Literature summary for 2.3.1.12 extracted from

Milne, J.L.; Wu, X.; Borgnia, M.J.; Lengyel, J.S.; Brooks, B.R.; Shi, D.; Perham, R.N.; Subramaniam, S.
Molecular structure of a 9-MDa icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopy (2006), J. Biol. Chem., 281, 4364-4370.

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Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	P11961	-	-

Subunits

Subunits	Comment	Organism
More	cryoelectron microscopic analysis of the reconstructed three-dimensional structure of the purified E2E3 complex (dihydrolipoyl acetyltransferase/dihydrolipoyl dehydrogenase) and use of automated docking methods to interpret the density map in terms of the probable localization of the dihydrolipoyl acetyltransferase E2 and dihydrolipoyl dehydrogenase E3 molecules. The arrangement of pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3 molecules in the outer shell of the pyruvate dehydrogenase complex are remarkably similar and indicate that the design of the annular gap allows the lipoyl domain to have access to the active sites of pyruvate decarboxylase E1, dihydrolipoyl acetyltransferase E2, and dihydrolipoyl dehydrogenase E3 enzymes from within the annular gap	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)