Carbohydrate metabolism in Spirochaeta recurrentis. 3. Properties of aldolase in spirochaetes

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Abstract
Some of the properties of a diphosphofructoaldolase in cell-free extracts of S. recurrentis were studied. By the hydrazine triose-trapping method, a pH optimum of 8.75 and an approximate Km 1.3 m[image] were demonstrated. These values are similar to those derived for the enzyme from other sources. The enzyme is activated by Co2+ and Zn2+ ions, cysteine and reduced glutathione. Fe2+, Mn2+ and Mg2+ ions either inhibit or have no effect. Ethylenediaminetetra-acetate, 8-hydroxyquinoline, [alpha][alpha][image]-dipyridyl and p-chloromercuribenzoate inhibit aldolase activity. On the basis of these findings the spirochaetal enzyme is classed as a sulphydryl-group-containing metalloaldolase. The extent of metal-ion activation of different aldolases is briefly discussed.