Case Discussion: Enzymes

1. Covalent enzyme Catalysis involves the formation of a transient covalent bond

between an enzyme and its substrate. Below are the general structures of
commonly encountered acyl-enzyme intermediates and other covalent derivatives.
a. give examples of amino acid residues that have side chains with the
reactive groups indicated above.
b. Give chemical names to the acyl-intermediates
2. Hexokinase catalyzes the phosphorylation of glucose and fructose by ATP.
however, km for glucose= 0.13mmol L -3 . Suppose that Vmax is the same for
glucose and fructose and that the enzyme displays hyperbolic kinetics.
a. Calculate the normalized initial velocity of the reaction (i.e., v o / Vmax) for
each substrate when [S]o=0.13, 1.3 and 13.0 mmol L -1
b. For which substrate does hexokinase have the greater affinity?
3. For phosphofructokinase in the liver, ATP, ADP, and citrate are effectors of the
reaction rate. Define what type of effectors they are, based on the information given
on the reaction below
Effector control of phosphofructokinase