Structural and Biochemical Analysis of a Unique Phosphatase from Bdellovibrio bacteriovorus Reveals Its Structural and Functional Relationship with the Protein Tyrosine Phosphatase Class of Phytase

摘要: Bdellovibrio bacteriovorus is an unusual δ-proteobacterium that invades and preys on other Gram-negative bacteria of potential interest as a whole cell therapeutic against pathogens man, animals crops. PTPs (protein tyrosine phosphatases) are important class enzyme involved in desphosphorylating variety substrates, often with implications signaling. The B. open reading frame Bd1204 predicted to encode PTP unknown function. both structurally mechanistically related the PTP-like phytase (PTPLP) enzymes possesses number unique properties not observed any PTPLPs characterized date. does display catalytic activity some common protein phosphatase substrates but highly specific for hydrolysis phosphomonoester bonds inositol hexakisphosphate. structure reveals has smallest least electropositive active site all date yet substrate specificity by strict preference These two features believed be most significant contributors phytate degrading enzymes. We speculate may phosphate acquisition outside prey.