Mowbray, Sherry
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
Genomic DNA for a class IV chitinase was cloned from yam (Dioscorea opposita Thunb) leaves and sequenced. The deduced amino acid sequence shows 50 to 59% identity to class IV chitinases from other plants. The yam chitinase, however, has an additional sequence of 8 amino acids (a C-terminal extension) following the cysteine that was reported as the last amino acid for other class IV chitinases; this extension is perhaps involved in subcellular localization. A homology model based on the structure of a class II chitinase from barley was used as an aid to interpreting the available data. The analysis suggests that the class IV enzyme recognizes an even shorter segment of the substrate than class I or II enzymes. This observation might help to explain why class IV enzymes are better suited to attack against pathogen cell walls
Published in
Bioscience, Biotechnology and Biochemistry
2004, volume: 68, number: 7, pages: 1508-1517
Publisher: JAPAN SOC BIOSCI BIOTECHN AGROCHEM
SLU Authors
Ubhayasekera, Wimal
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
UKÄ Subject classification
Forest Science
Publication identifier
- DOI: https://doi.org/10.1271/bbb.68.1508
Permanent link to this page (URI)
https://res.slu.se/id/publ/4787