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Study of the structures and interactions of components in 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase complex
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Zhang, Xu. Study of the structures and interactions of components in 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase complex. Retrieved from https://doi.org/doi:10.7282/t3-p1yx-4b15

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TitleStudy of the structures and interactions of components in 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase complex
NameZhang, Xu (author); Jordan, Frank (chair); Szostak, Michal (internal member); Huskey, Phil (internal member); Farinas, Edgardo (outside member); Rutgers University; Graduate School - Newark
Date Created2021
Other Date2021-01 (degree)
Subject2-oxoadipate dehydrogenase complex, Chemistry
Extent1 online resource (xiv, 181 pages)
DescriptionMultienzyme complexes are assemblies containing several copies of one or several enzymes, and they generally carry out sequential catalytic transformations. Multienzyme complexes are essential for the living organisms, therefore deciphering how the components behave in isolation, but also how they interact with each other is critical for understanding the functions of enzyme complexes. The 2-oxoglutarate (OG) dehydrogenase complex (OGDHc) is a central enzyme in all forms of aerobic metabolism catalyzing the oxidative decarboxylation of OG, generating succinyl-CoA and NADH. The 2-oxoadipate dehydrogenase complex (OADHc) is a novel multienzyme complex functioning on the final degradation pathway of L-lysine, L-hydroxylysine and L-tryptophan. Many findings have suggested interesting similarities and differences between these two enzyme complexes, especially the unprecedented sharing of the dihydrolipamide acyltransferase component. In this thesis, hydrogen-deuterium exchange mass spectrometry (HDX-MS) and chemical cross-linking mass spectrometry (CL-MS), along with other biochemical methods and computational modeling, were employed to study the assembly of human OGDHc. In addition, studies were also carried out to investigate the functional and structural consequences of the mutation on the DHTKD1 gene encoding the 2-oxoadipate dehydrogenase. Moreover, HDX-MS was used to study the conformational changes induced by substitution of active center histidines in E. coli 1-deoxy-D-xylulose 5-phosphate (DXP) synthase, a thiamin diphosphate dependent enzyme.
NotePh.D.
NoteIncludes bibliographical references
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/t3-p1yx-4b15
LanguageEnglish
CollectionGraduate School - Newark Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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