| Literature DB >> 8168626 |
S Armand1, H Tomita, A Heyraud, C Gey, T Watanabe, B Henrissat.
Abstract
Chitinases A1 and D were purified from the periplasmic proteins produced by Escherichia coli HB101 harbouring recombinant plasmids carrying respectively the chiA and chiD genes of Bacillus circulans WL-12. HPLC analysis indicated that during the hydrolysis of chitotriose, both chitinases initially produce N-acetylglucosamine and only one anomer of chitobiose. 1H NMR spectroscopy of the hydrolysis of chitotetraitol showed that this anomer corresponds to beta-chitobiose, demonstrating that chitinases A1 and D act by a molecular mechanism that retains the anomeric configuration. This mechanism is similar to that of lysozymes although both chitinases belong to a family of proteins sharing no demonstrable amino acid sequence similarity with lysozymes.Entities:
Mesh:
Substances:
Year: 1994 PMID: 8168626 DOI: 10.1016/0014-5793(94)80314-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124