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Thiamine diphosphate is tightly but not covalently bound to the 2-oxoglutarate dehydrogenase component [57] ThDP remains an essential cofactor and alphaketoglutarate dehydrogenase complex in the form of homo dimers alpha2, homo tetramers alpha 4 or heterotetramers alpha 2 beta 2 contain ThDP binding pockets that constitute two or four active sites for this enzyme which operate independently without an obligatory alternating mechanism in the E1b component [58] and overall activity is abolished at 50% phosphorylation (1 of 2 sites) within each active channel similar to PDC [59].Alpha ketoglutarate dehydrogenase/2 oxoglutarate dehydrogenase E1k heterotetramer core has 24 /60 copies containing lipoyl active site as well as active sites for E1 and E3 subunits based on similar mammalian PDC structural studies and molecular wt of 64.5 KDa [5]

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doi: 10.3389/fnins.2016.00077 19 MerloSCanonicoPLSortinoMA