dc.contributor.advisor | Rehling, Peter Prof. Dr. | |
dc.contributor.author | Mühlhausen, Helene | |
dc.date.accessioned | 2014-12-05T09:58:29Z | |
dc.date.available | 2015-01-21T23:50:05Z | |
dc.date.issued | 2014-12-05 | |
dc.identifier.uri | http://hdl.handle.net/11858/00-1735-0000-0023-9953-2 | |
dc.identifier.uri | http://dx.doi.org/10.53846/goediss-4808 | |
dc.language.iso | deu | de |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/ | |
dc.subject.ddc | 610 | de |
dc.title | Untersuchungen zur molekularen Ursache der Multiplen Sulfatase-Defizienz: Reinigung, Funktions- und Strukturanalyse von varianten Proteinen des Formylglycin-generierenden Enzyms | de |
dc.type | doctoralThesis | de |
dc.title.translated | The molecular cause of multiple sulfatase deficiency: cleaning, functional and structural analysis of variant proteins of formylglycine-generating enzyme | de |
dc.contributor.referee | Schön, Margarete Prof. Dr. | |
dc.date.examination | 2015-01-14 | |
dc.description.abstracteng | The Multiple sulfatase deficiency (MSD) is an inherited metabolic disease caused by mutations in the SUMF1 gene. The encoded ER-located Cα-formylglycine-generating enzyme (FGE) catalyzes the activation of newly synthesized sulfatases by cotranslationally oxidizing a conserved cysteine residue to the Cα-formylglycine (FGly), the catalytically active amino acid residue of sulfatases. Some FGE mutants have already been characterized biochemically and initial assumptions about the relationship between genotype and phenotype of the disease are set up. Crystallization of the FGE-WT enabled - about the localization of the mutations in the model - to make predictions in terms of their expected damage. The confirmation of the suspected relationship between genotypic and phenotypic specificities effects, using the crystal structure model of a FGE mutant could not be achieved to date. Currently no data from completely purified FGE mutants exists. | de |
dc.contributor.coReferee | Zweckstetter, Markus Prof. Dr. | |
dc.subject.ger | Formylglycin generierendes Enzym | de |
dc.subject.ger | Multiple Sulfatase Defizienz | de |
dc.subject.ger | Aufreinigung | de |
dc.subject.ger | Mutanten | de |
dc.subject.ger | Affinitätschromatographie | de |
dc.subject.ger | Anionenaustauschchromatographie | de |
dc.subject.ger | Substratbindung | de |
dc.subject.ger | Kristallstruktur | de |
dc.subject.eng | FGE | de |
dc.subject.eng | mutants | de |
dc.subject.eng | purification | de |
dc.subject.eng | substrate binding | de |
dc.subject.eng | crystal structure | de |
dc.subject.eng | multiple sulfatase deficiency | de |
dc.subject.eng | formylglycine generating enzyme | de |
dc.subject.eng | affinity chromatography | de |
dc.subject.eng | variant proteins | de |
dc.identifier.urn | urn:nbn:de:gbv:7-11858/00-1735-0000-0023-9953-2-3 | |
dc.affiliation.institute | Medizinische Fakultät | de |
dc.subject.gokfull | Medizin (PPN619874732) | de |
dc.description.embargoed | 2015-01-21 | |
dc.identifier.ppn | 810737655 | |