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

Belz, Tyson, Jin, Yi, 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: 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: 20 Jul 2018 20:04
URI: http://orca.cf.ac.uk/id/eprint/103498

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