30433-91-1Relevant articles and documents
Application of the cyanurate-isocyanurate rearrangement to amine synthesis: Preparation of 2-(2-thienyl)ethylamine
Harrington,Sanchez
, p. 1307 - 1314 (1993)
This communication describes a new method for preparation of 2-(2-thienyl)ethylamine, an important pharmaceutical intermediate. The method is based on the O-to-N migration of an alkyl group via cyanurate-isocyanurate rearrangment.
1,2,5-oxadiazole derivative used as indoleamine 2,3-dioxygenase inhibitor
-
, (2019/10/01)
The invention belongs to the technical field of 1,2,5-oxadiazole derivatives, and particularly relates to a 1,2,5-oxadiazole derivative or a pharmaceutically acceptable salt thereof which is used as an indoleamine 2,3-dioxygenase inhibitor. The structure of the 1,2,5-oxadiazole derivative or the pharmaceutically acceptable salt thereof used as the IDO inhibitor is shown in the following formula I.The invention provides a general formula compound I with a novel structure. Experimental results show that some compounds have excellent IDO inhibitory activity and permeation performance at the sametime. The compound is expected to be marketed as a tumor molecular immunotherapeutic drug for cancer treatment.
Generation of novel family of reductases from PCR based library for the synthesis of chiral alcohols and amines
Sehajpal, Pallvi,Kirar, Seema,Ghosh, Saptarshi,Banerjee, Uttam Chand
, p. 83 - 91 (2018/08/17)
Biocatalysis has shown tremendous potential in the synthesis of drugs and drug intermediates in the last decade. Screening of novel biocatalysts from the natural genome space is the growing trend to replenish the harsh chemical synthetic routes, commonly used in the pharmaceutical and chemical industry. Here, we report a novel ketoreductase (KERD) and a nitrile reductase isolated from the PCR based library generated from the genome of Rhodococcus ruber and Bacillus subtilis, respectively. Both the proteins are hypothetical in nature as there is no putative homology found in the database, although both the enzymes have significant activity towards the synthesis of chiral alcohols and amines. Enzyme activity over a wide range of substrates (aromatic and aliphatic) for both the novel catalysts was observed. From the unique gene sequence to activity over a broad range of substrate and >99% conversion at higher concentrations (100 mM and above) entitles both the hypothetical enzymes as novel. The novel KERD has shown >99% selectivity for the synthesis of (S)-phenylethanol which makes it a potential candidate for industrial catalysis. The novel nitrile reductase has also shown promising activity for the synthesis of (R)-2-phenylethanolamine, which is a difficult moiety to synthesize chemically. In this report, starting from a homology based library, two highly potent whole cell biocatalysts are obtained.