Authentic Biochemistry

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 --- Send in a voice message: https://anchor.fm/dr-daniel-j-guerra/message