1. Nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene
- Author
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S Aiba, T Imanaka, and Ryoichi Nakajima
- Subjects
Bacillus amyloliquefaciens ,Bacillus ,Microbiology ,Geobacillus stearothermophilus ,chemistry.chemical_compound ,Species Specificity ,Amino Acid Sequence ,Amylase ,Cloning, Molecular ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,Methionine ,Base Sequence ,biology ,Protein primary structure ,Nucleic acid sequence ,biology.organism_classification ,Molecular biology ,Amino acid ,Molecular Weight ,Open reading frame ,chemistry ,Biochemistry ,Genes, Bacterial ,biology.protein ,alpha-Amylases ,Bacillus subtilis ,Research Article - 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.
- Published
- 1985
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