Lipase Structure

Lipases are interphase-active enzymes with hydrophobic domains. The hydro-phobic surface (loop) on lipase is thought to enable lipophilic interfacial binding with substrate molecules that actually induces the conformational changes in lipases. The open conformation will provide substrate with access to the active site, and vice versa. In certain types of lipases, the movements of a short a-hehcal hydrophobic loop in the lipase structure cause a conformational change that exposes the active sites to the substrate. This movement also increases the nonpolarity of the surface surrounding the catalytic site [30, 32, 34, 35]. Obviously, the hydrophobic surface plays an important role in the activity of lipase as an enzyme. 

H. Verheij. Probing the interaction of phospholipase A2 and phospholipids with recombinant DNA techniques. In Lipases Structure, Mechanism and Genetic Engineering (L. Alberghina, R. Schmid, R. Verger, eds.). VCH, Weinheim, 1991, pp. 309-317. 

Many thanks go to Iris Baum and Lars Haller for designing the cover and creating the lipase structure shown on the cover. Frank Brouwer is acknowledged for providing the photo on the book cover. 

Crystallization of lipases from several sources had been reported (Misset et al. 1994 Jaeger et al. 1999). Mammalian, fungal and bacterial lipases had been crystallized and since 1990 lipase structure has been determined by X-ray all of them, except pancreatic lipase, where of bacterial origin (Jaeger and Reetz 1998). These enzymes have molecular weights which vary between 20 and 60 kDa. They have very similar folds despite a lack of sequence similarity (Smith et al. 1992). A comparison with X-ray structure of other hydrolytic enzymes revealed that all these enzymes share the same folding patter. Because all of them are hydrolytic enzymes, the common folding pattern was named a/(3 hydrolase fold (Ollis et al. 1992). The a/(3... 

Alberghina L, Schmidt RD, Verger R (eds) (1991) Lipases Structure, Mechanism and Genetic Engineering. GBF Monographs, vol 16. Verlag Chemie, Weinheim... 

The 3D structure of the lipase B from Candida antarctica was first reported by Brady et al. [3], in 1990, and subsequently other lipase structures have been solved [4]. The main features of lipase structures are as follows ... 

LIPASE STRUCTURE AND INTERFACIAL ACTIVATION 2.3.1 Lipase Structure... 

Hui DY, Howies PN. Carboxyl ester lipase structure-function relationship and physiological role in lipoprotein metabolism and atherosclerosis. J Lipid Res2002 43 2017-2030. 

Schmid A, Dordick JS, Hauer B, Kiener A, Wubbolts M, Witholt B (2001) Industrial biocatalysis today and tomorrow. Nature 409 258—268 Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A (1997) The open conformation of a pseudomonas lipase. Structure 5 187-202... 

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