Allosteric Properties of Chorismate Mutase from Quercus pedunculata

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Abstract
Chorismate mutase from Quercus pedunculata Ehrh. leaves has been purified by ammonium sulfate precipitation, molecular sieving and hydroxyapatite chromatography. Some results obtained during the purification suggest the presence, in oak, of two isofunctional forms of the enzyme, the one sensitive, the other insensitive to the action of aromatic amino acids. The regulable form exhibits a molecular weight of about 45,000. It is inhibited by tyrosine and by phenylalanine and is activated by tryptophan. In addition to its activating properties, this latter compound, endowed with a great affinity for the enzyme, reverses the inhibition due to the two other amino acids.The H+ concentration of the medium plays an important role in the sensitivity of the enzyme with regard to its effectors. Inhibition by tyrosine and by phenylalanine is maximal at pH 6.5, at which value the two ligands present an identical effect. At alkaline pH values, the rate of inhibition decreases regularly, tyrosine becoming the most effective inhibitor. Activation by tryptophan is particularly acute in a mildly acid medium; at pH 6.5, this effector increases the enzymatic activity threefold. Its action is weak (20% activation) in the optimum pH zone (pH 7.8) and increases towards the more basic pH values. As a result, tryptophan maintains a constant level of enzymatic activity throughout a large pH zone (between 6.5 and pH 9.0). The physiological significance of these results is discussed.