Phosphorylation of Streptomycin at C₆-OH of Streptidine Moiety by an Intracellular Enzyme of Streptomyces griseus

Abstract

In streptomycin-producing Streptomyces griseus HUT 6037, an enzyme which phosphorylated streptomycin appeared in old mycelium at stationary to autolyzing stage. This enzyme phosphorylated streptomycin with equimolar ATP at C₆-OH in the streptidine moiety. This phosphomonoester of streptomycin was identified with the phosphorylated streptomycin (referred to as L compound) which was previously reported to accumulate in the culture broth when the pH was controlled below neutral.