35296-56-1

Basic information

• Product Name: L-Tyrosine, 3-hydroxy-O-Methyl-
• Synonyms: L-Tyrosine, 3-hydroxy-O-Methyl-;3-Hydroxy-O-methyl-L-tyrosine;(2S)-2-AMINO-3-(3-HYDROXY-4-METHOXYPHENYL)PROPANOIC ACID
• CAS NO: 35296-56-1
• Molecular Formula: C₁₀H₁₃NO₄
• Molecular Weight: 211.21452
• Mol File: 35296-56-1.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 409.7±45.0 °C(Predicted)
• Appearance: /
• Density: 1.321±0.06 g/cm3(Predicted)
• PKA: 2.23±0.20(Predicted)
• CAS DataBase Reference: L-Tyrosine, 3-hydroxy-O-Methyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Tyrosine, 3-hydroxy-O-Methyl-(35296-56-1)
• EPA Substance Registry System: L-Tyrosine, 3-hydroxy-O-Methyl-(35296-56-1)

Safety Data

• Hazardous Substances Data: 35296-56-1(Hazardous Substances Data)

Usage

Uses

3-Hydroxy-O-methyl-L-tyrosine is used in the preparation of tyrosine-based components of natural products such as saframycin MX1 and its analogs, which are naturally potent anti-tumor agents currently under clinical development.

Upstream product

• 59-92-7 levodopa 
• 14031-35-7 S-Adenosyl-L-methionine 
• 133641-14-2 N-(tert-butyloxycarbonyl)-3-(3-formyl-4-methoxyphenyl)-L-alanine 
• 574735-09-4 2-tert-butoxycarbonylamino-3-(3-formyl-4-methoxy-phenyl)-propionic acid methyl ester 

Relevant articles and documents

Targeted Rediscovery and Biosynthesis of the Farnesyl-Transferase Inhibitor Pepticinnamin E

The natural product pepticinnamin E potently inhibits protein farnesyl transferases and has potential applications in treating cancer and malaria. Pepticinnamin E contains a rare N-terminal cinnamoyl moiety as well as several nonproteinogenic amino acids, including the unusual 2-chloro-3-hydroxy-4-methoxy-N-methyl-L-phenylalanine. The biosynthesis of pepticinnamin E has remained uncharacterized because its original producing strain is no longer available. Here we identified a gene cluster (pcm) for this natural product in a new producer, Actinobacteria bacterium OK006, by means of a targeted rediscovery strategy. We demonstrated that the pcm cluster is responsible for the biosynthesis of pepticinnamin E, a nonribosomal peptide/polyketide hybrid. We also characterized a key O-methyltransferase that modifies 3,4-dihydroxy-l-phenylalanine. Our work has identified the gene cluster for pepticinnamins for the first time and sets the stage for elucidating the unique chemistry required for biosynthesis.

Formation of 3-hydroxy-4-methoxyphenylalanine from 3,4-dihydroxyphenylalanine by rat liver homogenate

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