Phosphorylation of Streptomycin at C₆-OH of Streptidine Moiety by an Intracellular Enzyme ofStreptomyces 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 A TP at C 6-0H 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.

Antibiotic resistance in pathogenic and producing bacteria, with special reference to beta-lactam antibiotics.

“…Consequently, it is probable that the f,-lactamases at the present time have been evolved convergently from many different proteins into one common property: hydrolysis of the ,B-lactam ring. If one accepts the idea that the enzymes inactivating antibiotics in pathogenic bacteria may be derived from antibioticproducing Streptomyces (11,137,246), these divergent properties can be easily understood. The reason is that the Streptomyces must protect itself at any cost from f,-lactam compounds which are its own metabolites.…”

Mechanism of resistance to streptothricin of a producing microorganism

“…Some streptomycetes which produce aminoglycoside antibiotics possess antibiotic-modifying enzymes (Nimi et al, 1971;Satoh et al, 1975;Dowding, 1979). These enzymes have been recently demonstrated to have a protective effect on protein synthesis by their producers (Sugiyama et al, 1981 and1983;Hotta et al, 1981).…”