6230-11-1

Basic information

• Product Name: 4-Methoxy-L-phenylalanine
• Synonyms: H-4-METHOXY-PHE-OH;H-TYR(ME)-OH;H-P-METHOXY-PHE-OH;H-PHE(4-OME)-OH;L-4-METHOXYPHE;L-TYROSINE-O-METHYL ETHER;4-METHOXY-L-PHENYLALANINE;4-METHOXYPHENYLALANINE
• CAS NO: 6230-11-1
• Molecular Formula: C₁₀H₁₃NO₃
• Molecular Weight: 195.22
• EINECS: 228-333-9
• Product Categories: Unusual Amino Acids;Amino Acids 13C, 2H, 15N;Amino Acids & Derivatives;Aromatics;Chiral Reagents
• Mol File: 6230-11-1.mol

Chemical Properties

• Melting Point: 259-261 °C (dec.)(lit.)
• Boiling Point: 331.88°C (rough estimate)
• Flash Point: 165.8 °C
• Appearance: /Solid
• Density: 1.1926 (rough estimate)
• Vapor Pressure: 1.62E-05mmHg at 25°C
• Refractive Index: 1.5150 (estimate)
• Storage Temp.: Store at RT.
• Solubility: Aqueous Acid (Slightly, Sonicated)
• PKA: 2.24±0.10(Predicted)
• Water Solubility: Very soluble in water.
• BRN: 2212726
• CAS DataBase Reference: 4-Methoxy-L-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 4-Methoxy-L-phenylalanine(6230-11-1)
• EPA Substance Registry System: 4-Methoxy-L-phenylalanine(6230-11-1)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 6230-11-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
4-Methoxy-L-phenylalanine is used as a fine chemical intermediate for the synthesis of various pharmaceutical compounds. Its unique structure may offer advantages in the development of new drugs, particularly those targeting specific receptors or enzymes.
Used in Chemical Synthesis:
As a non-natural amino acid derivative, 4-Methoxy-L-phenylalanine can be used as a building block in the synthesis of complex organic molecules. Its distinct chemical properties may facilitate the creation of novel compounds with specific functions or improved properties.
Used in Research and Development:
4-Methoxy-L-phenylalanine can serve as a valuable tool in research, particularly in the fields of biochemistry and molecular biology. It may be used to study the effects of amino acid modifications on protein structure and function, or to investigate the interactions between proteins and other biomolecules.
Used in Specialty Chemicals:
4-Methoxy-L-phenylalanine may also find applications in the production of specialty chemicals, such as those used in the fragrance, flavor, or cosmetic industries. Its unique structure could contribute to the development of new products with enhanced properties or novel sensory characteristics.

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

Upstream product

• 76757-95-4 N-formyl-O-methyl-L-tyrosine 
• 2746-25-0 p-Methoxybenzyl bromide 
• 108437-90-7 trans-(2S,5S)-N--2,5-bis(methoxymethoxymethyl)pyrrolidine 
• 60-18-4 L-tyrosine 
• 77-78-1 dimethyl sulfate 
• 74-88-4 methyl iodide 
• 86936-90-5 chryscandin 
• 207910-78-9 (Z)-2-hydroxy-3-(4-methoxyphenyl)acrylic acid 
• 123-11-5 4-methoxy-benzaldehyde 
• 71198-72-6 (4Z)-4-(4-methoxybenzylidene)-2-methyl-oxazolin-5-one 
• 215179-91-2 (S)-1-Acetyl-3-[1-(4-methoxy-phenyl)-meth-(Z)-ylidene]-6-methyl-piperazine-2,5-dione 
• 6318-42-9 5-(4-methoxy-benzyl)-hydantoin 
• 943-89-5 (E)-3-(4-methoxyphenyl)acrylic acid 
• 1334149-95-9 apratoxin S₅ 

Downstream Products

• 7479-01-8 O-methyl-L-tyrosine methyl ester hydrochloride 
• 52913-16-3 2-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-3-(4-methoxyphenyl)-propionic acid 
• 6318-42-9 (S)-5-(4-methoxy-benzyl)-imidazolidine-2,4-dione 
• 98778-85-9 3-iodo-4-O-methyl-L-tyrosine 
• 42429-13-0 (S)-2-bromo-3-(4-methoxy-phenyl)-propionic acid 
• 121428-55-5 (S)-4-methoxy-N-benzoyl-phenylalanine 
• 17554-34-6 (2S)-2-[(benzyloxycarbonyl)amino]-3-(4-methoxyphenyl)propanoic acid 
• 149470-55-3 (S)-3-(4-methoxyphenyl)-2-(4-methylphenylsulfonamido)propanoic acid 
• 94165-29-4 O-methyl-N-phenylacetyl-L-tyrosine 
• 17355-19-0 methyl (S)-2-amino-3-(4-methoxyphenyl)propionate 
• 1581-96-0 N-Trifluoracetyl-O-methyl-L-tyrosin 
• 978-68-7 N-Trifluoracetyl-L-alanyl-O-methyl-L-tyrosin 
• 53267-93-9 O-methyl-N-tert-butoxycarbonyl-L-tyrosine 
• 23007-98-9 3-Hydroxy-2-(4-methoxyphenyl)propionsaeure 

Relevant articles and documents

Biosynthesis of the anti-infective marformycins featuring pre-nrps assembly line N -formylation and O -methylation and post-assembly line C -hydroxylation chemistries

The biosynthetic gene cluster governing production of anti-infective marformycins was identified from deep sea-derived Streptomyces drozdowiczii SCSIO 10141. The putative mfn gene cluster (45 kb, 20 orfs) was found to encode six NRPSs and related proteins for cyclodepsipeptide core construction (mfnCDEFKL), a methionyl-tRNA formyltransferase (mfnA), a SAM-dependent methyltransferase (mfnG), and a cytochrome P450 monooxygenase for piperazic acid moiety hydroxylation (mfnN); notably, only MfnN uses an intact cyclodepsipeptide intermediate as its substrate.

C(sp3) -C(sp2) Method for constructing key and β - aryl amino acid preparation method

The invention provides C. (sp3) - C(sp2) A method for constructing a key and β -aryl amino acid relates to the technical field of chemical substance synthesis and transition metal application, which comprises β-C amino acid. (sp3) Ring carbon C in place of phenolic hydroxyl group(sp2) A method of constructing C-C keys by direct coupling. The process will contain inactive β-C. (sp3) Amino acids of - H and ligands L of specific structure1 The tetradentate chelate is generated by complexation with bivalent nickel, and the amino acid labile β-C is completed under the catalysis of palladium with phenolic ester under basic conditions. (sp3) - H Aryl, proton transfer and the like are reacted to achieve C. (sp3) - C(sp2) Construction of a bond, finally hydrolytically releasing β-C aryl amino acid and ligand L1 C. (sp3) - C(sp2) The key construction method is simple and convenient to operate. The method has the advantages of low cost, strong reaction universality, high yield and stereoselectivity. The synthetic method provides a novel method for preparing various non-natural β - aryl amino acids, and provides a novel method for amino acidification/peptide modification of phenolic compounds with biological activity, and provides a novel approach and selection for the design and synthesis of new drugs.

A novel phenylalanine ammonia-lyase from Pseudozyma antarctica for stereoselective biotransformations of unnatural amino acids

A novel phenylalanine ammonia-lyase of the psychrophilic yeast Pseudozyma antarctica (PzaPAL) was identified by screening microbial genomes against known PAL sequences. PzaPAL has a significantly different substrate binding pocket with an extended loop (26 aa long) connected to the aromatic ring binding region of the active site as compared to the known PALs from eukaryotes. The general properties of recombinant PzaPAL expressed in E. coli were characterized including kinetic features of this novel PAL with L-phenylalanine (S)-1a and further racemic substituted phenylalanines rac-1b-g,k. In most cases, PzaPAL revealed significantly higher turnover numbers than the PAL from Petroselinum crispum (PcPAL). Finally, the biocatalytic performance of PzaPAL and PcPAL was compared in the kinetic resolutions of racemic phenylalanine derivatives (rac-1a-s) by enzymatic ammonia elimination and also in the enantiotope selective ammonia addition reactions to cinnamic acid derivatives (2a-s). The enantiotope selectivity of PzaPAL with o-, m-, p-fluoro-, o-, p-chloro- and o-, m-bromo-substituted cinnamic acids proved to be higher than that of PcPAL.

EPHA4 CYCLIC PEPTIDE ANTAGONISTS AND METHODS OF USE THEREOF

Disclosed herein are compounds and methods of use thereof for the modulation of EphA4 receptor activity. In an aspect, is provided a method of treating or preventing a disease or disorder mediated by EphA4, comprising administering to a subject in need thereof a therapeutically effective amount of a compound as described herein, including certain embodiments, or the structural Formula (I), (l-A), (II), (III), (IV), (IV-1), (V), (Vl-A), (Vl-B), (VII-1), (VII-2), (VIII-1), or (VIII-2), or an enantiomer, a mixture of enantiomers, a mixture of two or more diastereomers, or an isotopic variant thereof; or a pharmaceutically acceptable salt, solvate, or hydrate thereof.

Chemoenzymatic synthesis of L-3,4-dimethoxyphenyl-alanine and its analogues using aspartate aminotransferase as a key catalyst

In this study, a chemoenzymatic synthesis method for the production of L-3,4-dimethoxyphenyl-alanine and its analogues from phenylpyruvate derivatives was developed. The aspartate aminotransferase from Escherichia coli was engineered by error prone PCR and the improved variants were identified. When 3, 4-dimethoxy phenylpyruvate was added by fed-batch on a preparative scale, L-3,4-dimethoxyphenyl-alanine was formed in 95.4% conversion and > 99% ee with the best aspartate aminotransferase variant as the catalyst. This study provided an efficient method for the production of methoxy substituted phenylalanines using the engineered aspartate aminotransferase.

Preparation method of O-methyl-threonine/tyrosine

The invention relates to a preparation method of O-methyl-threonine/tyrosine. The preparation method mainly overcomes the disadvantages of the existing method that a toxic reagent is volatile, the reagent is dangerous, the steps are long, the yield is low, and the like. The preparation method of the O-methyl-threonine/tyrosine comprises the following steps: N-t-butyloxycarboryl-threonine/tyrosineis catalyzed by sodium hydroxide and reacts with dimethyl sulfate to generate N-t-butyloxycarboryl-O-methyl-threonine/tyrosine, and then t-butyloxycarboryl is removed from the N-t-butyloxycarboryl-O-methyl-threonine/tyrosine through acid substances to obtain the product O-methyl-threonine/tyrosine. The product has important application in the fields of antibiotics and polypeptide drugs.

Tailored Mutants of Phenylalanine Ammonia-Lyase from Petroselinum crispum for the Synthesis of Bulky l- and d-Arylalanines

Tailored mutants of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) were created and tested in ammonia elimination from various sterically demanding, non-natural analogues of phenylalanine and in ammonia addition reactions into the corresponding (E)-arylacrylates. The wild-type PcPAL was inert or exhibited quite poor conversions in both reactions with all members of the substrate panel. Appropriate single mutations of residue F137 and the highly conserved residue I460 resulted in PcPAL variants that were active in ammonia elimination but still had a poor activity in ammonia addition onto bulky substrates. However, combined mutations that involve I460 besides the well-studied F137 led to mutants that exhibited activity in ammonia addition as well. The synergistic multiple mutations resulted in substantial substrate scope extension of PcPAL and opened up new biocatalytic routes for the synthesis of both enantiomers of valuable phenylalanine analogues, such as (4-methoxyphenyl)-, (napthalen-2-yl)-, ([1,1′-biphenyl]-4-yl)-, (4′-fluoro-[1,1′-biphenyl]-4-yl)-, and (5-phenylthiophene-2-yl)alanines.

Bio-inspired enantioselective full transamination using readily available cyclodextrin

The mimics of vitamin B6-dependent enzymes that catalyzed an enantioselective full transamination in the pure aqueous phase have been realized for the first time through the establishment of a new “pyridoxal 5′-phosphate (PLP) catalyzed non-covalent cyclodextrin (CD)-keto acid inclusion complexes” system, and various optically active amino acids have been obtained.

Kinetic Resolution of Aromatic β-Amino Acids Using a Combination of Phenylalanine Ammonia Lyase and Aminomutase Biocatalysts

An enzymatic strategy for the preparation of (R)-β-arylalanines employing phenylalanine aminomutase and ammonia lyase (PAM and PAL) enzymes has been demonstrated. Candidate PAMs with the desired (S)-selectivity from Streptomyces maritimus (EncP) and Bacillus sp. (PabH) were identified via sequence analysis using a well-studied template sequence. The newly discovered PabH could be linked to the first ever proposed biosynthesis of pyloricidin-like secondary metabolites and was shown to display better β-lyase activity in many cases. In spite of this, a method combining the higher conversion of EncP with a strict α-lyase from Anabaena variabilis (AvPAL) was found to be more amenable, allowing kinetic resolution of five racemic substrates and a preparative-scale reaction with >98% (R) enantiomeric excess. This work represents an improved and enantiocomplementary method to existing biocatalytic strategies, allowing simple product separation and modular telescopic combination with a preceding chemical step using an achiral aldehyde as starting material. (Figure presented.).

Novel chiral open-chain pyridoxamine catalyst and synthesis method and application thereof

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