51703-58-3

Usage

Uses

Used in Pharmaceutical Synthesis:
(RS)-Phenylglycinamide hydrochloride is used as a key intermediate for the synthesis of various pharmaceuticals. Its role is to provide a stable and soluble building block that can be easily incorporated into the development of new drugs.
Used in Biochemical and Pharmacological Studies:
In the field of biochemical and pharmacological research, (RS)-phenylglycinamide hydrochloride is used as a research tool to investigate the function and interactions of amino acids and related compounds. Its application aids in understanding the complex roles these molecules play in biological systems.
Used in Chemical Process Research:
(RS)-Phenylglycinamide hydrochloride is also utilized in the study of chemical processes involving phenylglycine derivatives. Its application in this context helps researchers gain insights into the behavior and properties of these compounds, which can be crucial for the development of new chemical methodologies and applications.

Upstream product

• 15028-40-7 DL-2-phenylglycine methyl ester hydrochloride 
• 100-52-7 benzaldehyde 
• 700-63-0 Phenylglycinamid 
• 16750-42-8 2-amino-2-phenylacetonitrile 

Downstream Products

• 700-63-0 (R)-phenylglycine amide 
• 16256-40-9 2,2-pentamethylene-5-phenylimidazolidone-4 
• 63291-39-4 (R)-phenylglycine amide hydrochloride 
• 60079-51-8 (S)-phenylglycinamide hydrochloride 
• 2935-35-5 (S)-2-phenylglycine 
• 875-74-1 (R)-phenylglycine 

Relevant academic research and scientific papers

Enzymatic synthesis of chiral phenylalanine derivatives by a dynamic kinetic resolution of corresponding amide and nitrile substrates with a multi-enzyme system

Mutant α-amino-ε-caprolactam (ACL) racemase (L19V/L78T) from Achromobacter obae with improved substrate specificity toward phenylalaninamide was obtained by directed evolution. The mutant ACL racemase and thermostable mutant D-amino acid amidase (DaaA) from Ochrobactrum anthropi SV3 co-expressed in Escherichia coli (pACLmut/pDBFB40) were utilized for synthesis of (R)-phenylalanine and non-natural (R)-phenylalanine derivatives (4-OH, 4-F, 3-F, and 2-F-Phe) by dynamic kinetic resolution (DKR). Recombinant E. coli with DaaA and mutant ACL racemase genes catalyzed the synthesis of (R)-phenylalanine with 84% yield and 99% ee from (RS)-phenylalaninamide (400 mM) in 22 h. (R)-Tyrosine and 4-fluoro-(R)-phenylalanine were also efficiently synthesized from the corresponding amide compounds. We also co-expresed two genes encoding mutant ACL racemase and L-amino acid amidase from Brevundimonas diminuta in E. coli and performed the efficient production of various (S)-phenylalanine derivatives. Moreover, 2-aminophenylpropionitrile was converted to (R)-phenylalanine by DKR using a combination of the non-stereoselective nitrile hydratase from recombinamt E. coli and mutant ACL racemase and DaaA from E. coli encoding mutant ACL racemase and DaaA genes. Copyright

IMIDAZOLINONE DERIVATIVES AS CGRP RECEPTOR ANTAGONISTS

The present invention is directed to imidazolinone derivatives which are antagonists of CGRP receptors and useful in the treatment or prevention of diseases in which CGRP is involved, such as migraine. The invention is also directed to pharmaceutical comp

CONVERSION OF α-AMINONITRILES TO AMIDES BY A NEW PINNER TYPE REACTION

α-Aminonitriles were converted exclusively to the amides by 2-mercaptoethanol in anhydrous THF at -78 deg C by bubbling dry HCl gas.

Hydrolysis of various nitrile compounds to the amides by catalysis of 2-mercaptoethanol in a phosphate buffer

α-Aminonitriles, 4-nitrobenzonitrile and 3,5-dinitrobenzonitrile were hydrolyzed exclusively to amides efficiently when they were stirred with 2-mercaptoethanol in a phosphate buffer (pH 7.0, 50 mM).