49759-61-7

Basic information

• Product Name: 4-Methyl-D-phenylalanine
• Synonyms: (R)-2-AMINO-3-P-TOLYL-PROPIONIC ACID;RARECHEM BK PT 0070;D-4-METHYLPHE;D-4-METHYLPHENYLALANINE;H-P-ME-D-PHENYLALANINE;H-P-ME-D-PHE-OH;H-D-PHE(P-ME)-OH;H-D-PHE(4-ME)-OH
• CAS NO: 49759-61-7
• Molecular Formula: C₁₀H₁₃NO₂
• Molecular Weight: 179.22
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Phenylalanine [Phe, F];Unusual Amino Acids;Amino acids methyl、ethyl、t-butyl series;a-amino
• Mol File: 49759-61-7.mol

Chemical Properties

• Boiling Point: 323.5 °C at 760 mmHg
• Flash Point: 149.5 °C
• Appearance: /
• Density: 1.165 g/cm³
• Storage Temp.: Store at RT.
• CAS DataBase Reference: 4-Methyl-D-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 4-Methyl-D-phenylalanine(49759-61-7)
• EPA Substance Registry System: 4-Methyl-D-phenylalanine(49759-61-7)

Safety Data

• Hazard Codes: Xi
• Hazardous Substances Data: 49759-61-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
4-Methyl-D-phenylalanine is used as a reagent for the synthesis of aminophenylpropanyl phosphate derivatives, which can exhibit pin1 inhibitory activity. This application is particularly relevant in the development of new drugs targeting specific enzymes or proteins involved in various diseases.
Used in Chemical Synthesis:
In the chemical industry, 4-Methyl-D-phenylalanine can be utilized as a building block for the creation of complex organic molecules. Its unique structure allows for the development of novel compounds with potential applications in various fields, such as materials science, agrochemistry, and pharmaceuticals.

Upstream product

• 49759-58-2 (S)-2-Benzyloxycarbonylamino-3-p-tolyl-propionic acid 
• 93634-54-9 (Z)-2-methyl-4-(4-methylbenzylidene)oxazol-5(4H)-one 
• 104-87-0 4-methyl-benzaldehyde 
• 104-81-4 4-Methylbenzyl bromide 
• 49759-54-8 2-Benzyloxycarbonylamino-3-p-tolyl-propionic acid ethyl ester 
• 49759-46-8 2-Benzyloxycarbonylamino-2-(4-methyl-benzyl)-malonic acid diethyl ester 
• 4599-47-7 p-methylphenylalanine 
• 1866-39-3 trans-p-methylcinnamic acid 
• 683809-83-8 2-amino-3-(4-fluoromethylphenyl)propionic acid 
• 6955-13-1 N-acetyl-4-methyl-phenylalanine 
• 1866-39-3 4-methylcinnamic acid 
• 624-31-7 4-tolyl iodide 
• 38335-22-7 2-oxo-3-(p-tolyl)propanoic acid 
• 3060-50-2 2,2-diphenylglycine 

Downstream Products

• 82057-63-4 (S)-2-(2-Nitro-phenylsulfanylamino)-3-p-tolyl-propionic acid 
• 74046-14-3 (S)-2-Acetylamino-3-p-tolyl-propionic acid 
• 17028-03-4 3-(4-hydroxy-3-methylphenyl)-L-alanine 
• 15742-88-8 L-(p-hydroxymethyl)phenylalanine 
• 479064-87-4 (R)-3-amino-3-(4-methyl-phenyl)-propionic acid 
• 82057-57-6 o-nitrobenzenesulfenyl-p-methylphenylalanyl-isoleucyl-glutaminyl-asparaginyl-S-(β-carboxyethyl)homocysteinyl-prolyl-leucyl-glycine amide 
• 4599-47-7 p-methylphenylalanine 
• 1866-39-3 trans-p-methylcinnamic acid 
• 39260-86-1 p-Methylphenethylamine hydrochloride 
• 98698-22-7 (S)-7-methyl-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid 
• 204260-38-8 (2S)-2-(9H-fluorene-9-ylmethoxycarbonylamino)-3-(4-methylphenyl)propanoic 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.

Ligand-Enabled β-C–H Arylation of α-Amino Acids Without Installing Exogenous Directing Groups

Herein we report acid-directed β-C(sp3)-H arylation of α-amino acids enabled by pyridine-type ligands. This reaction does not require the installation of an exogenous directing group, is scalable, and enables the preparation of Fmoc-protected unnatural amino acids in three steps. The pyridine-type ligands are crucial for the development of this new C(sp3)-H arylation.

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.

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

The invention relates to a novel chiral open-chain pyridoxamine catalyst and a synthesis method and application thereof. The structural general formula of the pyridoxamine catalyst is shown in the specification, wherein R1, R2, R3 and R4 are one of hydrogen, C1-24 alkyl, C1-24 alkyl containing substituent groups, substances shown in the specification and halogen, the substituent groups on C1-24 alkyl are a substance shown in the specification or a substance shown in the specification or a substance shown in the specification or O-Rw or S-Rw' or halogen, and Rx, Rx', Ry, Ry', Ry'', Rz, Rz', Rw and Rw' are one of hydrogen, methyl, ethyl, n-propyl, isopropyl, n-butyl, tertiary butyl, cyclopentyl, cyclohexyl, cycloheptyl, phenyl, benzyl, (1-phenyl)ethyl, 1-naphthyl, 2-naphthyl and halogen. Compared with the prior art, the pyridoxamine catalyst can achieve rapid and efficient synthesis of chiral amino acid, the preparation raw materials are easy to obtain, reaction conditions are mild, cost is low, and when the novel chiral open-chain pyridoxamine catalyst is used for a transamination reaction, the conditions are mild, and the reaction is stable.

A new type of chiral-pyridoxamines for catalytic asymmetric transamination of α-keto acids

A new type of chiral pyridoxamines bearing an adjacent chiral stereocenter has been developed via multi-step synthesis. The pyridoxamines displayed catalytic activity in asymmetric transamination of α-keto acids to give a variety of optically active amino acids in 27–78% yields with 34–62% ee's under very mild conditions. This work provides a synthetic strategy to construct new chiral pyridoxamines using bromopyridine 7 as a key synthon and also represents an early example of the applications of chiral pyridoxamines in asymmetric catalysis.

The bacterial ammonia lyase EncP: A tunable biocatalyst for the synthesis of unnatural amino acids

Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylates, yielding high value amino acids as products. Recent examples include the use of phenylalanine ammonia lyases (PALs), either alone or as a gateway to deracemization cascades (giving (S)- or (R)-α-phenylalanine derivatives, respectively), and also eukaryotic phenylalanine aminomutases (PAMs) for the synthesis of the (R)-β-products. Herein, we present the investigation of another family member, EncP from Streptomyces maritimus, thereby expanding the biocatalytic toolbox and enabling the production of the missing (S)-β-isomer. EncP was found to convert a range of arylacrylates to a mixture of (S)-α- and (S)-β-arylalanines, with regioselectivity correlating to the strength of electron-withdrawing/-donating groups on the ring of each substrate. The low regioselectivity of the wild-type enzyme was addressed via structure-based rational design to generate three variants with altered preference for either α- or β-products. By examining various biocatalyst/substrate combinations, it was demonstrated that the amination pattern of the reaction could be tuned to achieve selectivities between 99:1 and 1:99 for β:α-product ratios as desired.

Efficient kinetic resolution of amino acids catalyzed by lipase AS 'Amano' via cleavage of an amide bond

Herein the efficient kinetic resolution of non-natural alpha-amino acids catalyzed by lipase AS 'Amano' via cleaving the amide bond is reported. The starting materials were the corresponding amino acid amides and the amino acids were generated with ees of up to 99% with E values of >600. These results indicated that the lipase AS 'Amano' could be a powerful amide hydrolase for the kinetic resolution of amino acid starting from the corresponding amino acid amides.

Mechanistic approach of the difference in non-enzymatic hydrolysis rate between the L and D enantiomers of no-carrier added 2-[18F] fluoromethyl-phenylalanine

No-carrier added (n.c.a.) 2-[18F]fluoromethyl-l-phenylalanine was found to be very sensitive to hydrolysis in aqueous solutions. This problem was solved partially by the addition of calcium ions (0.04M), increasing the shelf-life to at least 6h. In this paper the defluorination reaction was studied in detail to elucidate its mechanism. Therefore, L and D enantiomers of 2-[18F]FMP and 4-[18F]FMP were synthesized, as well as 2-[18F]fluoromethyl-phenethylamine and 4-[18F] fluoromethyl-phenethylamine, both decarboxylated 'mimetic' molecules of the amino acid analogues. Radiosynthesis, using a customized Scintomics automatic synthesis hotboxthree module, resulted in a high overall yield and a radiochemical purity of >99%. The defluorination rates of all compounds were studied by HPLC. The L enantiomer of n.c.a 2-[18F]FMP defluorinated seven times faster than the D enantiomer and 2-[18F]fluoromethyl- phenethylamine. Both enantiomers of 4-[18F]FMP and 4-[ 18F]fluoromethyl-phenethylamine were stable. From these data, the reaction mechanism, involving two distinct intramolecular interactions, was derived. First, the interaction between the amine and the benzylic fluorine weakens the carbon-fluorine bond. Secondly, the formation of a second hydrogen bridge between the carboxyl group and one of the benzylic hydrogen atoms renders the fluorine atom even more susceptible to hydrolysis. The latter interaction induces an additional chiral center. The probability of its formation differs considerably between L and D enantiomers of n.c.a. 2-[18F]FMP, which explains the difference in hydrolysis rate. Copyright

Phenylalanine aminomutase-catalyzed addition of ammonia to substituted cinnamic acids: A route to enantiopure α- and β-amino acids

(Chemical Equation Presented) An approach is described for the synthesis of aromatic α- and β-amino acids that uses phenylalanine aminomutase to catalyze a highly enantioselective addition of ammonia to substituted cinnamic acids. The reaction has a broad scope and yields substituted α- and β-phenylalanines with excellent enantiomeric excess. The regioselectivity of the conversion is determined by substituents present at the aromatic ring. A box model for the enzyme active site is proposed, derived from the influence of the hydrophobicity of substituents on the enzyme affinity toward various substrates.

Use of whole cell culture of Aeromonas sp. as enantioselective scavenger: A facile preparation of l-amino acid derivatives in high enantiomeric excess

The bacterium Aeromonas sp. (CGMCC 2226) can enantioselectively scavenge d-isomer, making l-amino acid derivatives (AADs) in high ee. The enantioselective scavenger (ES) has shown a broad substrate scope. Eleven l-AADs, Phe derivatives substituted with methyl-, mono- and dichloro-, bromo-, and nitro-group, were produced in high ee from corresponding racemates.