67206-16-0 Usage
Classification
Amino acid derivative This compound is classified as an amino acid derivative because it contains both an amino group (-NH2) and a carboxylic acid group (-COOH) in its structure.
Chloroacetyl functional group
A combination of chlorine and acetyl groups (-COCH3) The presence of the chloroacetyl group gives this compound its unique structure and potential reactivity with biological molecules.
Potential applications
Medicinal chemistry or biochemistry Due to its unique structure and potential reactivity with biological molecules, 2-[(chloroacetyl)amino]pent-4-enoic acid may have potential applications in the fields of medicinal chemistry or biochemistry.
Further research and testing
Necessary to determine specific properties and potential uses Before this compound can be utilized in any practical applications, additional research and testing are required to understand its specific properties and potential uses.
Check Digit Verification of cas no
The CAS Registry Mumber 67206-16-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,7,2,0 and 6 respectively; the second part has 2 digits, 1 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 67206-16:
(7*6)+(6*7)+(5*2)+(4*0)+(3*6)+(2*1)+(1*6)=120
120 % 10 = 0
So 67206-16-0 is a valid CAS Registry Number.
67206-16-0Relevant 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.
