Abstract
In vertebrates there are at least three genetic families of lipases that regulate the distribution of ingested neutral ester lipids, that is, triacylglycerols and their degradation products, among tissues and among intracellular compartments. Each of the lipases involved in lipid homeostasis is adapted to function optimally in a specific environment. Even so, the major challenges faced by lipases are shared by all species. Most notably, the lipases of the families mentioned previously are separated from the bulk of their substrates by a monolayer or multilayer of amphipathic molecules. This occurs because the lipases are water-soluble proteins, whereas their triacylglycerol and diacylglycerol substrates are relatively apolar and form bulk oil phases in aqueous environments (Small, 1970). In vivo, amphipathic lipids and/or proteins are also present, depending on where the lipase functions. Thus, the lipase needs to remain soluble in water yet be able to attach itself to the appropriate substrate-containing lipid droplet, lipoprotein, or membrane. It must also avoid futile association with inert interfaces, that is, membranes that do not cover substrate-containing bulk phases, which would effectively inhibit the activity of the lipase by separating it from its intended substrate. The specific strategies used for adsorbing to the proper interface and gaining access to the substrate depend on the interfacial compositions of the substrate-containing and competing interfaces.
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Brockman, H. (2001). Pancreatic Lipase. In: Mansbach, C.M., Tso, P., Kuksis, A. (eds) Intestinal Lipid Metabolism. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1195-3_4
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DOI: https://doi.org/10.1007/978-1-4615-1195-3_4
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5435-2
Online ISBN: 978-1-4615-1195-3
eBook Packages: Springer Book Archive