Which statement is correct about the Michaelis-Menten consta…

Which statement is correct about the Michaelis-Menten constant, Km, for the kinetic mechanism below?   a.  It is numerically equal to the substrate concentration required to achieve one half the maximum velocity.   b.  Its defined as Km = k1/(k−1 + k2).   c.  It is approximately equal to the dissociation constant for the enzyme-substrate complex to E + P.   d.  The value of Km is constant for an enzyme regardless of the specific substrate molecule used to determine it.   e.  Its numeric value has the units of moles−1.

All are characteristic of allosteric enzymes EXCEPT:  …

All are characteristic of allosteric enzymes EXCEPT:   a.  Effectors may show stimulatory or inhibitory activity.   b.  They have multiple subunits.   c.  They obey Michaelis-Menten kinetics.   d.  The regulatory effect is by altering conformation and interaction of subunits.   e.  Binding one subunit impacts binding of substrate to other subunits.