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C‐Terminal domain of β‐1,3‐glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble β‐1,3‐glucan
Author(s) -
Yamamoto Mami,
Ezure Toru,
Watanabe Takeshi,
Tanaka Hirosato,
Aono Rikizo
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00881-3
Subject(s) - bacillus circulans , glucanase , chemistry , glucan , binding domain , bacillus (shape) , terminal (telecommunication) , domain (mathematical analysis) , biochemistry , microbiology and biotechnology , binding site , enzyme , biology , computer science , mathematics , telecommunications , mathematical analysis
The deduced amino acid sequences of 72‐kDa β‐1,3‐glucanase from Bacillus circulans WL‐12 (GlcA) and 91‐kDa enzyme from B. circulans IAM1165 (BglH) are highly homologous, except that the latter has an additional long C‐terminal region composed of 192 amino acid residues. Two mutant enzymes (BglH deprived of the C‐terminal region and GlcA with the C‐terminal region added) were constructed. The enzymes possessing the C‐terminal region bound more abundantly to pachyman (insoluble β‐1,3‐glucan) and Aspergillus oryzae cell wall than those not possessing the region. This indicates that the C‐terminal region participated in binding of the enzymes to insoluble β‐1,3‐glucan.