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.
|Number of pages||6|
|Journal||European Journal of Biochemistry|
|Publication status||Published - Jan 1 1991|
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