v5.1.0.3
Glycine data from LIS
Type | Binding_site |
Description | Lipoxygenases ([intenz: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 []. Sequence data is available for the following lipoxygenases: Plant lipoxygenases ( ). Plants express a variety of cytosolic isozymes as well as what seems to be a chloroplast isozyme [].Mammalian arachidonate 5-lipoxygenase ( ). Mammalian arachidonate 12-lipoxygenase ( ). Mammalian arachidonate 15-lipoxygenase B (also known as erythroid cell-specific 15-lipoxygenase; ). The iron atom in lipoxygenases is bound by four ligands, three of which are histidine residues []. 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 [] to be important for the activity of lipoxygenases.This entry represents a motif that contains the iron-binding sites. |
Short Name | LipOase_Fe_BS |