Pathways & interactions
Lipoxygenase, C-terminal (IPR013819)
Short name: LipOase_C
Overlapping homologous superfamilies
- Lipoxigenase, C-terminal domain superfamily (IPR036226)
Lipoxygenases (EC:1.13.11.-) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. In mammals a number of lipoxygenases isozymes are involved in the metabolism of prostaglandins and leukotrienes [PMID: 3017195]. Sequence data is available for the following lipoxygenases:
- Plant lipoxygenases (EC:126.96.36.199). Plants express a variety of cytosolic isozymes as well as what seems to be a chloroplast isozyme [PMID: 7508918].
- Mammalian arachidonate 5-lipoxygenase (EC:188.8.131.52).
- Mammalian arachidonate 12-lipoxygenase (EC:184.108.40.206).
- Mammalian arachidonate 15-lipoxygenase B (also known as erythroid cell-specific 15-lipoxygenase; EC:220.127.116.11).
The iron atom in lipoxygenases is bound by four ligands, three of which are histidine residues [PMID: 8502991]. Six histidines are conserved in all lipoxygenase sequences, five of them are found clustered in a stretch of 40 amino acids. This region contains two of the three iron-ligands; the other histidines have been shown [PMID: 1567851] to be important for the activity of lipoxygenases.
This entry represents the C-terminal region of these proteins.