The retaining β-Kdo glycosyltransferase WbbB uses a double-displacement mechanism with an intermediate adduct rearrangement step

WbbB, a lipopolysaccharide O-antigen synthesis enzyme from Raoultella terrigena, contains an N-terminal glycosyltransferase domain with a highly modified architecture that adds a terminal β-Kdo (3-deoxy-d-manno-oct-2-ulosonic acid) residue to the O-antigen saccharide, with retention of stereochemist...

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Detalles Bibliográficos
Autores principales: Forrester, Taylor J. B., Ovchinnikova, Olga G., Li, Zhixiong, Kitova, Elena N., Nothof, Jeremy T., Koizumi, Akihiko, Klassen, John S., Lowary, Todd L., Whitfield, Chris, Kimber, Matthew S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9587256/
https://www.ncbi.nlm.nih.gov/pubmed/36271007
http://dx.doi.org/10.1038/s41467-022-33988-1

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9587256/
https://www.ncbi.nlm.nih.gov/pubmed/36271007
http://dx.doi.org/10.1038/s41467-022-33988-1

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