Abstract
The question of regulation of α-ketoglutarate dehydrogenase complex (KGDHC) has been considered in the biochemical literature very rarely. Moreover, such information is not usually accurate, especially in biochemical textbooks. From the mini-review of research works published during the last 25 years, the following basic view is clear: a) animal KGDHC is very sensitive to ADP, Pi, and Ca2+; b) these positive effectors increase manifold the affinity of KGDHC to α-ketoglutarate; c) KGDHC is inhibited by ATP, NADH, and succinyl-CoA; d) the ATP effect is realized in several ways, probably mainly via opposition versus ADP activation; e) NADH, besides inhibiting dihydrolipoamide dehydrogenase component competitively versus NAD+, decreases the affinity of α-ketoglutarate dehydrogenase to substrate and inactivates it; f) thioredoxin protects KGDHC from self-inactivation during catalysis; g) bacterial and plant KGDHC is activated by AMP instead of ADP. These main effects form the basis of short-term regulation of KGDHC.
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Translated from Biokhimiya, Vol. 70, No. 7, 2005, pp. 880–884.
Original Russian Text Copyright © 2005 by Strumilo.
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Strumilo, S. Short-Term Regulation of the α-Ketoglutarate Dehydrogenase Complex by Energy-Linked and Some Other Effectors. Biochemistry (Moscow) 70, 726–729 (2005). https://doi.org/10.1007/s10541-005-0177-1
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DOI: https://doi.org/10.1007/s10541-005-0177-1