31982-78-2 Usage
General Description
L-Leucine hydroxamate is a chemical compound derived from the amino acid leucine, which is an essential amino acid involved in protein synthesis and muscle repair. L-leucine hydroxamate has been studied for its potential use as an antioxidant and anti-inflammatory agent, as well as its ability to enhance the production of cellular energy. It has also been investigated for its potential in cancer treatment, as it has been shown to inhibit the growth of cancer cells in experimental studies. Additionally, L-leucine hydroxamate has demonstrated the ability to protect against oxidative stress and may have potential applications in the treatment of neurodegenerative diseases. However, further research is needed to fully understand its potential therapeutic benefits and to determine its safety for use in humans.
Check Digit Verification of cas no
The CAS Registry Mumber 31982-78-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,1,9,8 and 2 respectively; the second part has 2 digits, 7 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 31982-78:
(7*3)+(6*1)+(5*9)+(4*8)+(3*2)+(2*7)+(1*8)=132
132 % 10 = 2
So 31982-78-2 is a valid CAS Registry Number.
InChI:InChI=1/C6H14N2O2/c1-4(2)3-5(7)6(9)8-10/h4-5,10H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1
31982-78-2Relevant articles and documents
-
Safir,Williams
, p. 1298,1300 (1952)
-
Production of hydroxamic acids by immobilized Pseudomonas aeruginosa cells: Kinetic analysis in reverse micelles
Bernardo, Marisa,Pacheco, Rita,Serralheiro, Maria Luisa M.,Karmali, Amin
, p. 28 - 33 (2013/07/19)
Intact cells from Pseudomonas aeruginosa strain L10 containing amidase were used as biocatalysts both free and immobilized in a reverse micellar system. The apparent kinetic constants for the transamidation reaction in hydroxamic acids synthesis, were determined using substrates such as aliphatic, amino acid and aromatic amides and esters, in both media. In reverse micelles, K m values decreased 2-7 fold relatively to the free biocatalyst using as substrates acetamide, acrylamide, propionamide and glycinamide ethyl ester. We have concluded that overall the affinity of the biocatalyst to each substrate increases when reactions are performed in the reversed micellar system as opposed to the buffer system. The immobilized biocatalyst in general, exhibits higher stability and faster rates of reactions at lower substrates concentration relatively to the free form, which is advantageous. Additionally, the immobilization revealed to be suitable for obtaining the highest yields of hydroxamic acids derivatives, in some cases higher than 80%.
