29076-84-4Relevant articles and documents
Hydrogen bond directed aerobic oxidation of amines via photoredox catalysis
Wang, Hongyu,Man, Yunquan,Wang, Kaiye,Wan, Xiuyan,Tong, Lili,Li, Na,Tang, Bo
supporting information, p. 10989 - 10992 (2018/10/08)
An application of H-bonding interactions for directing the α-C-H oxidation of amines to amides and amino-ketones catalyzed by an organic photocatalyst is reported. The high efficiency of this method is demonstrated by the aerobic oxidation of pyrrolidines, diarylamines and benzylamines bearing urea groups with high yields and a wide substrate scope.
CATALYTIC PREPARATION OF ENAMIDES FROM ALKYL AZIDES AND ACYL DONORS
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Paragraph 0118-0119, (2016/10/10)
The present invention relates to a method to synthesize an enamide compound by generating imine which does not have a substituent group bonded to the nitrogen from an organic azide compound and conducting a reaction of the same with acyl doner. By using t
Tailoring D-amino acid oxidase from the pig kidney to r-stereoselective amine oxidase and its use in the deracemization of α-methylbenzylamine
Yasukawa, Kazuyuki,Nakano, Shogo,Asano, Yasuhisa
, p. 4428 - 4431 (2014/05/06)
The deracemization of racemic amines to yield enantioenriched amines using S-stereoselective amine oxidases (AOx) has recently been attracting attention. However, R-stereoselective AOx that are suitable for deracemization have not yet been identified. An R-stereoselective AOx was now evolved from porcine kidney D-amino acid oxidase (pkDAO) and subsequently use for the deracemization of racemic amines. The engineered pkDAO, which was obtained by directed evolution, displayed a markedly changed substrate specificity towards R?amines. The mutant enzyme exhibited a high preference towards the substrate α- methylbenzylamine and was used to synthesize the S?amine through deracemization. The findings of this study indicate that further investigations on the structure-activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis. A change in selectivity: An engineered porcine kidney D-amino acid oxidase (pkDAO) with markedly changed substrate selectivity towards R?amines was obtained by directed evolution. The mutant enzyme exhibited a high preference towards the substrate α-methylbenzylamine and was used to synthesize the S-configured amine through deracemization.