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1.An enzyme has ping-pong kinetics. At a concentration of substrate b ab a equal to 0.005 M and a saturating concentration of substrate , the apparent velocity (Vapp) is 0.08 moles/hour. Given the kM for substrate (kMB) is 0.002 M, calculate the Vmax of the enzyme. Under these conditions the apparent kM (kMapp) is 0.0029 M, what is the kM for substrate (kMA)?
2.An enzyme demonstrating ternary complex enzyme kinetics has the same kM for substrates a and b (kMA, kMB) as the enzyme in question 2 above. However, the apparent kM (kMapp) is approx. double, 0.0060 M. Calculate the true dissociation constant for this enzyme (kiA). If the Vapp for this enzyme under these conditions is 0.16 moles/hour determine the Vmax. How does this value compare to the enzyme in question 2 above?
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