001018222 001__ 1018222
001018222 005__ 20240124203859.0
001018222 0247_ $$2datacite_doi$$a10.34734/FZJ-2023-04618
001018222 0247_ $$2URN$$aurn:nbn:de:0001-20240124090434709-4196616-1
001018222 020__ $$a978-3-95806-722-6
001018222 037__ $$aFZJ-2023-04618
001018222 1001_ $$0P:(DE-Juel1)178698$$aSundermeyer, Lea$$b0$$eCorresponding author$$ufzj
001018222 245__ $$aAnalysis of the signal transduction cascade tuning the 2-oxoglutarate dehydrogenase activity in Corynebacterium glutamicum$$f- 2022-12-19
001018222 260__ $$aJülich$$bForschungszentrum Jülich GmbH Zentralbibliothek, Verlag$$c2023
001018222 300__ $$aVI, 119
001018222 3367_ $$2DataCite$$aOutput Types/Dissertation
001018222 3367_ $$0PUB:(DE-HGF)3$$2PUB:(DE-HGF)$$aBook$$mbook
001018222 3367_ $$2ORCID$$aDISSERTATION
001018222 3367_ $$2BibTeX$$aPHDTHESIS
001018222 3367_ $$02$$2EndNote$$aThesis
001018222 3367_ $$0PUB:(DE-HGF)11$$2PUB:(DE-HGF)$$aDissertation / PhD Thesis$$bphd$$mphd$$s1700486222_24513
001018222 3367_ $$2DRIVER$$adoctoralThesis
001018222 4900_ $$aSchriften des Forschungszentrums Jülich Reihe Schlüsseltechnologien / Key Technologies$$v273
001018222 502__ $$aDissertation, Univ. Düsseldorf, 2022$$bDissertation$$cUniv. Düsseldorf$$d2022
001018222 520__ $$aIn Corynebacterium glutamicum and many other actinobacteria, the 2-oxoglutarate dehydrogenase complex (ODH), a key enzyme of the tricarboxylic acid cycle, differs from wellknown representatives by an unusual E1 subunit (OdhA), which is fused with the succinyltransferase domain usually present in a separate E2o subunit. Therefore, OdhA requires the lipoyl groups of the E2p protein (AceF) of the pyruvate dehydrogenase complex (PDH) for transferring the succinyl group to coenzyme A. As a consequence, ODH forms a hybrid complex with PDH, composed of the four proteins OdhA, AceE (E1p), AceF, and Lpd (E3). Another unusual feature of ODH in C. glutamicum and other actinobacteria is its regulation by the 15-kDa protein OdhI, which contains a forkhead-associated (FHA) domain known to bind phospho-threonine epitopes. In its unphosphorylated state, OdhI binds to OdhA with nM affinity and inhibits ODH activity. Phosphorylation of OdhI by the soluble serine/threonine protein kinase PknG triggers a conformational change of OdhI that prevents its interaction with OdhA and thereby abolishes the inhibition of ODH activity. Dephosphorylation of phosphorylated OdhI is catalyzed by the phospho-serine/threonine protein phosphatase Ppp. Previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, whose genes form an operon with pknG....
001018222 536__ $$0G:(DE-HGF)POF4-2171$$a2171 - Biological and environmental resources for sustainable use (POF4-217)$$cPOF4-217$$fPOF IV$$x0
001018222 8564_ $$uhttps://juser.fz-juelich.de/record/1018222/files/Schluesseltech_273.pdf$$yOpenAccess
001018222 909CO $$ooai:juser.fz-juelich.de:1018222$$pVDB$$pdriver$$purn$$popen_access$$popenaire$$pdnbdelivery
001018222 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
001018222 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
001018222 9141_ $$y2023
001018222 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)178698$$aForschungszentrum Jülich$$b0$$kFZJ
001018222 9131_ $$0G:(DE-HGF)POF4-217$$1G:(DE-HGF)POF4-210$$2G:(DE-HGF)POF4-200$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$9G:(DE-HGF)POF4-2171$$aDE-HGF$$bForschungsbereich Erde und Umwelt$$lErde im Wandel – Unsere Zukunft nachhaltig gestalten$$vFür eine nachhaltige Bio-Ökonomie – von Ressourcen zu Produkten$$x0
001018222 920__ $$lyes
001018222 9201_ $$0I:(DE-Juel1)IBG-1-20101118$$kIBG-1$$lBiotechnologie$$x0
001018222 980__ $$aphd
001018222 980__ $$aVDB
001018222 980__ $$aUNRESTRICTED
001018222 980__ $$abook
001018222 980__ $$aI:(DE-Juel1)IBG-1-20101118
001018222 9801_ $$aFullTexts