The University of Southampton
University of Southampton Institutional Repository

Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease

Tews, Ivo, Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S. and Vorgias, C. E. (1996) Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease Nature Structural Biology, 3, (7), pp. 638-648. (PMID:8673609).

Record type: Article


Chitin, the second most abundant polysaccharide on earth, is degraded by chitinases and chitobiases. The structure of Serratia marcescens chitobiase has been refined at 1.9 A resolution. The mature protein is folded into four domains and its active site is situated at the C-terminal end of the central (beta alpha)8-barrel. Based on the structure of the complex with the substrate disaccharide chitobiose, we propose an acid-base reaction mechanism, in which only one protein carboxylate acts as catalytic acid, while the nucleophile is the polar acetamido group of the sugar in a substrate-assisted reaction. The structural data lead to the hypothesis that the reaction proceeds with retention of anomeric configuration. The structure allows us to model the catalytic domain of the homologous hexosaminidases to give a structural rationale to pathogenic mutations that underlie Tay-Sachs and Sandhoff disease.

PDF NatStructBiol_3-638.pdf - Version of Record
Restricted to Repository staff only
Download (1MB)

More information

Published date: July 1996
Organisations: Centre for Biological Sciences


Local EPrints ID: 200659
ISSN: 1072-8368
PURE UUID: ff1c374a-6db9-4d1a-a754-c9988dc6f523
ORCID for Ivo Tews: ORCID iD

Catalogue record

Date deposited: 02 Nov 2011 14:43
Last modified: 18 Jul 2017 11:14

Export record


Author: Ivo Tews ORCID iD
Author: A. Perrakis
Author: A. Oppenheim
Author: Z. Dauter
Author: K. S. Wilson
Author: C. E. Vorgias

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.