tyrosine. Its unique properties could be leveraged to design molecules with improved selectivity, potency, or other desirable characteristics, ultimately leading to more effective treatments for various diseases and conditions.

Upstream product

• 127-17-3 2-oxo-propionic acid 
• 95-48-7 ortho-cresol 
• 1991-87-3 4-methyl-L-phenylalanine 
• 699536-27-1 N-(tert-butyloxycarbonyl)-3-(4-hydroxy-3-methylphenyl)-L-alanine ethyl ester 
• 113-24-6 sodium pyruvate 
• 108-88-3 toluene 
• 57-60-3 piruvate 

Downstream Products

• 142057-17-8 3-Methyltyramine 
• 582320-57-8 3-(3,4-dihydroxy-5-methylphenyl)-L-alanine 
• 91715-65-0 <4-Hydroxy-3-methyl-phenyl>-brenztraubensaeure 
• 2370-57-2 m-methyl-DL-tyrosine 

Relevant articles and documents

Cutting long syntheses short: Access to non-natural tyrosine derivatives employing an engineered tyrosine phenol lyase

The chemical synthesis of 3-substituted tyrosine derivatives requires a minimum of four steps to access optically enriched material starting from commercial precursors. Attempting to short-cut the cumbersome chemical synthesis of 3-substituted tyrosine derivatives, a single step biocatalytic approach was identified employing the tyrosine phenol lyase from Citrobacter freundii. The enzyme catalyses the hydrolysis of tyrosine to phenol, pyruvate and ammonium as well as the reverse reaction, thus the formation of tyrosine from phenol, pyruvate and ammonium. Since the wild-type enzyme possessed a very narrow substrate spectrum, structure-guided, site-directed mutagenesis was required to change the substrate specificity of this C-C bond forming enzyme. The best variant M379V transformed, for example, o-cresol, o-methoxyphenol and o-chlorophenol efficiently to the corresponding tyrosine derivatives without any detectable side-product. In contrast, all three phenol compounds were non-substrates for the wild-type enzyme. Employing the mutant, various Ltyrosine derivatives (3-Me, 3-OMe, 3-F, 3-Cl) were obtained with complete conversion and excellent enantiomeric excess (>97%) in just a single 'green' step starting from pyruvate and commercially available phenol derivatives.

Multienzyme One-Pot Cascade for the Stereoselective Hydroxyethyl Functionalization of Substituted Phenols

The operability and substrate scope of a redesigned vinylphenol hydratase as a single biocatalyst or as part of multienzyme cascades using either substituted coumaric acids or phenols as stable, cheap, and readily available substrates are reported.

Vinylation of Unprotected Phenols Using a Biocatalytic System

Readily available substituted phenols were coupled with pyruvate in buffer solution under atmospheric conditions to afford the corresponding para-vinylphenol derivatives while releasing only one molecule of CO2 and water as the by-products. This transformation was achieved by designing a biocatalytic system that combines three biocatalytic steps, namely the C-C coupling of phenol and pyruvate in the presence of ammonia, which leads to the corresponding tyrosine derivative, followed by deamination and decarboxylation. The biocatalytic transformation proceeded with high regioselectivity and afforded exclusively the desired para products. This method thus represents an environmentally friendly approach for the direct vinylation of readily available 2-, 3-, or 2,3-disubstituted phenols on preparative scale (0.5 mmol) that provides vinylphenols in high yields (65-83%).