2.3.1.12	reconstitution of E1 with E2-E3 complex with a stoichiometry of E1:E2:E3 of 2:1:1	348946	
2.3.1.12	reconstitution of pyruvate dehydrogenase complex	486168, 486194	
2.3.1.12	reconstitution of pyruvate dehydrogenase complex with components from Escherichia coli and Salmonella typhimurium	348948	
2.3.1.12	reconstitution of pyruvate dehydrogenase complex, maximum activity is produced when transacetylase accommodates 12 pyruvate dehydrogenase dimers and 6 flavoprotein dimers	486201	
2.3.1.12	reconstitution of pyruvate dehydrogenase complex, optimum catalytic stoichiometry of E1:E2:E3 is 5.2:11.5:2	486202	
2.3.1.12	reconstitution of pyruvate dehydrogenase complex, stoichiometry pyruvate dehydrogenase:transacetylase:flavoprotein is 1:0.35:0.4	486207	
2.3.1.12	reconstitution of the active multienzyme complex with recombinant components	663289	
2.3.1.12	reconstitution with components from Escherichia coli and Azotobacter vinelandii, optimum catalytic stoichiometry of E1:E2:E3 is 1:1:0.5	348932	
2.3.1.12	treatment with dilute acetic acid solution results in dissociation into inactive subunits with MW 70000, removal of the acid results in restoration of enzymatic activity	486210	
2.3.1.12	treatment with guanidine hydrochloride and its subsequent removal results in little recovery of the core, but full recovery of X	486226	
2.3.1.12	treatment with guanidine hydrochloride and its subsequent removal results in refolding	486231	
2.3.1.12	treatment with guanidine hydrochloride results in dissociation into subunits, removal of guanidine hydrochloride results in refolding of the enzyme with 95% of the original activity	486225