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).
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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 |
|---|---|
| ISSNs: | 0969-2126 (print) |
| Related URLs: | |
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Natural and Environmental Sciences > Biological Sciences |
| Item ID: | 200661 |
| Date Deposited: | 02 Nov 2011 14:39 |
| Last Modified: | 08 Jun 2012 13:23 |
| Contributors: | Perrakis, A (Author) Tews, I (Author) Dauter, Z (Author) Oppenheim, A B (Author) Chet, I (Author) Wilson, K S (Author) Vorgias, C E (Author) |
| Date: | 15 December 1994 |
| Status: | Published |
| URI: | http://eprints.soton.ac.uk/id/eprint/200661 |
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