302346-96-9Relevant academic research and scientific papers
Synthesis and Characterization of an Anomeric Sulfur Analogue of CMP-Sialic Acid
Cohen, Scott B.,Halcomb, Randall L.
, p. 6145 - 6152 (2000)
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.
Creatine phosphate-creatine kinase in enzymatic synthesis of glycoconjugates
Zhang, Jianbo,Wu, Bingyuan,Zhang, Yingxin,Kowal, Przemyslaw,Wang, Peng George
, p. 2583 - 2586 (2007/10/03)
Enzymatic production of glycoconjugates is hampered by expensive phosphagens such as acetyl phosphate (AcP) and phosphoenolpyruvate (PEP). Here, we introduce creatine phosphate-creatine kinase system as a novel and practical energy source in carbohydrate
