Yamamoto M, Aono R, Horikoshi K
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Biosci Biotechnol Biochem. 1993 Sep;57(9):1518-25. doi: 10.1271/bbb.57.1518.
The nucleotides of a gene for the extracellular 87-kDa beta-1,3-glucanase of Bacillus circulans IAM1165 and its flanking regions were sequenced. The sequence showed an open reading frame for 877 amino acids, which corresponds to a precursor of the beta-1,3-glucanase. The coding region of 2631 bp is flanked by putative promoter and transcription terminator sequences. The signal peptide was considered to be consisted of 38 amino acids. The amino acid sequence of the mature enzyme composed of 839 amino acids showed high homology to that of the enzyme from B. circulans WL-12, although these enzymes are different in their sizes. A catalytic domain of the enzyme was estimated central region of the sequence on the basis of comparison of amono acid sequences of beta-1,3- or beta-1,3:1,4-glucanases. Properties of the periplasmic enzyme produced in Escherichia coli carrying the gene were identical with those of the extracellular enzyme produced by B. circulans IAM1165.
对环状芽孢杆菌IAM1165胞外87-kDaβ-1,3-葡聚糖酶基因及其侧翼区域的核苷酸进行了测序。该序列显示有一个877个氨基酸的开放阅读框，对应于β-1,3-葡聚糖酶的前体。2631 bp的编码区两侧是推定的启动子和转录终止子序列。信号肽被认为由38个氨基酸组成。由839个氨基酸组成的成熟酶的氨基酸序列与环状芽孢杆菌WL-12的酶具有高度同源性，尽管这些酶的大小不同。基于β-1,3-或β-1,3:1,4-葡聚糖酶氨基酸序列的比较，估计该酶的催化结构域位于序列的中央区域。携带该基因的大肠杆菌中产生的周质酶的性质与环状芽孢杆菌IAM1165产生的胞外酶的性质相同。
