1991-86-2

Basic information

• Product Name: α-Methyl-D-tyrosine
• Synonyms: α-Methyl-D-tyrosine;D-2-Me-Tyr-OH
• CAS NO: 1991-86-2
• Molecular Weight: 0
• Mol File: 1991-86-2.mol
• Article Data: 14

Chemical Properties

• Appearance: /
• CAS DataBase Reference: α-Methyl-D-tyrosine(CAS DataBase Reference)
• NIST Chemistry Reference: α-Methyl-D-tyrosine(1991-86-2)
• EPA Substance Registry System: α-Methyl-D-tyrosine(1991-86-2)

Safety Data

• Hazardous Substances Data: 1991-86-2(Hazardous Substances Data)

Usage

Description

α-Methyl-D-tyrosine is a non-natural, optically active amino acid derivative derived from the naturally occurring amino acid tyrosine. It is characterized by the presence of a methyl group at the alpha position and exhibits a D-configuration, making it a valuable compound in various applications due to its unique structural properties.

Uses

Used in Pharmaceutical Industry:
α-Methyl-D-tyrosine is used as an intermediate in the synthesis of various pharmaceutical compounds, particularly those with enantioselective properties. Its unique structure allows for the development of drugs with targeted effects, reducing potential side effects and improving overall efficacy.
Used in Enantioselective Hydrolysis:
α-Methyl-D-tyrosine is used as a chiral auxiliary in enantioselective hydrolysis of amino acids. This application is crucial in the production of enantiomerically pure compounds, which are essential in the pharmaceutical, agrochemical, and fragrance industries. The use of α-Methyl-D-tyrosine in this process helps to achieve high levels of enantioselectivity, leading to more efficient and effective synthesis of desired enantiomers.
Used in Research and Development:
α-Methyl-D-tyrosine is also utilized in research and development for the study of enzyme specificity, protein structure, and function. Its unique properties make it a valuable tool in understanding the mechanisms of various biological processes and can contribute to the development of new therapeutic strategies and drug candidates.

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Relevant articles and documents

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.

One-Pot Enzymatic Synthesis of d-Arylalanines Using Phenylalanine Ammonia Lyase and l-Amino Acid Deaminase

The phenylalanine ammonia-lyase (AvPAL) from Anabaena variabilis catalyzes the amination of substituent trans-cinnamic acid (t-CA) to produce racemic d,l-enantiomer arylalanine mixture owing to its low stereoselectivity. To produce high optically pure d-arylalanine, a modified AvPAL with high d-selectivity is expected. Based on the analyses of catalytic mechanism and structure, the Asn347 residue in the active site was proposed to control stereoselectivity. Therefore, Asn347 was mutated to construct mutant AvPAL-N347A, the stereoselectivity of AvPAL-N347A for d-enantiomer arylalanine was 2.3-fold higher than that of wild-type AvPAL (WtPAL). Furthermore, the residual l-enantiomer product in reaction solution could be converted into the d-enantiomer product through stereoselective oxidation by PmLAAD and nonselective reduction by reducing agent NH3BH3. At optimal conditions, the conversion rate of t-CA and optical purity (enantiomeric excess (eeD)) of d-phenylalanine reached 82% and exceeded 99%, respectively. The two enzymes displayed activity toward a broad range of substrate and could be used to efficiently synthesize d-arylalanine with different groups on the phenyl ring. Among these d-arylalanines, the yield of m-nitro-d-phenylalanine was highest and reached 96%, and the eeD exceeded 99%. This one-pot synthesis using AvPAL and PmLAAD has prospects for industrial application.

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.