Toggle Main Menu Toggle Search

Open Access padlockePrints

The Newcastle University research output collection, currently available on ePrints, will shortly be moving to a new open repository platform, Figshare. To prepare for the data migration we have paused adding new content to ePrints, and will resume once the new repository is launched. During this time you will continue to have access to ePrints (but no new content will appear). We will share updates here when available.

Substrate distortion by β-mannanase: Snapshots of the Michaelis and covalent-intermediate complexes suggest a B2,5 conformation for the transition state

Lookup NU author(s): Emeritus Professor Harry Gilbert, Lorand Szabo

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

The conformational reaction pathway for β-mannosidases proposed here is distinct from that of glucosidases and cellulases. The proposal is based on substrate distortions along the reaction pathway of a β-mannosidase (see picture) that were revealed by X-ray crystallography and are close in conformational space to known β-mannosidase inhibitors.

Publication metadata

Author(s): Ducros VM-A, Zechel DL, Murshudov GN, Gilbert HJ, Szabo L, Stoll D, Withers SG, Davies GJ

Publication type: Article

Publication status: Published

Journal: Angewandte Chemie: International Edition

Year: 2002

Volume: 41

Issue: 15

Pages: 2824-2827

ISSN (print): 1433-7851

ISSN (electronic): 1521-3773

Publisher: Wiley - V C H Verlag GmbH & Co. KGaA

URL: http://dx.doi.org/10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G

DOI: 10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G

PubMed id: 12203498

Altmetrics

Altmetrics provided by Altmetric

Share