THE OXIDATION OF TRICARBOXYLIC ACID CYCLE COMPOUNDS BY PENICILLIUM CHRYSOGENUM

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Abstract
The phosphatase in cell-free prepns. of P. chrysogenum rapidly hydrolyzed adenosine triphosphate, triphosphopyridine nucleotide, diphosphopyridine nucleotide, flavin adenine dinucleo-tide, riboflavin phosphate, acetyl phosphate and possibly coenzyme A. The use of phosphate and fluoride as phosphate inhibitors provided some stability of the cofactors and allowed oxidation of the tricarboxylic acid cycle compounds. The expts. descr. indicate that a tricarboxylic acid cycle could be present in P. chrvsogenum, strain NRRL 1951 .B25. The respective oxidases were found in cell-free prepns.; isocitric dehydrogenase and malic dehydrogenase activity was increased with the addition of acetate to the growing cells; and the condensation of acetyl phosphate and oxalacetate was shown.
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