Proceedings of the National Academy of Sciences of the United States of America
Department of Biological Sciences
Chitin deacetylase (EC 126.96.36.199) 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 evolutionarily distant proteins. NodB is a chitooligosaccharide deacetylase essential for the biosynthesis of the bacterial nodulation signals, termed Nod factors. The observed similarity of chitin deacetylase to the B. stearothermophilus gene product suggests that this gene encodes a polysaccharide deacetylase.
Kafetzopoulos D, Thireos G, Vournakis JN, Bouriotis V. The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products. Proc Natl Acad Sci U S A. 1993;90(17):8005-8008. doi:10.1073/pnas.90.17.8005
Dartmouth Digital Commons Citation
Kafetzopoulos, Dimitris; Thireos, George; Vournakis, John N.; and Bouriotis, Vassilis, "The Primary Structure of a Fungal Chitin Deacetylase Reveals the Function for Two Bacterial Gene Products." (1993). Open Dartmouth: Published works by Dartmouth faculty. 1670.