Issue 18, 2009

Structure of the Michaelis complex of β-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis

Abstract

The Michaelis complex of the β-mannosidase Man2A shows distortion to a 1S5 conformation adding to the growing body of evidence supporting catalysis through a boat conformation.

Graphical abstract: Structure of the Michaelis complex of β-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis

Supplementary files

Article information

Article type
Communication
Submitted
03 Feb 2009
Accepted
12 Mar 2009
First published
06 Apr 2009

Chem. Commun., 2009, 2484-2486

Structure of the Michaelis complex of β-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis

W. A. Offen, D. L. Zechel, S. G. Withers, H. J. Gilbert and G. J. Davies, Chem. Commun., 2009, 2484 DOI: 10.1039/B902240F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements