Molecular cloning and primary structure of human 15-lipoxygenase

Biochem Biophys Res Commun. 1988 Dec 15;157(2):457-64. doi: 10.1016/s0006-291x(88)80271-7.


A full-length cDNA encoding 15-lipoxygenase has been isolated from a human reticulocyte cDNA library. The predicted primary structure of the enzyme exhibits a sequence similarity of 61% and 45% with human 5-lipoxygenase and the soybean lipoxygenase isoenzyme I, respectively. When all three lipoxygenases are aligned, there are two distinct regions of significant sequence identity including a cluster of five histidine residues conserved in all three lipoxygenases. Because histidines can serve as ligands for the enzymatically active iron, this region may be critical to enzymatic function. These results provide a basis for exploring functional domains of lipoxygenases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Arachidonate 15-Lipoxygenase / genetics*
  • Arachidonate Lipoxygenases / genetics*
  • Base Sequence
  • Cloning, Molecular
  • DNA / genetics
  • Humans
  • Molecular Sequence Data
  • Restriction Mapping


  • DNA
  • Arachidonate Lipoxygenases
  • Arachidonate 15-Lipoxygenase