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

Proc Natl Acad Sci U S A. 1973 Aug;70(8):2276-80. doi: 10.1073/pnas.70.8.2276.

Abstract

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.

MeSH terms

  • Acetyltransferases / metabolism
  • Actinomycetales / enzymology*
  • Actinomycetales / metabolism
  • Anti-Bacterial Agents / biosynthesis
  • Anti-Bacterial Agents / metabolism*
  • Drug Resistance, Microbial*
  • Escherichia coli / enzymology
  • Gentamicins / metabolism
  • Glycosides / metabolism
  • Kanamycin / metabolism
  • Klebsiella pneumoniae / enzymology
  • Micromonospora / enzymology
  • Phosphotransferases / metabolism
  • Pseudomonas aeruginosa / enzymology
  • Streptomyces / enzymology
  • Streptomycin / metabolism
  • Transferases / metabolism*

Substances

  • Anti-Bacterial Agents
  • Gentamicins
  • Glycosides
  • Kanamycin
  • Transferases
  • Acetyltransferases
  • Phosphotransferases
  • Streptomycin