| Type: | Family | Name: | Lipoprotein lipase |
| Description: | Lipoprotein lipase (LPL) is a key enzyme of lipid metabolism that hydrolyses triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins []. The enzyme is thought to playa role in the development of obesity and atherosclerosis []. Human LPLcontains 448 amino acids; sequence comparison indicates that human LPL, hepatic lipase, and pancreatic lipase are members of a gene family []. Defects in LPL are a cause of familial chylomicronemia syndrome (or type I hyperlipoproteinemia) and also of a form of deficiency characterised byhypertriglyceridemia. Familial chylomicronemia is a recessive disorder usually manifesting in childhood. On a normal diet, patients often presentwith abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated withacute pancreatitis. LPL and pancreatic lipase share ~30% sequence identity, suggesting a similartertiary fold []. Molecular models of LPL have been constructed, based on X-ray crystal structures of pancreatic lipase []. These models allowed theauthors to propose hypotheses on the structural determinants of LPL that are responsible for heparin binding, dimer formation, and phospholipase activity. | Short Name: | Lipo_Lipase |
