Belz, Tyson, Jin, Yi orcid.org/0000-0002-6927-4371, Coines, Joan et al. (3 more authors) (2017) An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor. Chemical Communications. pp. 9238-9241. ISSN 1364-548X
Abstract
The non-hydrolyzable S-linked azasugars, 1,6-α-mannosylthio- and 1,6-α-mannobiosylthioisofagomine, were synthesized and shown to bind with high affinity to a family 76 endo-1,6-α-mannanase from Bacillus circulans. X-ray crystallography showed an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener.
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Item Type: | Article | ||||||
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Copyright, Publisher and Additional Information: | ©The Royal Society of Chemistry 2017. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. | ||||||
Dates: |
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Institution: | The University of York | ||||||
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) | ||||||
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Depositing User: | Pure (York) | ||||||
Date Deposited: | 11 Sep 2017 16:15 | ||||||
Last Modified: | 09 Apr 2024 23:10 | ||||||
Published Version: | https://doi.org/10.1039/c7cc04977c | ||||||
Status: | Published | ||||||
Refereed: | Yes | ||||||
Identification Number: | https://doi.org/10.1039/c7cc04977c | ||||||
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