Complete Nucleotide Sequence of a Gene Coding for Heat- and pH-Stable α-Amylase of Bacillus licheniformis: Comparison of the Amino Acid Sequences of Three Bacterial Liquefying α-Amylases Deduced from the DNA Sequences1
- 1 November 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 98 (5) , 1147-1156
- https://doi.org/10.1093/oxfordjournals.jbchem.a135381
Abstract
The gene coding for the heat-stable and pH-stable α-amylase of Bacillus liclieniformis 584 (ATCC 27811) was cloned in Escherichia coil and the nucleotide sequence of a DNA fragment of 1,948 base pairs containing the entire amylase gene was determined. As inferred from the DNA sequence, the B. licheniformis α-amylase had a signal peptide of 29 amino acid residues and the mature enzyme comprised 483 amino acid residues, giving a molecular weight of 55,200. The amino acid sequence of B. licheniformis α-amylase showed 65.4% and 80.3% homology with those of heat-stable Bacillus stearothermophilus α-amylase and relatively heat-unstable Bacillus amyloliquefaciens α-amylase, respectively. Nevertheless, several regions of the α-amylases appeared to be clearly distinct from one-another when their hydropathy profiles were compared.Keywords
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