Page 579 - Carrahers_Polymer_Chemistry,_Eighth_Edition
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542                                                    Carraher’s Polymer Chemistry



                             Reactant









                              Enzyme




                            Tight; inactive  Relaxed; active






                               (a)              (b)               (c)             (d)
                 FIGURE 16.7  Concerted model for allosteric enzymes. The major steps are (a) and (b). An equilibrium exists
                 between the tight (a) and relaxed (b) forms of the allosteric enzyme. The reactant molecule(s) approaches the
                 reactive site of one of the enzyme sites present in the relaxed form (c). Binding occurs, shifting the equilibrium
                 to the relaxed form(s). The second site is bound (d).






                            Reactant








                            Enzyme





                          Tight; inactive                                     Relaxed; active





                              (a)              (b)              (c)                (d)

                 FIGURE 16.8  Sequential model for allosteric enzymes. The individual steps are as follows: the reactive
                 molecule(s) approach the reactive site (a), which typically has a cavity similar to, but not the same as, the reac-
                 tant molecule(s); a conformational change is effected so that the reactive molecule(s) can be bound (b); the
                 bound portion of the enzyme changes shape; this shape change is transmitted to the other unit(s) containing
                 active sites (c); the remaining enzyme portion containing active sites undergoes a conformational change that
                 makes binding easier.







                                                                                              9/14/2010   3:43:14 PM
         K10478.indb   542                                                                    9/14/2010   3:43:14 PM
         K10478.indb   542
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