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J. Bacteriol., 09 1996, 5065-5070, Vol 178, No. 17
T Ohno, S Armand, T Hata, N Nikaidou, B Henrissat, M Mitsutomi and T Watanabe
The specificity of chitinase C-1 of Streptomyces griseus HUT 6037 for the
hydrolysis of the beta-1,4-glycosidic linkages in partially acetylated
chitosan is different from that of other microbial chitinases. In order to
study the primary structure of this unique chitinase, the chiC gene
specifying chitinase C-1 was cloned and its nucleotide sequence was
determined. The gene encodes a polypeptide of 294 amino acids with a
calculated size of 31.4 kDa. Comparison of the amino acid sequence of the
deduced polypeptide with that of other proteins revealed a C-terminal
catalytic domain displaying considerable sequence similarity to the
catalytic domain of plant class I, II, and IV chitinases which form
glycosyl hydrolase family 19. The N-terminal domain of the deduced
polypeptide exhibits sequence similarity to substrate-binding domains of
several microbial chitinases and cellulases but not to the chitin-binding
domains of plant chitinases. The previously purified chitinase C-1 from S.
griseus is suggested to be generated by proteolytic removal of the
N-terminal chitin-binding domain and corresponds to the catalytic domain of
the chitinase encoded by the chiC gene. High-performance liquid
chromatography analysis of the hydrolysis products from N-acetyl
chitotetraose revealed that chitinase C-1 catalyzes hydrolysis of the
glycosidic bond with inversion of the anomeric configuration, in agreement
with the previously reported inverting mechanism of plant class I
chitinases. This is the first report of a family 19 chitinase found in an
organism other than higher plants.
Copyright © 1996, American Society for Microbiology
A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Japan.
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