4090-17-9

Usage

Uses

Used in Organic Chemistry:
Chloroacetyl-DL-Valine is used as a chemical intermediate for the synthesis of other complex chemicals. Its chloroacetyl group enables it to form bonds with a variety of molecules, making it a versatile reagent in organic chemistry.
Used in Pharmaceutical Industry:
Chloroacetyl-DL-Valine is used as a building block in the development of pharmaceuticals. Its ability to react with other molecules allows for the creation of new drug candidates with potential therapeutic applications.
Used in Chemical Reactions:
Chloroacetyl-DL-Valine is used as a reagent in various chemical reactions due to its reactive chloroacetyl group. This property makes it a useful tool for researchers and chemists in the synthesis of new compounds and materials.

InChI:InChI=1/C7H12ClNO3/c1-4(2)6(7(11)12)9-5(10)3-8/h4,6H,3H2,1-2H3,(H,9,10)(H,11,12)

Upstream product

• 516-06-3 D,L-valine 
• 79-04-9 chloroacetyl chloride 
• 640-68-6 D-Val-OH 

Downstream Products

• 759-05-7 3-methyl-2-ketobutanoic acid 
• 7664-41-7 ammonia 
• 64-19-7 acetic acid 
• 17623-72-2 2-methyl-4-iso-propyl-4H-oxazolin-5-one 
• 109924-85-8 racemic Ac-ΔVal-Phe-OMe 
• 1963-21-9 L-glycyl-L-valine 
• 2325-17-9 Glycylvaline 
• 4894-12-6 4-isopropylidene-2-methyloxazol-5(4H)-one 
• 4997-97-1 pseudooxazolone 
• 87177-39-7 2-[2-(Diethoxy-thiophosphorylsulfanyl)-acetylamino]-3-methyl-butyric acid 

Relevant academic research and scientific papers

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.