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Issue 66, 2017
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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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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.

Graphical abstract: An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor

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Supplementary files

Article information


Submitted
28 Jun 2017
Accepted
27 Jul 2017
First published
28 Jul 2017

This article is Open Access

Chem. Commun., 2017,53, 9238-9241
Article type
Communication

An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor

T. Belz, Y. Jin, J. Coines, C. Rovira, G. J. Davies and S. J. Williams, Chem. Commun., 2017, 53, 9238
DOI: 10.1039/C7CC04977C

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