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Results 1 - 10 of 46 > >>
EC Number
Subunits
Commentary
Reference
?
x * 30028, catalytic domain, calculated from amino acid sequence; x * 30030, catalytic domain, FT mass spectrometry
?
x * 33100, about, E2, sequence calculation
?
x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry
?
x * 59000, SDS-PAGE, recombinant protein
?
x * 65959, calculated from amino acid sequence
dimer
2 * 36000, in the presence of dilute acetic acid
dimer
60mer, analytical ultracentrifugation
dimer
GST-L2, glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase exists as a dimer
dimer
multimer formation is probably lost by loss of a small segment during genetic rearrangement
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
Results 1 - 10 of 46 > >>