Abstract 2492 NDP-hexose substrate binding mechanism in bifunctional Neisseria meningitidis capsular polymerases
Glycans are essential components of extracellular surfaces where they mediate diverse functions including cell-cell recognition and adhesion. They also serve as biomaterials in various applications. Glycosytransferases (GTs) with different specificities provide a route for the synthesis of glycans with desired composition and there are attempts to engineer GTs to confer new properties including substrate specificities. Thus, the objective of this study was to investigate the mechanisms of substrate binding to generate a better understanding of the catalytic mechanism.
Authors
- Frances M. Moore (ORCID: https://orcid.org/0000-0003-2494-0235)
- Pumtiwitt C. McCarthy (ORCID: https://orcid.org/0000-0003-4096-1677)
- James Wachira (ORCID: https://orcid.org/0000-0001-7423-6743)
- T. J. Newman (ORCID: https://orcid.org/0000-0002-0332-337X)
- John-Paul Akinbami
Institutions
- University of New Mexico (US)
- San Diego State University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109203
- Primary Topic
- Supramolecular Chemistry and Complexes
- Type
- article
- Field-Weighted Citation Impact
- 0.00