The use of neamine as a molecular template: inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3'-phosphotransferase type IIa

Bioorg Med Chem Lett. 1998 Dec 15;8(24):3483-8. doi: 10.1016/s0960-894x(98)00633-7.

Abstract

Aminoglycoside 3'-phosphotransferase type IIa [APH(3')-IIa] is a member of the family of bacterial aminoglycoside-modifying enzymes. Bacteria that harbor these enzymes are resistant to aminoglycoside antibiotics. Four aminoglycoside-based affinity inactivators were synthesized and were shown to be both substrates and inactivators for APH(3')-IIa. These affinity inactivators are N-bromoacetylated derivatives of neamine, an aminoglycoside antibiotic, where the bromoacetyl moiety in each was introduced regiospecifically at a different amine of the parent compound.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacteria / drug effects
  • Bacteria / enzymology*
  • Drug Resistance, Microbial
  • Kanamycin Kinase / antagonists & inhibitors*
  • Molecular Probes
  • Molecular Structure
  • Neomycin / chemistry*

Substances

  • Molecular Probes
  • Kanamycin Kinase
  • Neomycin