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), 1169-1180. (doi:10.1016/S0969-2126(94)00119-7). (PMID:7704527).

Download

[img] PDF (Original Article) - Version of Record
Restricted to System admin

Download (1574Kb)

Description/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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/S0969-2126(94)00119-7
ISSNs: 0969-2126 (print)
Related URLs:
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Natural and Environmental Sciences > Biological Sciences
ePrint ID: 200661
Date Deposited: 02 Nov 2011 14:39
Last Modified: 06 Aug 2015 03:04
URI: http://eprints.soton.ac.uk/id/eprint/200661

Actions (login required)

View Item View Item

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