Biochemical characterization of Helicobacter pylori α1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides.
Carbohydr Res
; 480: 1-6, 2019 Jul 01.
Article
en En
| MEDLINE
| ID: mdl-31132553
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-ß-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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oligosacáridos
/
Helicobacter pylori
/
Fucosa
/
Fucosiltransferasas
/
Leche Humana
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Carbohydr Res
Año:
2019
Tipo del documento:
Article
País de afiliación:
China