Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa

FASEB J. 2013 Dec;27(12):4811-21. doi: 10.1096/fj.13-235952. Epub 2013 Aug 28.


Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with respect to eukaryotic LOXs, including a cluster of helices acting as a lid to the active center. The mobility of the lid and the structural variability of the N-terminal region of Pa_LOX was confirmed by comparing 2 crystal forms. The binding pocket contains a phosphatidylethanolamine phospholipid with branches of 18 (sn-1) and 14/16 (sn-2) carbon atoms in length. Carbon atoms from the sn-1 chain approach the catalytic iron in a manner that sheds light on how the enzymatic reaction might proceed. The findings in these studies suggest that Pa_LOX has the capacity to extract and modify unsaturated phospholipids from eukaryotic membranes, allowing this LOX to play a role in the interaction of P. aeruginosa with host cells.

Keywords: enzyme mechanisms; host–pathogen interactions; lipid peroxidation; membrane interaction; protein–phospholipid complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Catalytic Domain
  • Lipoxygenase / chemistry*
  • Lipoxygenase / metabolism
  • Molecular Docking Simulation
  • Molecular Sequence Data
  • Phosphatidylethanolamines / chemistry
  • Phosphatidylethanolamines / metabolism*
  • Protein Binding
  • Pseudomonas aeruginosa / enzymology*


  • Phosphatidylethanolamines
  • phosphatidylethanolamine
  • Lipoxygenase