Biochem multiple choice. help please

Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under which it can be applied. These include all of the following except one - choose the one that is not true. The kinetics must be analyzed in the early part of the time course (i.e. measuring the initial velocity), before product has accumulated to a significant level. The concentration of the enzyme-substrate complex is constant. The concentration of the enzyme-substrate complex (ES) is greater than 50% of total enzyme. The turnover number (kcat) for an enzyme is the number of times it can catalyze a reaction before it dies. the maximum number of substrate molecules that the enzyme can bind at one time. the maximum rate at which the enzyme's active site can catalyze the reaction. the number of times the enzyme can roll over and play dead before you have to give it a treat. An uncompetitive inhibitor binds at the active site at the enzyme, in competition with the substrate. always binds at a site far from the active site. never mimics a transition state of the reaction. would lead to a set of parallel lines from Lineweaver-Burke analysis at different inhibitor concentrations