Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates

Simple item page
dc.contributor.authorVan Herk, Peter
dc.contributor.supervisorMosimann, Steven C.
dc.date.accessioned2015-01-30T18:32:33Z
dc.date.available2015-01-30T18:32:33Z
dc.date.issued2014
dc.degree.levelMastersen_US
dc.degree.levelMasters
dc.description.abstractProtein tyrosine phosphatase-like myo-inositol phosphatases (PTPLPs) remove phosphoryl groups from phosphorylated myo-inositols (IPs) via largely ordered pathways. To understand the substrate specificity of this enzyme family, a simple method has been developed to produce pure, less-phosphorylated IPs that involves the hydrolysis of InsP6. The less-phosphorylated IPs were utilized to characterize the binding affinity and apparent kinetic parameters of a representative PTPLP. Finally, the structure of a PTPLP from Desulfovibrio magneticus and its hydrolytic pathway were determined. Main-chain conformational differences within the substrate binding site give rise to its unique InsP6 dephosphorylation pathway and has allowed for the identification of structural determinants that give rise to its specificity for the C4 phosphoryl of Ins(1,2,4,5,6)P5. Understanding how the number and nature of contacts in each of the phosphoryl binding sites control specificity will ultimately allow us to engineer PTPLPs with any desired substrate specificity.en_US
dc.description.sponsorshipUniversity of Lethbridge, NSERCen_US
dc.identifier.urihttps://hdl.handle.net/10133/3638
dc.language.isoen_CAen_US
dc.proquest.subject0487en_US
dc.proquest.subject0786en_US
dc.proquest.subject0307en_US
dc.proquestyesYesen_US
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistryen_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.subjectCrystallographyen_US
dc.subjectBiochemistryen_US
dc.subjectEnzymeen_US
dc.subjectPhosphataseen_US
dc.subjectMyo-Inositolen_US
dc.subjectPTPLPen_US
dc.subjectFluorescence Spectroscopyen_US
dc.subjectKineticen_US
dc.subjectSubstrate Specificityen_US
dc.subjectPhysical Biochemistryen_US
dc.titleSpecificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphatesen_US
dc.typeThesisen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Van_Herk_Peter_MSC_2014.pdf
Size:
34.4 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.63 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Arts and Science, Faculty of
University of Lethbridge Theses