Complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp |
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| Authors: | K Takegawa B Mikami S Iwahara Y Morita K Yamamoto T Tochikura |
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| Affiliation: | Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan. |
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| Abstract: | The complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp. has been determined by analysis of peptides after cleavage with lysyl endopeptidase, pepsin and chymotrypsin. The protein consists of a single polypeptide chain consisting of 267 amino acid residues and a molecular mass of 27972 Da. The sequence of Flavobacterium endo-beta-N-acetylglucosaminidase is very close to that of the Streptomyces enzyme (endo-H), having 60% similarity and very similar hydropathy profiles. Similarities were also found between Flavobacterium endo-beta-N-acetylglucosaminidase and chitinases from Bacillus circulans, Serratia marcescens and Phaseolus vulgaris. |
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