Thermodynamics and regulation involving lipoic acid biochemistry of the classical 2-oxo acid dehydrogenase complexes. Dr Guerra 23.02.2021

Authentic Biochemistry

English - February 23, 2021 21:41 - 29 minutes - 27.4 MB - ★★★★★ - 10 ratings
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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

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