Itkor P, Tsukagoshi N, Udaka S
Faculty of Agriculture, Nagoya University, Japan.
Biochem Biophys Res Commun. 1990 Jan 30;166(2):630-6. doi: 10.1016/0006-291x(90)90855-h.
The gene coding for the raw-starch-digesting amylase from Bacillus sp. B1018 was cloned into Escherichia coli, and its nucleotide sequence was determined. Starting at an ATG codon, there was an open reading frame composed of 2139 bp (713 amino acids). The NH2-terminal portion encoded a 27 amino acid-long signal peptide. S1 mapping revealed the presence of a typical promoter region upstream from the transcription initiation site. The deduced amino acid sequence of the extracellular mature enzyme was very similar to those of cyclodextrin glucanotransferases (CGTases), especially that of alkalophilic Bacillus sp. 1011 (87% homology). In fact, the B1018 amylase showed CGTase activity. The COOH-terminal portion of the B1018 amylase shows significant homology with other raw-starch-digesting enzymes.
将来自芽孢杆菌属B1018的可消化生淀粉的淀粉酶编码基因克隆到大肠杆菌中,并测定了其核苷酸序列。从一个ATG密码子开始,有一个由2139 bp(713个氨基酸)组成的开放阅读框。NH2末端部分编码一个27个氨基酸长的信号肽。S1作图显示在转录起始位点上游存在一个典型的启动子区域。推导的细胞外成熟酶的氨基酸序列与环糊精葡聚糖转移酶(CGTases)非常相似,尤其是嗜碱芽孢杆菌属1011的环糊精葡聚糖转移酶(同源性为87%)。实际上,B1018淀粉酶表现出CGTase活性。B1018淀粉酶的COOH末端部分与其他可消化生淀粉的酶具有显著的同源性。