25951-24-0Relevant articles and documents
Acceptorless dehydrogenation of primary alcohols to carboxylic acids by self-supported NHC-Ru single-site catalysts
Yin, Shenxiang,Zheng, Qingshu,Chen, Jie,Tu, Tao
, p. 165 - 172 (2022/03/23)
The acceptorless dehydrogenation of diverse aromatic and aliphatic primary alcohols to corresponding carboxylic acids has been accomplished by self-supported NHC-Ru single-site catalysts under mild reaction conditions. Besides broad substrates with excellent activity, selectivity and good tolerance to sensitive functional groups, the solid single-site catalyst could be recovered and reused for more than 20 runs without deactivation. Remarkably, up to 1.8 × 104 turnover numbers could be achieved by this newly developed sustainable protocol in gram scale at low catalyst loading, highlighting its potential in industry.
D-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-D-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice
Shibata, Kimihiko,Imanishi, Daiki,Abe, Katsumasa,Suzuki, Masataka,Takahashi, Shouji,Kera, Yoshio
, (2020/09/04)
N-Methyl-D-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of D-aspartate N-methyltransferase (DDNMT), which produces NMDA from D-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for D-aspartate and is S-adenosyl-L-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).
Unraveling Tetrazine-Triggered Bioorthogonal Elimination Enables Chemical Tools for Ultrafast Release and Universal Cleavage
Carlson, Jonathan C.T.,Mikula, Hannes,Weissleder, Ralph
supporting information, p. 3603 - 3612 (2018/03/21)
Recent developments in bond cleavage reactions have expanded the scope of bioorthogonal chemistry beyond click ligation and enabled new strategies for probe activation and therapeutic delivery. These applications, however, remain in their infancy, with fu
