Flip-Flop Mechanisms in Enzymology A Model : the Alkaline Phosphatase of Escherichia coli

摘要: A new mechanism is proposed which permits a clear-cut interpretation of the properties and features characteristic alkaline phosphatase Escherichia coli. It called Flip-Flop mechanism. The implies alternating functions for each two active sites phosphatase. phosphorylation one site concurrent with dephosphorylation other site. considered to be model. functional evolutive advantages suggest that it might fairly common among polymeric enzymes Michaelian kinetics, Data already reported in literature are discussed light Most intracellular polymeric, many may oligomeric. Kinetically speaking, there main types enzymes: those cooperative w-[S] profiles designated as allosteric “classical” MichaelisMenten kinetics. This last class much larger. Monod et al. [l] have shown kinetics necessitate structures indirect interactions between distinct binding sites. These mediated by structural change, transition [ 11.