α-Amylases hydrolyze α- 1,4-glycosidic bonds during assimilation of biological macromolecules. The amino
acid sequences of these enzymes in thousands of diverse organisms are known and the 3D structures of several proteins
have been solved. The 3D structure analysis of these universal enzymes from diverse organisms has been studied by the
generation of phylogenetic trees and structure based sequence analysis to generate a metric for the degree of conservation
that is responsible for individual speciation. Greater similarities are observed between reference NCBI tree and structure
based phylogenetic tree compared to sequence based phylogenetic tree indicating that structures truly represent the functional
aspects of proteins than from the sequence information alone. We report differences in the profile specific conserved
and insertion/deletion regions, factors responsible for the Ca2+ and Cl- ion binding and the disulfide connectivity
pattern that discriminate the enzymes over evolution.
Keywords: α-Amylase, calcium ion binding, chloride ion binding, disulfide bond, phylogenetic trees, protein sequence analysis,
3D structure analysis.
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