Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria.

Various species of Streptomyces possess aminoglycoside-modifying enzymes. Streptomyces kanamyceticus contains an enzyme that acetylates the 6'-amino group of kanamycin A and B, gentamicin C(1a), and neomycin. Streptomyces spectabilis produces an enzyme that acetylates the 2'-amino group of the hexose ring of gentamicin C(1a). These enzymes catalyze reactions identical to those catalyzed by enzymes found in gram-negative bacteria containing R(antibiotic resistance)-factors. The discovery of these enzymes suggests the possibility of an evolutionary relationship between the aminoglycosideinactivating enzymes (produced by resistance determinants) in bacteria containing R-factors and similar enzymes found in the actinomycetes.