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dc.contributor.authorWaterman, Mattheweng
dc.contributor.authorGriffith, S. C.eng
dc.contributor.authorBeamer, Lesa J. (Lesa Jean)eng
dc.contributor.corporatenameUniversity of Missouri-Columbia. Office of Undergraduate Researcheng
dc.contributor.meetingnameSummer Undergraduate Research and Creative Achievements Forum (2005 : University of Missouri--Columbia)eng
dc.date2005eng
dc.date.issued2005eng
dc.descriptionAbstract only availableeng
dc.description.abstractPhosphoacetylglucosamine mutase (PAGM) is a human enzyme that is the key to the formation of the essential metabolite UDP-N-acetylglucosamine. Bacterial phosphoglucomutase (PGM) from Acetobacter xylinum catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate. PAGM and PGM are members of the alpha-D-phosphohexomutase superfamily which all catalyze intramolecular phosphoryl transfer on sugar substrates. These two analogs are similar in their mechanism, but dissimilar in their substrate specificity, not only to each other, but also to other well characterized (structurally and mechanistically) members of their superfamily. Protein expression and purification techniques were used to attempt to produce crystals to determine the three dimensional structures of human PAGM and bacterial PGM by X-ray diffraction in order to clarify the structural explanation for substrate specificity within the alpha-D-phosphohexomutase superfamily.eng
dc.description.sponsorshipLife Sciences Undergraduate Research Opportunity Programeng
dc.identifier.urihttp://hdl.handle.net/10355/2227eng
dc.languageen_USeng
dc.publisherUniversity of Missouri--Columbia. Office of Undergraduate Researcheng
dc.relation.ispartof2005 Summer Undergraduate Research and Creative Achievements Forum (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Office of Undergraduate Research. Undergraduate Research and Creative Achievements Forumeng
dc.source.urihttp://undergradresearch.missouri.edu/forums-conferences/abstracts/abstract-detail.php?abstractid=eng
dc.subjectalpha-D-phosphohexomutase superfamilyeng
dc.subjectsubstrate specificityeng
dc.titleStructural basis for substrate specificity of the alpha-D-phosphohexomutase superfamilyeng
dc.typePresentationeng


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