Regulation of Chloramphenicol Synthesis in Streptomyces sp. 3022a. 3-Deoxy-D-arabino-heptulosonate 7-Phosphate Synthetase
The repression and end-product inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthetase were studied in a chloramphenicol-producing Streptomycetes. Synthesis of DAHP synthetase was repressed by p-hydroxybenzoate, and enzyme activity was inhibited competitively by sugar phosphates, especially D-ribose 5-phosphate. The presence of chloramphenicol, aromatic amino acids, or shikimic acid pathway intermediates did not repress enzyme synthesis nor inhibit enzyme activity. Chloramphenicol production by growing cultures was not affected by the intermediates or end products of the shikimic acid pathway nor by the repression of DAHP synthetase. Purification of DAHP synthetase activity indicated the presence of a single enzyme protein with a molecular weight of 88 000.