4395-73-7Relevant articles and documents
Enzymatic Primary Amination of Benzylic and Allylic C(sp3)-H Bonds
Jia, Zhi-Jun,Gao, Shilong,Arnold, Frances H.
supporting information, p. 10279 - 10283 (2020/07/27)
Aliphatic primary amines are prevalent in natural products, pharmaceuticals, and functional materials. While a plethora of processes are reported for their synthesis, methods that directly install a free amine group into C(sp3)-H bonds remain unprecedented. Here, we report a set of new-to-nature enzymes that catalyze the direct primary amination of C(sp3)-H bonds with excellent chemo-, regio-, and enantioselectivity, using a readily available hydroxylamine derivative as the nitrogen source. Directed evolution of genetically encoded cytochrome P411 enzymes (P450s whose Cys axial ligand to the heme iron has been replaced with Ser) generated variants that selectively functionalize benzylic and allylic C-H bonds, affording a broad scope of enantioenriched primary amines. This biocatalytic process is efficient and selective (up to 3930 TTN and 96percent ee), and can be performed on preparative scale.
Arylalkylamine vanadium (V) salts for the treatment and/or prevention of Diabetes mellitus
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Page/Page column 19; 20, (2010/11/26)
This invention provides compounds of formula (IIA) and pharmaceutical compositions thereof, where M, a, b, and R1-R5 are as defined herein, for treating human type 1 and type 2 diabetes, particularly insulin-resistant diabetes. Pharmaceutical compositions comprising the compounds of formula (IIA) are also disclosed.
New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: Analysis by SARs and computational docking
Yraola, Francesc,García-Vicente, Silvia,Fernández-Recio, Juan,Albericio, Fernando,Zorzano, Antonio,Marti, Luc,Royo, Miriam
, p. 6197 - 6208 (2007/10/03)
Structure activity relationships for semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1) were studied using a library of arylalkylamine substrates, with the aim of contributing to the discovery of more efficient SSAO substrates. Experimental data were contrasted with computational docking studies, thereby allowing us to examine the mechanism and substrate-binding affinity of SSAO and thus contribute to the discovery of more efficient SSAO substrates and provide a structural basis for their interactions. We also built a model of the mouse SSAO structure, which provides several structural rationales for interspecies differences in SSAO substrate selectivity and reveals new trends in SSAO substrate recognition. In this context, we identified novel efficient substrates for human SSAO that can be used as a lead for the discovery of antidiabetic agents.
