Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe

Bioorg Med Chem. 2012 Jan 15;20(2):592-6. doi: 10.1016/j.bmc.2011.06.068. Epub 2011 Jun 29.


Matrix metalloproteases (MMPs) are secreted or membrane-bound zinc-containing proteases that play diverse roles in development and immunity in plants and in tissue remodeling in animals. We developed a photoreactive probe based on the MMP inhibitor marimastat, conjugated to a 4-azidotetrafluorobenzoyl moiety as photoreactive group and biotin as detection or sorting function. The probe labels At2-MMP, At4-MMP, At5-MMP, and likely other plant MMPs in leaf extracts, as shown by transient At-MMP expression in Nicotiana benthamiana, protein blot, and LC-MS/MS analysis. This MMP probe is a valuable tool to study the post-translational status of MMPs during plant immunity and other MMP-regulated processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Catalytic Domain
  • Chromatography, High Pressure Liquid
  • Hydroxamic Acids / chemistry*
  • Matrix Metalloproteinase Inhibitors*
  • Matrix Metalloproteinases / genetics
  • Matrix Metalloproteinases / metabolism
  • Plant Leaves / enzymology
  • Plant Proteins / antagonists & inhibitors*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Protease Inhibitors / chemistry*
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Tandem Mass Spectrometry
  • Ultraviolet Rays


  • Hydroxamic Acids
  • Matrix Metalloproteinase Inhibitors
  • Plant Proteins
  • Protease Inhibitors
  • Recombinant Proteins
  • marimastat
  • Matrix Metalloproteinases