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

Belz, Tyson, Jin, Yi ORCID: https://orcid.org/0000-0002-6927-4371, Coines, Joan, Rovira, Carme, Davies, Gideon J. and Williams, Spencer J. 2017. An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor. Chemical Communications 53 , pp. 9238-9241. 10.1039/C7CC04977C

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Chemistry
Publisher:	Royal Society of Chemistry
ISSN:	1359-7345
Date of First Compliant Deposit:	31 August 2017
Date of Acceptance:	27 July 2017
Last Modified:	12 Nov 2024 17:00
URI:	https://orca.cardiff.ac.uk/id/eprint/103498

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