137503-97-0

Basic information

• Product Name: CHLOROAC-D-PHE-OH
• Synonyms: N-CHLOROACETYL-D-PHENYLALANINE;N-ALPHA-CHLOROACETYL-D-PHENYLALANINE;CHLOROAC-D-PHENYLALANINE;CHLOROAC-D-PHE-OH;CHLOROACETYL-D-PHENYLALANINE;CLAC-D-PHE-OH;N-(2-Chloroacetyl)-B-phenyl-D-alanine;(R)-α-[(Chloroacetyl)amino]benzenepropanoic acid
• CAS NO: 137503-97-0
• Molecular Formula: C₁₁H₁₂ClNO₃
• Molecular Weight: 241.67
• EINECS: 932-536-4
• Mol File: 137503-97-0.mol
• Article Data: 1

Chemical Properties

• Melting Point: 125 °C
• Boiling Point: 482.2 °C at 760 mmHg
• Flash Point: 245.4 °C
• Appearance: /
• Density: 1.312 g/cm³
• Refractive Index: -49 ° (C=1, EtOH)
• Storage Temp.: Store at RT.
• CAS DataBase Reference: CHLOROAC-D-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: CHLOROAC-D-PHE-OH(137503-97-0)
• EPA Substance Registry System: CHLOROAC-D-PHE-OH(137503-97-0)

Safety Data

• Hazardous Substances Data: 137503-97-0(Hazardous Substances Data)

Usage

General Description

"CHLOROAC-D-PHE-OH" is the chemical name for N-(4-chloro-2-butanoyl)phenylalanine, a compound often used in the synthesis of pharmaceuticals. CHLOROAC-D-PHE-OH is an amino acid derivative, containing a chloroacetyl group and a phenylalanine residue. It is commonly used in the development of drugs for various medical conditions, including cancer and neurodegenerative diseases. Its properties and structure make it a valuable building block in the production of new molecules with potential therapeutic applications.

Upstream product

• 150-30-1 Phenylalanine 
• 7765-11-9 N-chloroacetyl-DL-phenylalanine 

Downstream Products

• 673-06-3 D-(R)-phenylalanine 
• 34258-14-5 glycyl-D-phenylalanine 
• 23927-19-7 (R)-3-benzyl-2,5-piperazinedione 

Relevant articles and documents

Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I

Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occuring α-amino acids.Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis.Eleven α-amino and α-methyl α-amino acids were resolved on a 2-29-g scale.Crude L- and D-amino acid products had generally >90percent ee.The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.