2370-57-2

Basic information

• Product Name: methyl-3-tyrosine
• Synonyms: methyl-3-tyrosine
• CAS NO: 2370-57-2
• Molecular Formula: C₁₀H₁₃NO₃
• Molecular Weight: 195.22
• Mol File: 2370-57-2.mol

Chemical Properties

• Boiling Point: 386.5°Cat760mmHg
• Flash Point: 187.5°C
• Appearance: /
• Density: 1.283g/cm³
• Vapor Pressure: 1.15E-06mmHg at 25°C
• Refractive Index: 1.602
• CAS DataBase Reference: methyl-3-tyrosine(CAS DataBase Reference)
• NIST Chemistry Reference: methyl-3-tyrosine(2370-57-2)
• EPA Substance Registry System: methyl-3-tyrosine(2370-57-2)

Safety Data

• Hazardous Substances Data: 2370-57-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Applications:
Methyl-3-tyrosine is used as an intermediate in the synthesis of pharmaceutical compounds. The presence of the methyl group at position 3 on the phenyl ring can influence the reactivity and selectivity of the molecule, making it a valuable building block for the development of new drugs.
Used in Research and Development:
Methyl-3-tyrosine can be utilized as a research tool in the study of tyrosine metabolism and its role in various biological processes. It may also be used to investigate the effects of tyrosine derivatives on enzyme activity and protein function.
Used in Chemical Synthesis:
Methyl-3-tyrosine can be employed as a starting material or a reagent in the chemical synthesis of various organic compounds, including specialty chemicals, dyes, and other fine chemicals.
Used in Analytical Chemistry:
Methyl-3-tyrosine may be used as a reference compound or a standard in analytical chemistry for the development and validation of analytical methods, such as high-performance liquid chromatography (HPLC), mass spectrometry (MS), and other techniques for the analysis of tyrosine and its derivatives.
Used in Nutritional Supplements:
Methyl-3-tyrosine could potentially be used as an ingredient in nutritional supplements, particularly those aimed at supporting cognitive function or athletic performance. However, further research would be required to establish its safety and efficacy in this context.

InChI:InChI=1/C10H13NO3/c1-6-4-7(2-3-9(6)12)5-8(11)10(13)14/h2-4,8,12H,5,11H2,1H3,(H,13,14)/t8-/m0/s1

Upstream product

• 91715-65-0 <4-Hydroxy-3-methyl-phenyl>-brenztraubensaeure 
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• 93902-19-3 ethyl-α-acetamido-α-(3-methyl-4-methoxybenzyl)malonate 

Downstream Products

• 92502-13-1 3-Methyl-N-acetyl-DL-tyrosin-aethylester 
• 90888-36-1 5-Iod-3-methyl-DL-tyrosin 

Relevant articles and documents

Biocascade Synthesis of L-Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol-Lyase and L-Lactate Oxidase

A one-pot biocascade of two enzymatic steps catalyzed by an l-lactate oxidase and a tyrosine phenol-lyase has been successfully developed in the present study. The reaction provides an efficient method for the synthesis of l-tyrosine derivatives, which exhibits readily available starting materials and excellent yields. In the first step, an in situ generation of pyruvate from readily available bio-based l-lactate catalyzed by a highly active l-lactate oxidase from Aerococcus viridans (AvLOX) was developed (using oxygen as oxidant and catalase as hydrogen peroxide removing reagent). Pyruvate thus produced underwent C–C coupling with phenol derivatives as acceptor substrate using specially designed thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii (TTPL). Overall, this cascade avoids the high cost and easy decomposition of pyruvate and offered an efficient and environmentally friendly procedure for l-tyrosine derivatives synthesis.

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.