Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl tRNA synthetases

Bioorg Med Chem Lett. 2000 Aug 21;10(16):1871-4. doi: 10.1016/s0960-894x(00)00360-7.

Abstract

Aminoalkyl adenylates and aminoacyl sulfamates derived from arginine, histidine and threonine, have been prepared and tested as inhibitors of their cognate Staphylococcus aureus aminoacyl tRNA synthetases. The arginyl derivatives were both potent nanomolar inhibitors of the Class I arginyl tRNA synthetase whereas for the Class II histidyl and threonyl tRNA synthetases, the acyl sulfamates were potent inhibitors but the adenylates had very little affinity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Monophosphate / analogs & derivatives*
  • Adenosine Monophosphate / chemical synthesis
  • Adenosine Monophosphate / chemistry
  • Adenosine Monophosphate / metabolism
  • Adenosine Monophosphate / pharmacology
  • Amino Acyl-tRNA Synthetases / antagonists & inhibitors*
  • Amino Acyl-tRNA Synthetases / metabolism*
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / metabolism
  • Staphylococcus aureus / enzymology*
  • Sulfonamides / chemical synthesis*
  • Sulfonamides / chemistry
  • Sulfonamides / metabolism*
  • Sulfonamides / pharmacology

Substances

  • Enzyme Inhibitors
  • Sulfonamides
  • Adenosine Monophosphate
  • Amino Acyl-tRNA Synthetases