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Magnesium-dependent phosphatase 1 (MDP1) is a eukaryotic magnesium-dependent acid phosphatase and an atypical member of the haloacid dehalogenase (HAD) superfamily[1][2][3][4][6]. It preferentially dephosphorylates phosphotyrosine residues, although it can also act on certain phosphosugar substrates such as ribose-5-phosphate and fructosamine-6-phosphate[4][5][6]. Unlike canonical protein tyrosine phosphatases, MDP1 shows low sequence homology with other known phosphatase families, and its structure lacks a "cap" domain typically present in related enzymes, resulting in an "open" active site suitable for large substrates[1][2][3]. MDP1 is not a major established drug target and is not directly linked to common diseases, but it may play a role in cellular phosphate homeostasis and glycation repair. The enzyme is magnesium-dependent and is inhibited by vanadate and fluoride, but not by other common phosphatase inhibitors[4][5][6].
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