Structure and mechanism of protein tyrosine phosphatase-like phytases

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dc.contributor.authorGruninger, Robert J.
dc.contributor.authorUniversity of Lethbridge. Faculty of Arts and Science
dc.contributor.supervisorMosimann, Steven C.
dc.contributor.supervisorSelinger, L. Brent
dc.date.accessioned2011-07-08T19:43:16Z
dc.date.available2011-07-08T19:43:16Z
dc.date.issued2009
dc.degree.disciplineChemistry & Biochemistry
dc.degree.fieldArts and Science
dc.degree.levelDoctor of Philosophy
dc.degree.levelPhD
dc.degree.subfieldSciences
dc.descriptionxix, 148 leaves : ill. (some col.) ; 29 cmen_US
dc.description.abstractThe structure and mechanism of the Protein Tyrosine Phosphatase-like Phytases (PTPLPs) from Selenomonas ruminantium (PhyAsr) and Mitsuokella multacida (PhyAmm) were investigated using a combination of enzyme kinetics, site-directed mutagenesis, and X-ray crystallography. I show that PTPLPs use a classical protein tyrosine phosphatase catalytic mechanism and adopt a core PTP fold. Several unique structural features of PTPLPs confer specificity for inositol phosphates. The effect of ionic strength and oxidation on the kinetics and structure of PTPLPs was investigated. The structural consequences of reversible and irreversible oxidation on PTPLPs and PTPs are compared and discussed. We determine the structural basis of substrate specificity in PTPLPs and propose a novel reaction mechanism for the hydrolysis of inositol polyphosphates by PTPLPs. Finally, the structure and function of a unique tandemly repeated phytase has been determined. We show that the active sites of the tandem repeat possess significantly different specificities for inositol polyphosphate.en_US
dc.identifier.urihttps://hdl.handle.net/10133/2473
dc.language.isoen_USen_US
dc.librarysymbolALU
dc.organizationUniversity of Lethbridge
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009en_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.relation.ispartofseriesThesis (University of Lethbridge. Faculty of Arts and Science)en_US
dc.subjectPhytasesen_US
dc.subjectProtein-tyrosine kinaseen_US
dc.subjectPhosphorylationen_US
dc.subjectDissertations, Academicen_US
dc.titleStructure and mechanism of protein tyrosine phosphatase-like phytasesen_US
dc.typeThesisen_US
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