环状芽孢杆菌IAM1165中β-1,3-葡聚糖酶H的C末端结构域在与不溶性β-1,3-葡聚糖结合中起作用。
C-terminal domain of beta-1,3-glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble beta-1,3-glucan.
作者信息
Yamamoto M, Ezure T, Watanabe T, Tanaka H, Aono R
机构信息
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
出版信息
FEBS Lett. 1998 Aug 14;433(1-2):41-3. doi: 10.1016/s0014-5793(98)00881-3.
The deduced amino acid sequences of 72-kDa beta-1,3-glucanase from Bacillus circulans WL-12 (GIcA) 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 (BgIH deprived of the C-terminal region and GIcA with the C-terminal region added) were constructed. The enzymes possessing the C-terminal region bound more abundantly to pachyman (insoluble beta-1,3-glucan) and A.spergillus oryzae cell wall than those not possessing the region. This indicates that the C-terminal region participated in binding of the enzymes to insoluble beta-1,3-glucan.
环状芽孢杆菌WL - 12（GIcA）的72 kDaβ-1,3 - 葡聚糖酶和环状芽孢杆菌IAM1165（BglH）的91 kDa酶推导的氨基酸序列高度同源，只是后者有一个由192个氨基酸残基组成的额外的长C末端区域。构建了两种突变酶（缺失C末端区域的BgIH和添加了C末端区域的GIcA）。与不具有该区域的酶相比，具有C末端区域的酶与茯苓聚糖（不溶性β-1,3 - 葡聚糖）和米曲霉细胞壁的结合更丰富。这表明C末端区域参与了酶与不溶性β-1,3 - 葡聚糖的结合。
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