302346-90-3Relevant academic research and scientific papers
Selective inhibitors of bacterial phosphopantothenoylcysteine synthetase
Patrone, James D.,Yao, Jiangwei,Scott, Nicole E.,Dotson, Garry D.
supporting information; experimental part, p. 16340 - 16341 (2010/01/30)
(Figure Presented) Bacterial phosphopantothenolycysteine synthetase (PPCS) catalyzes the formation of phosphopantothenoylcysteine (PPC) from (R)-phosphopantothenate, L-cysteine, and cytidine-5′-triphosphate (CTP) and has been shown to be essential for gro
Synthesis and Characterization of an Anomeric Sulfur Analogue of CMP-Sialic Acid
Cohen, Scott B.,Halcomb, Randall L.
, p. 6145 - 6152 (2007/10/03)
α-2,3-Sialyltransferase catalyzes the transfer of sialic acid from CMP-sialic acid (1) to a lactose acceptor. An analogue of 1 was synthesized in which the anomeric oxygen atom was replaced with a sulfur atom (1S). The key step in the synthesis of IS was a tetrazole-promoted coupling of a cytidine-5′-phosphoramidite with a glycosyl thiol of a protected sialic acid. Compounds 1 and 1S were characterized for their activity in a sialyl transfer assay. The rate of solvolysis in aqueous buffer of analogue 1S was 50-fold slower than that of 1. Analogue 1S was found to be substrate for α-2,3-sialyltransferase. The Km of 1S was just 3-fold higher than that of 1, while the kcat of 1S was 2 orders of magnitude lower compared to 1.
