Summary
A comparison was made of the amino acid sequences of 11 different α-amylases. The 6 animal α-amylases tested were found to be highly homologous (about 80 to 90%, depending on the species compared). Amino acid sequence of Bacillus stearothermophilus α-amylase was fairly homologous (about 60%) with that of a thermostable α-amylase from Bacillus amyloliquefaciens. Homology was least among the thermolabile amylases from Bacillus subtilis, Aspergillus oryzae, plants and animals. Nevertheless, four highly homologous regions were found in the amino acid sequences of all the enzymes, despite their widely different origins. It was inferred that these four homologous regions were likely to be the active and/or substrate-binding sites.
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Nakajima, R., Imanaka, T. & Aiba, S. Comparison of amino acid sequences of eleven different α-amylases. Appl Microbiol Biotechnol 23, 355–360 (1986). https://doi.org/10.1007/BF00257032
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DOI: https://doi.org/10.1007/BF00257032