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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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JournalChemical Communications
DateAccepted/In press - 27 Jul 2017
DateE-pub ahead of print - 28 Jul 2017
DatePublished (current) - 25 Aug 2017
Issue number66
Number of pages4
Pages (from-to)9238-9241
Early online date28/07/17
Original languageEnglish


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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