On origin and evolution of carbonic anhydrase isozymes: A phylogenetic analysis from whole-enzyme to active site |
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Institution: | 1. Department of Chemistry, University of California Berkeley, Berkeley, CA 94720, USA;2. Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA;3. Energy Biosciences Institute, University of California Berkeley, Berkeley, CA 94720, USA |
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Abstract: | Genetic evolution of carbonic anhydrase enzyme provides an interesting instance of functional similarity in spite of structural diversity of the members of a given family of enzymes. Phylogenetic analysis of α-, β- and γ-carbonic anhydrase was carried out to determine the evolutionary relationships among various members of the family with the enzyme marking its presence in a wide range of cellular and chromosomal locations. The presence of more than one class of enzymes in a particular organism was revealed by phylogenetic time tree. The evolutionary relationships among the members of animal, plant and microbial kingdom were developed. The study revises a long-established notion of kingdom-specificity of the different classes of carbonic anhydrases and provides a new version of the presence of multiple classes of carbonic anhydrases in a single organism and the presence of a given class of carbonic anhydrase across different kingdoms. |
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Keywords: | Kingdom-specificity Active site Sequence alignment Carbonic anhydrases Biological function Structural similarity |
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