7765-11-9 Usage
General Description
Chloroacetyl-DL-Phenylalanine is a chemical compound that's generally used for scientific research purposes. The "DL" signifies that it contains two enantiomers, or mirror image molecules, which often are of interest in biochemistry and pharmacology. It's derived from Phenylalanine, one of the essential amino acids used in the biosynthesis of proteins. While this compound is not widely discussed in publicly available literature, it is important to note that it should be handled with proper precautions due to the potential reactivity of the chloroacetyl group. As with many technical chemicals, specialized knowledge is required to handle and use it safely and effectively, therefore its use is typically confined to professional research or industrial contexts.
Check Digit Verification of cas no
The CAS Registry Mumber 7765-11-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,7,6 and 5 respectively; the second part has 2 digits, 1 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 7765-11:
(6*7)+(5*7)+(4*6)+(3*5)+(2*1)+(1*1)=119
119 % 10 = 9
So 7765-11-9 is a valid CAS Registry Number.
InChI:InChI=1/C11H12ClNO3/c12-7-10(14)13-9(11(15)16)6-8-4-2-1-3-5-8/h1-5,9H,6-7H2,(H,13,14)(H,15,16)/t9-/m1/s1
7765-11-9Relevant articles and documents
Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I
Chenault, H. Keith,Dahmer, Juergen,Whitesides, George M.
, p. 6354 - 6364 (2007/10/02)
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.
