Hara Yukari, Hinoki Yumi, Shimoi Hitoshi, Ito Kiyoshi
Department of Molecular Biotechnology, Hiroshima University, Higashi-Hiroshima, Japan.
Biosci Biotechnol Biochem. 2003 Sep;67(9):2010-3. doi: 10.1271/bbb.67.2010.
Three endoglucanase genes (cel5A, cel5B, and cel61A) were cloned from an industrial fungus, Aspergillus kawachii. Yeasts transformed with these cDNAs showed endoglucanase activity in medium. Cel5A and Cel61A contained a type 1 cellulose-binding domain (CBD1) at the C-terminus of the enzyme. The putative catalytic regions of Cel5A and Cel5B showed homology with various endoglucanases belonging glycosyl hydrolase family 5 (GH5). Cel5B showed high homology with Cel5A in catalytic region, but it lacked CBD1 and linker. The cel5A contained four introns, whereas cel5B contained five introns. The putative catalytic region of Cel61A showed homology with enzymes belonging to GH61. The cel61A contained no introns.
从工业真菌泡盛曲霉中克隆出三个内切葡聚糖酶基因（cel5A、cel5B和cel61A）。用这些cDNA转化的酵母在培养基中显示出内切葡聚糖酶活性。Cel5A和Cel61A在酶的C末端含有一个1型纤维素结合结构域（CBD1）。Cel5A和Cel5B的推定催化区域与属于糖基水解酶家族5（GH5）的各种内切葡聚糖酶具有同源性。Cel5B在催化区域与Cel5A具有高度同源性，但它缺乏CBD1和连接子。cel5A包含四个内含子，而cel5B包含五个内含子。Cel61A的推定催化区域与属于GH61的酶具有同源性。cel61A不包含内含子。
