Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: A homodimeric enzyme with a complex domain organization

► Folding mechanism of a large two-domain dimeric enzyme. ► A minimum kinetic model involves an unstructured monomer and dimeric intermediates. ► Most part of ΔASA occurs during a slow subunit association/folding step. ► Topological constrain between subunits and interface explains this behavior.