114926-39-5

Basic information

• Product Name: 3-Methylphenyl-D-alanine
• Synonyms: RARECHEM BK PT 0064;(R)-2-AMINO-3-M-TOLYL-PROPIONIC ACID;3-METHYL-D-PHENYLALANINE;D-3-METHYLPHE;D-3-METHYLPHENYLALANINE;H-M-ME-D-PHE-OH;H-D-PHE(3-ME)-OH;3-Methy-D-Phenylalanine
• CAS NO: 114926-39-5
• Molecular Formula: C₁₀H₁₃NO₂
• Molecular Weight: 179.22
• EINECS: 145-896-5
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Amino Acid Derivatives;a-amino
• Mol File: 114926-39-5.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 322.8 °C at 760 mmHg
• Flash Point: 149 °C
• Appearance: /
• Density: 1.165 g/cm³
• Vapor Pressure: 8.9E-05mmHg at 25°C
• Refractive Index: 1.568
• Storage Temp.: Store at -15°C
• PKA: 2.22±0.10(Predicted)
• CAS DataBase Reference: 3-Methylphenyl-D-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: 3-Methylphenyl-D-alanine(114926-39-5)
• EPA Substance Registry System: 3-Methylphenyl-D-alanine(114926-39-5)

Safety Data

• Hazard Codes: Xi
• Hazardous Substances Data: 114926-39-5(Hazardous Substances Data)

Usage

Description

3-Methylphenyl-D-alanine, a derivative of D-Phenylalanine, is an organic compound with the molecular formula C10H13NO2. It plays a significant role in the synthesis of various bioactive molecules and has potential applications in the pharmaceutical industry due to its unique structural properties.

Uses

Used in Pharmaceutical Industry:
3-Methylphenyl-D-alanine is used as a reagent for the synthesis of aminophenylpropanyl phosphate derivatives, which exhibit pin1 inhibitory activity. This application is crucial in the development of novel therapeutic agents targeting specific enzymes or proteins involved in various diseases.
Used in Biochemical Research:
In the preparation of N-arylaminonitriles, 3-Methylphenyl-D-alanine serves as a key component. These N-arylaminonitriles are valuable as bioavailable peptidomimetic inhibitors of cathepsin B, a protease enzyme implicated in several pathological conditions. By inhibiting cathepsin B, these peptidomimetics can potentially be used in the treatment of such conditions.

InChI:InChI=1/C10H13NO2/c1-7-4-2-3-5-8(7)6-9(11)10(12)13/h2-5,9H,6,11H2,1H3,(H,12,13)/t9-/m1/s1

Upstream product

• 5472-70-8 3-methyl-phenylalanine 
• 3029-79-6 (E)-3-methylcinnamic acid 
• 2283-42-3 (S)-2-amino-3-(3-methylphenyl)propionic acid 
• 61676-25-3 2-oxo-3-m-tolyl-propionic acid 
• 620-13-3 1-bromomethyl-3-methyl-benzene 
• 145243-34-1 2-(Benzhydrylidene-amino)-3-m-tolyl-propionic acid methyl ester 

Downstream Products

• 1227832-59-8 C₂₁H₁₉NO₃ 
• 774243-64-0 C₁₀H₁₅NO 
• 374119-30-9 (S)-6-[1-carboxy-2-(3-methylphenyl)-ethylamino]-phthalide 
• 374119-37-6 (S)-2-(3-methoxycarbonylphenylamino)-3-(3-methylphenyl)-propionic acid 
• 374119-33-2 (R)-2-hydroxy-3-(3-methylphenyl)-propionic acid 

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.

Preparation of (R)-Phenylalanine Analogues by Enantioselective Destruction Using L-Amino Acid Oxidase

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