GLUCOSE METABOLISM OF CLOSTRIDIUM PERFRINGENS: EXISTENCE OF A METALLO-ALDOLASE

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Abstract
The homolactic fermentation of Fe-deficient C. perfringens was inhibited by alpha, alpha-dipyridyl and o-phenanthroline, an effect that was reversed by Fe++ and Co++ but not by Zn++, Cu++, Ni++, Mg++, Mn++, or Fe+++. Aldolase, the enzyme converting hexose diphosphate to triose phosphate, was prepd. in cell-free form-from C. perfringens and shown to be inhibited by the same agents that inhibit glycolysis. Furthermore the inhibition was reversed by Fe++, and less completely by Co++ The cell-free aldolase also required a reducing agent, such as cysteine, for max. activation. The essentiality of Fe for the function of aldolase offered a possible explanation of the indispensable requirement of Fe for clostridial growth and for the homolactic fermentation. The occurrence of aldolase as the key enzyme for the transformation of hexose diphosphate to triose phosphate suggested the occurrence of the Embden-Meyerhof system in this organism.

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