28292-43-5 Usage
Description
2-AMINO-5-METHYLHEXANE is an aliphatic amine that exists as a colorless oil. It is primarily utilized in the synthesis of various cyclic nitrogen-based compounds, which have a wide range of applications in different industries.
Uses
Used in Pharmaceutical Industry:
2-AMINO-5-METHYLHEXANE is used as a chemical intermediate for the production of pyridines and other cyclic nitrogen-based compounds. These compounds are essential in the development of various pharmaceutical products, such as antiparasitics and calcium channel inhibitors. The application reason is that these cyclic compounds possess unique properties that make them effective in treating specific medical conditions.
Used in Chemical Synthesis:
2-AMINO-5-METHYLHEXANE is used as a building block in the synthesis of complex organic molecules. Its aliphatic amine functionality allows for various chemical reactions, making it a versatile compound in the field of organic chemistry. The application reason is its ability to form a wide range of products with different properties and applications.
Check Digit Verification of cas no
The CAS Registry Mumber 28292-43-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,8,2,9 and 2 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 28292-43:
(7*2)+(6*8)+(5*2)+(4*9)+(3*2)+(2*4)+(1*3)=125
125 % 10 = 5
So 28292-43-5 is a valid CAS Registry Number.
InChI:InChI=1/C7H17N/c1-6(2)4-5-7(3)8/h6-7H,4-5,8H2,1-3H3/p+1/t7-/m0/s1
28292-43-5Relevant articles and documents
Biochemical and Structural Characterization of an (R)-Selective Transaminase in the Asymmetric Synthesis of Chiral Hydroxy Amines
Li, Fulong,Liang, Youxiang,Wei, Yuwen,Zheng, Yukun,Du, Yan,Yu, Huimin
, p. 4582 - 4589 (2021/08/07)
An (R)-selective transaminase RbTA with excellent stereoselectivity (>99% ee) in the asymmetric amination of hydroxy ketones was identified. Biochemical characterization showed that RbTA exhibited the highest activity toward 4-hydroxy-2-butanone among reported enzymes, and that it has broad substrate specificity, including for aliphatic, aromatic, and alicyclic ketones. Crystallization of RbTA were performed, as were molecular docking and mutagenesis studies. Residue Tyr125 plays a key role in substrate recognition by forming a hydrogen bond with hydroxy ketone. The applicability of the enzyme was determined in preparative-scale synthesis of (R)-3-amino-1-butanol, demonstrating the potential of RbTA as a green biocatalyst for production of value-added chiral hydroxy amines. This study provides an efficient tool for enzymatic synthesis of chiral hydroxy amines, as well as structural insight into substrate recognition by transaminases in the asymmetric amination of hydroxy ketones. (Figure presented.).