Complete amino acid sequence of endo‐β‐N‐acetylglucosaminidase from Flavobacterium sp.

Kaoru TAKEGAWA, Bunzo MIKAMI, Shojiro IWAHARA, Yuhei MORITA, Kenji YAMAMOTO, Tatsurokuro TOCHIKURA

Research output: Contribution to journalArticle

19 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)175-180
Number of pages6
JournalEuropean Journal of Biochemistry
Volume202
Issue number1
DOIs
Publication statusPublished - Jan 1 1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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