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Study of the structures and interactions of components in 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase complex
Descriptive
TitleInfo
Title
Study of the structures and interactions of components in 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase complex
Name
(type = personal)
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Zhang
NamePart
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Xu
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Xu Zhang
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author
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Jordan
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Frank
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Frank Jordan
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Advisory Committee
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chair
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Szostak
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Michal
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Michal Szostak
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Advisory Committee
Role
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internal member
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(type = personal)
NamePart
(type = family)
Huskey
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(type = given)
Phil
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Phil Huskey
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Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Farinas
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(type = given)
Edgardo
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Edgardo Farinas
Affiliation
Advisory Committee
Role
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outside member
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NamePart
Rutgers University
Role
RoleTerm
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degree grantor
Name
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NamePart
Graduate School - Newark
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school
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Text
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theses
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ETD doctoral
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2021
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2021-01
Language
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English
Abstract
Multienzyme 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.
Subject
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Topic
2-oxoadipate dehydrogenase complex
Subject
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Topic
Chemistry
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Title
Rutgers University Electronic Theses and Dissertations
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ETD_11362
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application/pdf
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text/xml
Extent
1 online resource (xiv, 181 pages)
Note
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Ph.D.
Note
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Includes bibliographical references
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Title
Graduate School - Newark Electronic Theses and Dissertations
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rucore10002600001
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NjNbRU
Identifier
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doi:10.7282/t3-p1yx-4b15
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Rights
RightsDeclaration
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The author owns the copyright to this work.
RightsHolder
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Name
FamilyName
Zhang
GivenName
Xu
Role
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RightsEvent
Type
Permission or license
DateTime
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2020-12-23 14:49:54
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Name
Xu Zhang
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Copyright holder
Affiliation
Rutgers University. Graduate School - Newark
AssociatedObject
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License
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Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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Embargo
DateTime
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2021-01-31
DateTime
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2023-01-31
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2023.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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2021-01-25T20:30:16
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2021-01-25T20:30:16
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