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P-type ATPase diversity and evolution: the origins of ouabain sensitivity and subunit assembly.
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2001
Year
Novel IsoformsMolecular BiologyP-type AtpasesPhylogenetic AnalysisBiosynthesisPhylogeneticsBiochemical TaxonomyBioenergeticsStructure-function Enzyme KineticsMolecular PhysiologyBiochemistryP-type Atpase SubunitsP-type Atpase DiversityStructural BiologyOuabain SensitivityProtein PhosphorylationBiologyCellular EnzymologyNatural SciencesPhysiologyProtein EvolutionMedicineSubunit Assembly
Molecular aspects of the diversity of P-type ATPases are explored in this review. From the substrate specificities among different ATPase molecules, the existence of isoforms within a single class of pump becomes evident and it is now recognized as a universal phenomenon. From the phylogenetic analyses using a vast collection of the deduced amino acid sequences for the P-type ATPase subunits, it also becomes evident that the divergence of substrate-specificity occurred early in the evolution and has been conserved ever since. Further extensive analyses identify a set of novel isoforms that retain an ancestral characteristic of the Na+/K+-(H+/K+-)ATPases in invertebrates.