PYRITHIAMINE ADAPTATION OF STAPHYLOCOCCUS AUREUS II. : Tricarboxylic Acid Cycle and Related Enzymes

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Das, S. K. (Calcutta University, Calcutta, India), and G. C. Chatterjee. Pyrithiamine adaptation of Staphylococcus aureus. II. Tricarboxylic acid cycle and related enzymes. J. Bacteriol. 86:1157–1164. 1963.—Evidence for the stimulated operation of the tricarboxylic acid cycle in Staphylococcus aureus after pyrithiamine adaptation is presented. In the cell-free extracts, isocitric, glutamic, malic, and succinic dehydrogenases and catalase were found to be stimulated after the adaptation of S. aureus to pyrithiamine. Besides such stimulation, the appearance of isocitratase and malate synthetase in the adapted strain supports the appearance of the glyoxalate bypass after such adaptation. There is little change in the activities of reduced nicotinamide adenine dinucleotide (NADH) and reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidases and diaphorase. Lactic dehydrogenase, NADH-cytochrome c reductase, and NADPH-cytochrome c reductase could not be demonstrated either in the normal or in the pyrithiamine-adapted S. aureus. These observations support the postulation that there is a stimulation in the tricarboxylic acid cycle and can account for the very marked stimulation in the utilization of acetate by the organism after adaptation.

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