Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase

Cruz-Navarrete, F.A., Baxter, N.J., Flinders, A.J. et al. (4 more authors) (2024) Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase. Communications Biology, 7. 909. ISSN 2399-3642

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© The Author(s) 2024. Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

Keywords: phosphoryl transfer enzyme; allomorphic control mechanism; proline 24 isomerisation; near-attack conformation; NMR spectroscopy; X-ray crystallography; biocatalysis biophysical chemistry; enzyme mechanisms; solution-state NMR
Dates:
  • Published: 27 July 2024
  • Published (online): 27 July 2024
  • Accepted: 11 July 2024
  • Submitted: 12 March 2024
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield)
Depositing User: Symplectic Sheffield
Date Deposited: 29 Jul 2024 15:39
Last Modified: 29 Jul 2024 15:39
Status: Published
Publisher: Nature Portfolio
Refereed: Yes
Identification Number: 10.1038/s42003-024-06577-9
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