1. Biochemical characterization of Helicobacter pylori α1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides.
- Author
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Bai J, Wu Z, Sugiarto G, Gadi MR, Yu H, Li Y, Xiao C, Ngo A, Zhao B, Chen X, and Guan W
- Subjects
- Chemistry Techniques, Synthetic, Humans, Hydrogen-Ion Concentration, Metals pharmacology, Fucose chemistry, Fucosyltransferases metabolism, Helicobacter pylori enzymology, Milk, Human chemistry, Oligosaccharides chemical synthesis, Oligosaccharides chemistry
- Abstract
Fucosylated human milk oligosaccharides (HMOs) have important biological functions. Enzymatic synthesis of such compounds requires robust fucosyltransferases. A C-terminal 66-amino acid truncated version of Helicobacter pylori α1-3-fucosyltransferase (Hp3FT) is a good candidate. Hp3FT was biochemically characterized to identify optimal conditions for enzymatic synthesis of fucosides. While N-acetyllactosamine (LacNAc) and lactose were both suitable acceptors, the former is preferred. At a low guanosine 5'-diphospho-β-L-fucose (GDP-Fuc) to acceptor ratio, Hp3FT selectively fucosylated LacNAc. Based on these enzymatic characteristics, diverse fucosylated HMOs, including 3-fucosyllactose (3-FL), lacto-N-fucopentaose (LNFP) III, lacto-N-neofucopentaose (LNnFP) V, lacto-N-neodifucohexaose (LNnDFH) II, difuco- and trifuco-para-lacto-N-neohexaose (DF-paraLNnH and TF-para-LNnH), were synthesized enzymatically by varying the ratio of the donor and acceptor as well as controlling the order of multiple glycosyltransferase-catalyzed reactions., (Copyright © 2019 Elsevier Ltd. All rights reserved.)
- Published
- 2019
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