Thermodynamics and regulation involving lipoic acid biochemistry of the classical 2-oxo acid dehydrogenase complexes. Dr Guerra 23.02.2021
- Author
- Dr Daniel J. Guerra
- Published
- Tue 23 Feb 2021
- Episode Link
- https://podcasters.spotify.com/pod/show/dr-daniel-j-guerra/episodes/Thermodynamics-and-regulation-involving-lipoic-acid-biochemistry-of-the-classical-2-oxo-acid-dehydrogenase-complexes--Dr-Guerra-23-02-2021-equic8
The Pyruvate dehydrogenase hydrated E1-E2 interface is enthalpy driven, while the dehydrated E3-peripheral subunit binding domain complex is driven by entropy obtaining a favourable delta G= delta H-T delta S= -33.4kj mol where the domain interfacial hydration obtains surface thermal complementarity and contributes finally to an aggregate strength of multiple affinities of individual non-covalent binding interactions via enthalpy-driven catalysis.
Lipoamidase activity of mitochondrial Sirtuin 4 modulates cellular fate by generating a debilitating removal of PDH-E2 dihydrolipoyllysine acetyltransferase-bound lipoic acid thus driving glutaminolysis over glucose oxidation.
Cell. 2014 Dec 18; 159(7): 1615–1625.
PNAS | August 23, 2016 | vol. 113 | no. 34
Structure VOLUME 13, ISSUE 8, P1119-1130, AUGUST 01, 2005
