75383-61-8 Usage
Uses
Used in Pharmaceutical Research:
Benzyl 3-hydroxybenzylcarbamate is employed as an intermediate in organic synthesis, contributing to the development of new pharmaceutical compounds. Its unique structure allows it to be a valuable component in the creation of various drugs.
Used in Neurodegenerative Disease Treatment:
Benzyl 3-hydroxybenzylcarbamate is used as a potential therapeutic agent for neurodegenerative diseases such as Alzheimer's. Its role as an inhibitor of acetylcholinesterase makes it a candidate for further exploration in treating conditions that involve the breakdown of acetylcholine, thereby potentially slowing the progression of cognitive decline.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, benzyl 3-hydroxybenzylcarbamate is used as a target for research and development. Its potential pharmacological properties and the possibility of enhancing its biological activities through structural modifications make it an attractive subject for scientific inquiry and drug design.
Check Digit Verification of cas no
The CAS Registry Mumber 75383-61-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,5,3,8 and 3 respectively; the second part has 2 digits, 6 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 75383-61:
(7*7)+(6*5)+(5*3)+(4*8)+(3*3)+(2*6)+(1*1)=148
148 % 10 = 8
So 75383-61-8 is a valid CAS Registry Number.
InChI:InChI=1/C15H15NO3/c17-14-8-4-7-13(9-14)10-16-15(18)19-11-12-5-2-1-3-6-12/h1-9,17H,10-11H2,(H,16,18)
75383-61-8Relevant academic research and scientific papers
Efficient Tryptic Hydrolysis of Aryl Esters with a Cationic Center in the Leaving Group. Further Characterization of "Inverse Substrates"
Nakano, Michiharu,Tanizawa, Kazutaka,Nozawa, Masayuki,Kanaoka, Yuichi
, p. 2212 - 2215 (2007/10/02)
The kinetic properties of esters derived from guanidinophenol and aminomethylphenol were investigated with trypsin.These compounds, in which the site-specific groups (positive charge) are of inverse type compared with normal substrates, were demonstrated to be specific substrates, like aminophenyl esters.The behavior of these "inverse substrates" with trypsin and pseudotrypsin was also compared.A dramatic decrease in the efficiency of hydrolysis of the "inverse substrates" by pseudotrypsin as compared to that by trypsin was observed, which was comparable in extent to that observed for specific normal-type substrates.All these observations confirm the view that specific interaction between the positive charge at the leaving moiety of "inverse substrates" and the anionic site of the trypsin active center is an essential feature of the catalysis, just as in the case of normal-type substrates.
