The structures and the mechanisms of functioning of multienzyme comple
xes of the 2-ketoacid dehydrogenase family are considered. It is assum
ed that identical protein subunits form identical interfaces with thei
r neighbors and hence have identical surroundings in multienzyme compl
exes capable of self-assembly. Dividing the subunits into different co
nformational classes, one can position the peripheral components on th
e skeleton in a way allowing symmetry of the entire complex. The numbe
r of conformational classes is determined by the skeleton architecture
and symmetry considerations. This structural analysis has some implic
ations for the reaction mechanisms of multienzyme complexes. Some spec
ific cases are discussed.