| Literature DB >> 3924897 |
R Nakajima, T Imanaka, S Aiba.
Abstract
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.Entities:
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Year: 1985 PMID: 3924897 PMCID: PMC219130 DOI: 10.1128/jb.163.1.401-406.1985
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490