title: Sequence homology between purple acid phosphatases and phosphoprotein phosphatases. Are phosphoprotein phosphatases metalloproteins containing oxide-bridged dinuclear metal centers?
abstract: The amino acid sequences of mammalian purple acid phosphatases and phosphoprotein phosphatases are shown to possess regions of significant homology. The conserved residues contain a high percentage of possible metal-binding residues. The phosphoprotein phosphatases 1, 2A and 2B are proposed to be iron-zinc metalloenzymes with active sites isostructural (or nearly so) with those of the purple phosphatases.
authors.affiliation: University of Virginia, Department of Chemistry, Charlottesville 22901.
authors.forename: J B
authors.initials: JB
authors.lastname: Vincent
authors.forename: B A
authors.initials: BA
authors.lastname: Averill
mesh_terms: D000135:Acid Phosphatase; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008667:Metalloproteins; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
chemical_list: D008667:Metalloproteins; D010749:Phosphoprotein Phosphatases; D000135:Acid Phosphatase