An tetrameric enzyme catalyzing the atp-dependent phosphorylation of glycerol was purified, and its kinetic properties characterized. these properties are as follows: a plot of vo vs. [s] yielded a hyperbolic curve double-reciprocal plots of 1/vo vs [glycerol] measured at increasing [atp] appear equivalent to that measured in the presence of a mixed noncompetitive inhibitor exhibiting preferential interaction with the enzyme-substrate complex. the products of the reaction are inhibitory above a threshold concentration. product inhibition increases km while vmax remains constant. based on this description answer the following: is this enzyme allosteric or non-allosterie? what class of enzyme has been purified? what type of kinetic process is consistent with the observed kinetics? provide a kinetic scheme diagramming the reaction of this enzyme