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Sequence homology between purple acid phosphatases and phosphoprotein phosphatases
Author(s) -
Vincent John B.,
Averill Bruce A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81389-6
Subject(s) - phosphatase , phosphoprotein , biochemistry , homology (biology) , chemistry , phosphorylation , biology , amino acid
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.