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

WbbB is a structurally unusual retaining glycosyltransferase. Here, the authors show that WbbB forms an Asp232-Kdo adduct prior to transfer to the saccharide acceptor. Therefore, unlike any previously studied glycosyltransferase, WbbB uses the double-displacement mechanism first proposed in 1953.

Bibliographic Details
Main Authors: Taylor J. B. Forrester, Olga G. Ovchinnikova, Zhixiong Li, Elena N. Kitova, Jeremy T. Nothof, Akihiko Koizumi, John S. Klassen, Todd L. Lowary, Chris Whitfield, Matthew S. Kimber
Format: Article
Language:English
Published: Nature Portfolio 2022-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-33988-1
Description
Summary:WbbB is a structurally unusual retaining glycosyltransferase. Here, the authors show that WbbB forms an Asp232-Kdo adduct prior to transfer to the saccharide acceptor. Therefore, unlike any previously studied glycosyltransferase, WbbB uses the double-displacement mechanism first proposed in 1953.
ISSN:2041-1723