1998
DOI: 10.1074/jbc.273.37.24158
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Subunit Interactions in the Mammalian α-Ketoglutarate Dehydrogenase Complex

Abstract: Selective tryptic proteolysis of the mammalian ␣-ketoglutarate dehydrogenase complex (OGDC) leads to its rapid inactivation as a result of a single cleavage within the N-terminal region of its ␣-ketoglutarate dehydrogenase (E1) component, which promotes the dissociation of the dihydrolipoamide dehydrogenase (E3) enzyme and also a fully active E1 fragment. Similarities between the N-terminal region of E1 and the dihydrolipoamide acetyltransferase (E2) and E3-binding components (E3BP) of the pyruvate dehydrogena… Show more

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Cited by 52 publications
(14 citation statements)
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“…28 Other studies suggest that single copies of E1 and E3 form homodimers by a high‐affinity reaction, with the homodimers binding to the E2k core through the N‐terminal region of E1. 28,32 Human E2k lacks the consensus binding domains for E1 and E3 that have been identified in other mammalian E2ks, 10,11 and the mechanism of association of the three proteins in human KGDHC has not yet been specified.…”
Section: Structure Of Kgdhcmentioning
confidence: 99%
“…28 Other studies suggest that single copies of E1 and E3 form homodimers by a high‐affinity reaction, with the homodimers binding to the E2k core through the N‐terminal region of E1. 28,32 Human E2k lacks the consensus binding domains for E1 and E3 that have been identified in other mammalian E2ks, 10,11 and the mechanism of association of the three proteins in human KGDHC has not yet been specified.…”
Section: Structure Of Kgdhcmentioning
confidence: 99%
“…The two subunits (E1, E2) that encode the 2-oxoglutarate dehydrogenase (E1) and the dihydrolipoamide succinyltransferase (E2) activity, are located next to each other. The third subunit (E3) encoding the dihydrolipoamide dehydrogenase activity of the 2-oxoglutarate dehydrogenase enzyme complex is known to be often shared with the E1-E2 subunit sets of pyruvate dehydrogenase and of branched-chain α-keto acid dehydrogenases (Berg and de Kok, 1997; McCartney et al, 1998). Therefore, it appears little as surprise that subunit E3 does not cluster with the first two components of the 2-oxoglutarate dehydrogenase enzyme complex.…”
Section: Resultsmentioning
confidence: 99%
“…The biological significance of the KGDHC-dependent paracatalytic reactions involving E 1 k-E 3 interaction is supported further by the fact that KGDHC from brain possesses a specific isoform of E 1 k and a lower E 3 content than that of the heart complex (116). Structural differences between the two E 1 k isoforms (117) and the role of E 1 k in the E 3 binding to the complex (118) suggest that the lower E 3 content of brain KGDHC is determined by the structure of the brain-specific isoform of E 1 k. The decreased content of E 3 in the brain KGDHC may thus represent an additional means by which the brain is protected from excessive ROS generation.…”
Section: Potential Role Of Paracatalytic Side Reactions In Disementioning
confidence: 99%