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Crystal structure of a bacterial chitinase at 2.3 A resolution

Perrakis, A, Tews, I, Dauter, Z, Oppenheim, A B, Chet, I, Wilson, K S and Vorgias, C E (1994) Crystal structure of a bacterial chitinase at 2.3 A resolution Structure, 2, (12), pp. 1169-1180. (doi:10.1016/S0969-2126(94)00119-7). (PMID:7704527).

Record type: Article

Abstract

The reaction mechanism seems to be similar to that of lysozyme and most other glycosylhydrolases, i.e. general acid-base catalysis. The role of the amino-terminal domain could not be identified, but it has similarities to the fibronectin III domain. This domain may possibly facilitate the interaction of chitinase A with chitin.

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Published date: 15 December 1994
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 200661
URI: http://eprints.soton.ac.uk/id/eprint/200661
ISSN: 0969-2126
PURE UUID: 015b5b99-f308-490b-96cb-192fbf698257
ORCID for I Tews: ORCID iD orcid.org/0000-0002-4704-1139

Catalogue record

Date deposited: 02 Nov 2011 14:39
Last modified: 18 Jul 2017 11:14

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Contributors

Author: A Perrakis
Author: I Tews ORCID iD
Author: Z Dauter
Author: A B Oppenheim
Author: I Chet
Author: K S Wilson
Author: C E Vorgias

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