Abstract
The α-amylase family constitutes the clan GH-H consisting of the three glycoside hydrolase (GH) families GH13, GH70 and GH77. The entire α-amylase family counts ~5,000 known amino acid sequences that exhibit almost 30 different enzyme specificities. Besides the other basic characteristics of the family, such as hydrolysis and/or transglycosylation of several α-glucosidic linkages and the employment of the catalytic triad in the enzymatic reaction, the α-amylase family members should contain from four up-to seven conserved sequence regions. These regions may be considered to be the ‘’ of the individual enzyme specificities and/or taxonomic sources. This article is therefore focused on showing the importance of the conserved sequence regions as the sequence fingerprints in special cases of: (i) the GH13 α-amylases from plants and archaeons; (ii) the oligo-1,6-glucosidase and neopullulanase GH13 subfamilies; and (iii) the unique GH77 amylomaltases from borreliae.
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