The active site of an enzyme can perturb the pKas of amino acid side chains such that they are raised or lowered from what we would expect given the pKa values of the free amino acids. Consider an enzyme that uses a catalytic glutamate and a catalytic lysine in general acid-base catalysis. If the catalytic glutamate has a pKa of 7 and the catalytic lysine has a pKa of 9, then what percent (to two figures) of the enzyme is "typically" protonated such that the catalytic glutamate is unprotonated and the catalytic lysine is protonated?