Lipoxygenases (LOXs, LOs) catalyze the the dioxygenation of polyunsaturated fatty acids, including arachidonic acid. Animal LO enzymes include 5-LO, 12-LO (epidermal-, platelet-, and leukocyte-type), 15-LO, and eLOX-3 (epidermis-type LO-3). 12-LO and 15-LO and its metabolites participate in apoptosis, autophagy and ferroptosis, and have been implicated in the development of insulin resistance and diabetes [, ].This entry represents the PLAT domain of vertebrate LOs []. 12-LO and 15-LO are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates [, , ].
This entry represents a domain superfamily found in a variety of membrane or lipid associated proteins. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a β-sandwich composed of two sheets of four strands each [, , ]. The most highly conserved regions coincide with the β-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth β-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.
This entry represents a domain found in a variety of membrane or lipid associated proteins. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a β-sandwich composed of two sheets of four strands each [, , ]. The most highly conserved regions coincide with the β-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth β-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.
