| Literature DB >> 1935974 |
K Takegawa1, B Mikami, S Iwahara, Y Morita, K Yamamoto, T Tochikura.
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.Entities:
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Year: 1991 PMID: 1935974 DOI: 10.1111/j.1432-1033.1991.tb16359.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956