General description
Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis.[5] Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1).[6] The N-terminal catalytic domain is essential for lipolysis. The C-terminal is crucial for binding lipoproteins. Altered LPL levels may play role in the pathogenesis of atherosclerosis, coronary heart disease and chronic lymphocytic leukemia.[7]Application
Lipoprotein Lipase from Pseudomonas sp. has been used in the enzymatic erosion studies in gamma irradiated poly(trimethylene carbonate) (PTMC) films.[8]
Biochem/physiol Actions
Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.[1][2]
Lipoprotein lipase belongs to the family of triglyceride lipases. It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.
Unit Definition
1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314 as substrate)
Other Notes
Preparation of aldol acceptors (R)- and (S)-3-azido-2-hydroxypropanal via lipase-catalyzed resolution of the racemic acetal precursor[3]; Effect of enzyme form on its properties in toluene[4]