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dc.contributor.author Gruninger, Robert J.
dc.contributor.author Thibault, John
dc.contributor.author Capeness, Michael J.
dc.contributor.author Till, Robert
dc.contributor.author Mosimann, Steven C.
dc.contributor.author Sockett, R. Elizabeth
dc.contributor.author Selinger, L. Brent
dc.contributor.author Lovering, Andrew L.
dc.date.accessioned 2016-12-21T18:08:15Z
dc.date.available 2016-12-21T18:08:15Z
dc.date.issued 2014
dc.identifier.citation Gruninger, R.J., Thibault, J., Capeness, M.J., Till, R., Mosimann, S. C., Sockett, R. E., ... & Lovering, A. L. (2014). 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. PLoS ONE, 9(4), e94403. doi:10.1371/journal.pone.0094403 en_US
dc.identifier.uri https://hdl.handle.net/10133/4752
dc.description Sherpa Romeo green journal: open access en_US
dc.description.abstract Bdellovibrio bacteriovorus is an unusual d-proteobacterium that invades and preys on other Gram-negative bacteria and is of potential interest as a whole cell therapeutic against pathogens of man, animals and crops. PTPs (protein tyrosine phosphatases) are an important class of enzyme involved in desphosphorylating a variety of substrates, often with implications in cell signaling. The B. bacteriovorus open reading frame Bd1204 is predicted to encode a PTP of unknown function. Bd1204 is both structurally and mechanistically related to the PTP-like phytase (PTPLP) class of enzymes and possesses a number of unique properties not observed in any other PTPLPs characterized to date. Bd1204 does not display catalytic activity against some common protein tyrosine phosphatase substrates but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate. The structure reveals that Bd1204 has the smallest and least electropositive active site of all characterized PTPLPs to date yet possesses a unique substrate specificity characterized by a strict preference for inositol hexakisphosphate. These two active site features are believed to be the most significant contributors to the specificity of phytate degrading enzymes. We speculate that Bd1204 may be involved in phosphate acquisition outside of prey. en_US
dc.language.iso en_US en_US
dc.publisher Public Library of Science en_US
dc.subject Bdellovibrio bacteriovorus en_US
dc.subject Protein tyrosine phosphatases en_US
dc.subject Phytase en_US
dc.subject Phosphatase en_US
dc.title 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 en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Biological Sciences en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution Lethbridge Research and Development Centre en_US
dc.publisher.institution University of Nottingham en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.institution University of Birmingham en_US


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