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dc.contributor.authorNoble, Carteren_US
dc.date.accessioned2014-03-14T21:36:47Z
dc.date.available2014-03-14T21:36:47Z
dc.date.issued1975-12-05en_US
dc.identifier.otheretd-06022010-020209en_US
dc.identifier.urihttp://hdl.handle.net/10919/42841
dc.description.abstractStudies of the binding of coenzyme analogs to yeast 6-phosphogluconate dehydrogenase indicate that NADP binding to the enzyme results from selective interactions between regions of the coenzyme binding site and portions of the NADP molecule. These studies suggested the existence of coenzyme binding site regions which selectively interact with the adenosine, 2'-phosphate, and pyrophosphate moieties of NADP. The importance of the 2'-phosphate to coenzyme binding was indicated by enhanced binding of adenosine derivatives possessing this moiety when compared to adenosine derivatives not phosphorylated at this position. The better binding of the 2'-phosphorylated derivatives became more pronounced with increasing resemblance of the derivative to the NADP molecule, and NAD was not inhibitory up to 70 roM. These results substantiate the concept that interaction of the enzyme with the d2'-phosphate is a key factor in the specificity of yeast 6-phosphogluconate dehydrogenase for NADP. Structural analogs of the pyridinium portion of the NADP molecule, Nl-alkylnicotinamide chlorides, did not inhibit yeast 6-phosphogluconate dehydrogenase at concentrations normally required for selective interactions with dehydrogenases; however, enzyme activity was decreased at micellar concentrations of Nl-dodecylnicotinamide chloride. Investigations of the role and environment of the essential sulfhydryl group of this enzyme were also performed. N-alkylmaleimides (N-methyl - N-hexyl, inclusive) were shown to inactivate the enzyme, but without a chainlength effect. In the presence of 6-phosphogluconate, the enzyme was protected from N-ethylmaleimide inactivation and this protection was enhanced by the addition of NADPH or AADP.en_US
dc.format.mediumBTDen_US
dc.publisherVirginia Techen_US
dc.relation.haspartLD5655.V855_1975.N633.pdfen_US
dc.subjectCoenzymesen_US
dc.subject.lccLD5655.V855 1975.N633en_US
dc.titleStudies of the coenzyme binding site and essential sulfhydryl group of years 6-phosphogluconate dehydrogenase.en_US
dc.typeThesisen_US
dc.contributor.departmentBiochemistry and Nutritionen_US
dc.description.degreeMaster of Scienceen_US
thesis.degree.nameMaster of Scienceen_US
thesis.degree.levelmastersen_US
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen_US
thesis.degree.disciplineBiochemistry and Nutritionen_US
dc.contributor.committeechairAnderson, Bruce M.en_US
dc.contributor.committeememberBarnett, Lewis B.en_US
dc.contributor.committeememberBrown, Ross D. Jr.en_US
dc.contributor.committeememberHess, John L.en_US
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-06022010-020209/en_US
dc.date.sdate2010-06-02en_US
dc.date.rdate2010-06-02
dc.date.adate2010-06-02en_US


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