Synthesis of Partially O-Acetylated N-Acetylneuraminic Acid Using Regioselective Silyl Exchange Technology
نویسندگان
چکیده
منابع مشابه
Synthesis of Partially O-Acetylated N-Acetylneuraminic Acid Using Regioselective Silyl Exchange Technology
Postglycosylation acetylation of sialic acid imparts unique roles to sialoglycoconjugates in mammalian immune response making structural and functional understanding of these analogues important. Five partially O-acetylated Neu5Ac analogues have been synthesized. Reaction of per-O-silylated Neu5Ac ester with AcOH and Ac2O in pyridine promotes regioselective silyl ether/acetate exchange in the f...
متن کاملYjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid.
The nanATEK-yhcH, yjhATS, and yjhBC operons in Escherichia coli are coregulated by environmental N-acetylneuraminic acid, the most prevalent sialic acid in nature. Here we show that YjhS (NanS) is a probable 9-O-acetyl N-acetylneuraminic acid esterase required for E. coli to grow on this alternative sialic acid, which is commonly found in mammalian host mucosal sites.
متن کاملSynthesis of N-acetylneuraminic acid and of CMP-N-acetylneuraminic acid in the rat liver cell.
Adult male rats, under starving and normal conditions, were injected intravenously with N-acetyl[3H]mannosamine and after various time intervals the specific radioactivities of free N-acetylneuraminic acid (NeuAc) and CMP-N-acetylneuraminic acid were determined in the liver. The specific radioactivity of free NeuAc was high even within 20s after injection; the maximum was reached between 7 and ...
متن کاملCorrigendum: Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis process
The original version of this article contained an error in testing the kinetic parameters of CgNal towards pyruvate, in which the concentration of ManNAc (50 mM) was not in excess. This error was corrected by re-running the assay in the presence of excessive ManNAc (180 mM). The corrected kinetic parameters of CgNal towards pyruvate are shown in Table 1. These changes do not change the conclusi...
متن کاملCharacterization of a novel N-acetylneuraminic acid lyase favoring N-acetylneuraminic acid synthesis
N-Acetylneuraminic acid lyase (NAL, E.C. number 4.1.3.3) is a Class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) from pyruvate and N-acetyl-D-mannosamine (ManNAc). Due to the equilibrium favoring Neu5Ac cleavage, the enzyme catalyzes the rate-limiting step of two biocatalytic reactions producing Neu5Ac in industry. We report the biochemical charact...
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ژورنال
عنوان ژورنال: Organic Letters
سال: 2014
ISSN: 1523-7060,1523-7052
DOI: 10.1021/ol502389g