Nakajima R, Imanaka T, Aiba S
J Bacteriol. 1985 Jul;163(1):401-6. doi: 10.1128/jb.163.1.401-406.1985.
The nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene and its flanking regions was determined. An open reading frame was found, comprising a total of 1,647 base pairs (549 amino acids) and starting from a GUG codon as methionine. It was shown by NH2-terminal amino acid sequence analysis that the extracellular amylase consisted of 515 amino acid residues, which corresponded to a molecular weight of 58,779. Thus the NH2-terminal portion of the gene encodes 34 amino acid residues as a signal peptide. The amino acid sequence deduced from the alpha-amylase gene was fairly homologous (61%) with that of another thermostable amylase from Bacillus amyloliquefaciens.
测定了嗜热脂肪芽孢杆菌α-淀粉酶基因及其侧翼区域的核苷酸序列。发现了一个开放阅读框,其总共包含1647个碱基对(549个氨基酸),并从作为甲硫氨酸的GUG密码子开始。通过氨基末端氨基酸序列分析表明,细胞外淀粉酶由515个氨基酸残基组成,其分子量为58779。因此,该基因的氨基末端部分编码34个氨基酸残基作为信号肽。从α-淀粉酶基因推导的氨基酸序列与解淀粉芽孢杆菌的另一种耐热淀粉酶的氨基酸序列具有相当高的同源性(61%)。