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  • Title: Complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp.
    Author: Takegawa K, Mikami B, Iwahara S, Morita Y, Yamamoto K, Tochikura T.
    Journal: Eur J Biochem; 1991 Nov 15; 202(1):175-80. PubMed ID: 1935974.
    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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