Complete amino acid sequence of endo‐β‐N‐acetylglucosaminidase from Flavobacterium sp.
Open Access
- 1 November 1991
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 202 (1) , 175-180
- https://doi.org/10.1111/j.1432-1033.1991.tb16359.x
Abstract
The complete amino acid sequence of endo-β-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-β-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-β-N-acetylglucosaminidase and chitinases from Bacillus circulans, Serratia marcescens and Phaseolus vulgaris.Keywords
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