The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products.
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ABSTRACT:
SUBMITTER: Kafetzopoulos D
PROVIDER: S-EPMC47276 | biostudies-other | 1993 Sep
REPOSITORIES: biostudies-other
Publications
The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products.
Kafetzopoulos D D Thireos G G Vournakis J N JN Bouriotis V V
Proceedings of the National Academy of Sciences of the United States of America 19930901 17
Chitin deacetylase (EC 3.5.1.41) hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. A cDNA to the Mucor rouxii mRNA encoding chitin deacetylase was isolated, characterized, and sequenced. Protein sequence comparisons revealed significant similarities of the fungal chitin deacetylase to rhizobial nodB proteins and to an uncharacterized protein encoded by a Bacillus stearothermophilus open reading frame. These data suggest the functional homology of these evolutionaril ...[more]
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