The effect of \(\mathrm{pH}\) on the activity of an enzyme was examined. At its
active site, the enzyme has an ionizable group that must be negatively charged
in order for substrate binding and catalysis to take place. The ionizable
group has a \(\mathrm{p} K_{\mathrm{a}}\) of \(6.0 .\) The substrate is positively
charged throughout the \(\mathrm{pH}\) range of the experiment. (EQUATION CAN'T
COPY)
(a) Draw the \(V_{0}\) -versus-pH curve when the substrate concentration is much
greater than the \(K_{M}\) of the enzyme.
(b) Draw the \(V_{0}\) -versus-pH curve when the substrate concentration is much
less than the \(K_{M}\) of the enzyme.
(c) At which \(\mathrm{pH}\) will the velocity equal one-half of the maximal
velocity attainable under the conditions described in (b)?
