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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

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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

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