133992-69-5 Usage
Uses
Used in Pharmaceutical Industry:
2-ACETYLAMINO-3-CYCLOPROPYLPROPIONIC ACID is used as an anti-inflammatory and analgesic agent for the treatment of pain and inflammation associated with conditions such as rheumatoid arthritis, osteoarthritis, and ankylosing spondylitis. It functions by inhibiting the production of prostaglandins, which are substances in the body that cause inflammation and pain.
Used in Pain Management:
2-ACETYLAMINO-3-CYCLOPROPYLPROPIONIC ACID is used as a pain reliever to alleviate discomfort caused by various conditions, including musculoskeletal disorders and inflammatory diseases. It is available in oral tablet form and is generally well-tolerated, although it may cause side effects such as stomach upset, dizziness, and skin rash in some individuals.
It is important to use 2-ACETYLAMINO-3-CYCLOPROPYLPROPIONIC ACID under the supervision of a healthcare professional and to follow their recommended dosage and administration instructions to ensure safe and effective treatment.
Check Digit Verification of cas no
The CAS Registry Mumber 133992-69-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,3,9,9 and 2 respectively; the second part has 2 digits, 6 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 133992-69:
(8*1)+(7*3)+(6*3)+(5*9)+(4*9)+(3*2)+(2*6)+(1*9)=155
155 % 10 = 5
So 133992-69-5 is a valid CAS Registry Number.
InChI:InChI=1/C8H13NO3/c1-5(10)9-7(8(11)12)4-6-2-3-6/h6-7H,2-4H2,1H3,(H,9,10)(H,11,12)
133992-69-5Relevant 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
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.
