An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor-Reference-Cited by-同舟云学术

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

Published:2017 Issue:66 Volume:53 Page:9238-9241
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Belz Tyson¹²³⁴,Jin Yi⁵⁶⁷⁸⁹,Coines Joan¹⁰¹¹¹²¹³,Rovira Carme¹⁰¹¹¹²¹³¹⁴^ORCID,Davies Gideon J.⁵⁶⁷⁸⁹^ORCID,Williams Spencer J.¹²³⁴^ORCID

Affiliation:

1. School of Chemistry and Bio21 Molecular Science and Biotechnology Institute

2. University of Melbourne

3. Parkville

4. Australia

5. York Structural Biology Laboratory

6. Department of Chemistry

7. University of York

8. Heslington

9. UK

10. Departament de Química Inorgànica i Orgànica (Secció de Química Orgànica) & Institut de Química Teórica i Computacional (IQTCUB)

11. Universitat de Barcelona

12. 08028 Barcelona

13. Spain

14. Institució Catalana de Recerca i Estudis Avançats (ICREA)

Abstract

The non-hydrolyzable S-linked azasugar 1,6-α-mannobiosylthioisofagomine effects potent inhibition ofBacillus circulansfamily 76endo-1,6-α-mannanase through an atypical interaction involving the acid/base residue of the enzyme.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CC/C7CC04977C

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