Abstract
Lipases and esterases are lipolytic enzymes hydrolyzing hydrophobic long- and short-chain carboxylic acid esters, respectively (Verger, 1997). Lipases play an important role in intracellular lipid metabolism and extracellular lipid degradation. Information on the biological function of esterases is rather scarce. In organic chemistry these proteins represent about 25% of the biocatalysts currently used for stereo- and regioselective hydrolysis or esterification of synthetic substrates (Faber, 1992). Either crude enzyme preparations (e.g. pancreatic lipase) or a growing number of „pure" recombinant proteins are being employed for such purposes (Schmid and Verger, 1998). Knowledge of qualitative and quantitative enzyme composition is essential (Schmid and Verger, 1998) though not always available for crude enzymes. On the other hand, the fraction of active enzyme is an important parameter for (electrophoretically) pure (recombinant) lipases or esterases in monomeric or crystallized form. Both analytical requirements are not easy to meet using state of the art procedures (Schmid and Verger, 1998). Basic information on structure-function relationships of lipases and esterases has been obtained by X-ray crystallography (Anthonsen et al., 1995). However, information on lipases in solution and their interactions with their (supramolecular) substrates is scarce. High-resolution NMR spectroscopy of these systems requires high protein concentrations and, at the same time, a minimum of protein self-association (Anthonsen et al., 1994). Only the three-dimensional structure of cutinase has been solved by NMR to date.
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Hermetter, A., Mayer, B., Scholze, H., Zenzmaier, E., Graupner, M. (2001). Fluorescence Spectroscopic Studies on Structure and Function of Lipolytic Enzymes. In: Pifat-Mrzljak, G. (eds) Supramolecular Structure and Function 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1363-6_5
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DOI: https://doi.org/10.1007/978-1-4615-1363-6_5
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