You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: a) What is the V_max in the absence of inhibitor?
b) What is the K_m in the absence of inhibitor?
c) When [S] = 0.0004, what will V_0 be in the absence of inhibitor?
d) When [S] = 0.0004, what will V_0 be in the presence of inhibitor?
e) What kind of inhibitor is it likely to be?

Atp is is our little "pocket" of energy. of course, if you have too little, then it means you have too little energy, and you'll pass out. the way to not have enough, is to have no energy sources (glucose, fats, proteins). you can't have too many atp molecules. cycles like the krebs cycle produce it, but if you have too much of any substrate (or too little for that matter), the cycle stops and atp is no longer made (it stops until substrate levels are such that the process can go on). in any case, this is unlikely since atp is constantly hydrolyzed and remade, even while you're asleep. you won't have too much. if you have zero, you are dead or dying.