39878-65-4

Basic information

• Product Name: O-METHYL-D-TYROSINE
• Synonyms: (R)-2-AMINO-3-(4-METHOXY-PHENYL)-PROPIONIC ACID;O-METHYL-D-TYROSINE;H-P-METHOXY-D-PHE-OH;H-4-METHOXY-D-PHE-OH;H-D-PHE(4-OME)-OH;H-D-TYR(ME)-OH;D-TYROSINE(ME)-OH;D-4-METHOXYPHE
• CAS NO: 39878-65-4
• Molecular Formula: C₁₀H₁₃NO₃
• Molecular Weight: 195.22
• EINECS: 228-333-9
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Unusual Amino Acids;Amino Acids;I - Z;Modified Amino Acids
• Mol File: 39878-65-4.mol
• Article Data: 14

Chemical Properties

• Melting Point: 262-263 °C (decomp)
• Boiling Point: 350.6 °C at 760 mmHg
• Flash Point: 165.8 °C
• Appearance: /Solid
• Density: 1.209 g/cm³
• Vapor Pressure: 1.62E-05mmHg at 25°C
• Refractive Index: 1.559
• Storage Temp.: Store at RT.
• PKA: 2.24±0.10(Predicted)
• CAS DataBase Reference: O-METHYL-D-TYROSINE(CAS DataBase Reference)
• NIST Chemistry Reference: O-METHYL-D-TYROSINE(39878-65-4)
• EPA Substance Registry System: O-METHYL-D-TYROSINE(39878-65-4)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 39878-65-4(Hazardous Substances Data)

Usage

Chemical Properties

White powder

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)/t9-/m1/s1

Upstream product

• 42429-13-0 (S)-2-bromo-3-(4-methoxy-phenyl)-propionic acid 
• 742100-87-4 N-chloroacetyl-D-tyrosine 
• 77-78-1 dimethyl sulfate 
• 2746-25-0 p-Methoxybenzyl bromide 
• 108437-90-7 trans-(2S,5S)-N--2,5-bis(methoxymethoxymethyl)pyrrolidine 
• 556-02-5 tyrosine 
• 161633-99-4 (R)-3-(4-Methoxy-phenyl)-2-((4S,5R)-2-oxo-4,5-diphenyl-oxazolidin-3-yl)-propionic acid benzyl ester 
• 70601-62-6 (D)-N-acetyl-4-methoxy-phenylalanine 
• 5703-26-4 4-Methoxyphenylacetaldehyde 
• 248937-25-9 (R,S)-2-[(2-hydroxy-1-phenylethyl)amino]-2-(4-methoxyphenyl)propanenitrile 
• 6230-11-1 O-Methyltyrosine 
• 7635-29-2 O-methyl tyrosine 
• 6318-42-9 5-(4-methoxy-benzyl)-hydantoin 
• 53796-61-5 N-acetyl-O-methyl-tyrosine 

Downstream Products

• 144754-19-8 (R)-4-methoxy-N-benzoyl-phenylalanine 
• 17355-19-0 methyl (R)-2-amino-3-(4-methoxyphenyl)propanoate 
• 1253909-38-4 (R)-2-amino-3-(4-methoxy-phenyl)-propan-1-ol 
• 70601-64-8 (R)-4-methoxyphenylalanine methyl ester hydrochloride 
• 77128-72-4 N-(9-Fluorenylmethyloxy)carbonyl-O-methyl-L-tyrosine 

Relevant articles and documents

Cyclic Tetrapeptides with Synergistic Antifungal Activity from the Fungus Aspergillus westerdijkiae Using LC-MS/MS-Based Molecular Networking

Fungal natural products play a prominent role in the development of pharmaceuticalagents. Two new cyclic tetrapeptides (CTPs), westertide A (1) and B (2), with eight known compounds (3-10) were isolated from the fungus Aspergillus westerdijkiae guided by

Deracemization and stereoinversion to aromatic d-amino acid derivatives with ancestral l-amino acid oxidase

Enantiomerically pure amino acid derivatives could be foundational compounds for peptide drugs. Deracemization of racemates to l-amino acid derivatives can be achieved through the reaction of evolved d-amino acid oxidase and chemical reductants, whereas deracemization to d-amino acid derivatives has not progressed due to the difficulty associated with the heterologous expression of l-amino acid oxidase (LAAO). In this study, we succeeded in developing an ancestral LAAO (AncLAAO) bearing broad substrate selectivity (13 l-amino acids) and high productivity through an Escherichia coli expression system (50.7 mg/L). AncLAAO can be applied to perform deracemization to d-amino acids in a similar way to deracemization to l-amino acids. In fact, full conversion (>99% ee, d-form) could be achieved for 16 racemates, including nine d,l-Phe derivatives, six d,l-Trp derivatives, and a d,l-phenylglycine. Taken together, we believe that AncLAAO could be a key enzyme to obtain optically pure d-amino acid derivatives in the future.

Engineered Aminotransferase for the Production of d-Phenylalanine Derivatives Using Biocatalytic Cascades

d-Phenylalanine derivatives are valuable chiral building blocks for a wide range of pharmaceuticals. Here, we developed stereoinversion and deracemization biocatalytic cascades to synthesize d-phenylalanine derivatives that contain electron-donating or -withdrawing substituents of various sizes and at different positions on the phenyl ring with a high enantiomeric excess (90 to >99 % ee) from commercially available racemic mixtures or l-amino acids. These whole-cell systems couple Proteus mirabilis l-amino acid deaminase with an engineered aminotransferase that displays native-like activity towards d-phenylalanine, which we generated from Bacillus sp. YM-1 d-amino acid aminotransferase. Our cascades are applicable to preparative-scale synthesis and do not require cofactor-regeneration systems or chemical reducing agents.