Fermentation of MR-387A and B, Novel Aminopeptidase M Inhibitors by Streptomyces sp. SL-387: Phosphate Repression of Inhibitor Formation

The effect of inorganic phosphate on the fermentative production of aminopeptidase M inhibitors MR-387A and B by Streptomyces sp. SL-387 has been studied. With inorganic phosphate concentrations higher than 0.78 mM, an inverse correlation was found between the maximum inhibitor production and the initial phosphate concentration added. Growth sensitivity of this actinomycete to arsenate, a phosphate analogue, and the use of magnesium carbonate, a phosphate-trapping agent, suggested that the inhibitor formation was under phosphate repression. Exogenous ATP further increased the degree of phosphate interference in both phosphate-repressed and non repressed culture conditions. The use of a phosphate analogue and a protein synthesis inhibitor also suggested that the phosphate itself repressed inhibitor formation.