701907-44-0

Usage

Uses

Used in Pharmaceutical Industry:
(S)-3-Amino-3-(3-methyl-phenyl)-propionic acid is used as a chiral building block for the synthesis of various pharmaceutical compounds, contributing to the development of new drugs with improved efficacy and selectivity.
Used in Peptide Synthesis:
(S)-3-Amino-3-(3-methyl-phenyl)-propionic acid is used as an amino acid derivative in the synthesis of peptides, enabling the creation of novel peptide-based therapeutics and diagnostic agents.
Used in Biochemical Research:
(S)-3-Amino-3-(3-methyl-phenyl)-propionic acid is used as a research reagent in biochemical studies, aiding in the investigation of biological processes and the discovery of new drug targets.

InChI:InChI=1/C10H13NO2/c1-7-3-2-4-8(5-7)9(11)6-10(12)13/h2-5,9H,6,11H2,1H3,(H,12,13)/t9-/m0/s1

Upstream product

• 33166-79-9 ethyl m-toluoylacetate 
• 3029-79-6 3-methylcinnamic acid 
• 68208-17-3 (R,S)-3-amino-3-(3-methylphenyl)propionic acid 

Downstream Products

• 1318785-08-8 (S)-3-{[1-(2-fluoro-phenyl)-5-hydroxy-1H-pyrazole-3-carbonyl]-amino}-3-m-tolyl-propionic acid 

Relevant academic research and scientific papers

Glutamate as an Efficient Amine Donor for the Synthesis of Chiral β- and γ-Amino Acids Using Transaminase

A recyclable glutamate amine donor system employing transaminase (TA), glutamate dehydrogenase (GluDH) and mutant formate dehydrogenase (FDHm) was developed, wherein amine donor Glu was regenerated using GluDH and thereby circumvented the inhibition of TA by α-ketoglutarate. Various enantiopure β-, γ-amino acids, and amines were successfully synthesized with high conversions and excellent enantiomeric excess using this system.

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 tandem biocatalytic process for the kinetic resolution of aromatic β-amino acids

We describe a simple and efficient enzymatic tandem reaction for the preparation of enantiomerically pure β-phenylalanine and its analogues from the corresponding racemates. In this process, phenylalanine aminomutase (PAM) catalyzes the stereoselective isomerization of (R)-β-phenylalanines to (S)-a-phenylalanines, which are in situ transformed to cinnamic acids by phenylalanine ammonia lyase (PAL). Preparative scale conversions are done with a mutated PAM with enhanced catalytic activity.