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An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor
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| Journal | Chemical Communications |
|---|---|
| Date | Accepted/In press - 27 Jul 2017 |
| Date | E-pub ahead of print - 28 Jul 2017 |
| Date | Published (current) - 25 Aug 2017 |
| Issue number | 66 |
| Volume | 53 |
| Number of pages | 4 |
| Pages (from-to) | 9238-9241 |
| Early online date | 28/07/17 |
| Original language | English |
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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©The Royal Society of Chemistry 2017. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
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