Activation of interfacial enzymes at membrane surfaces

Ole G. Mouritsen, Thomas Lars Andresen, Avi Halperin, Per Lyngs Hansen, Ask F. Jakobsen, Uffe Bernchou Jensen, Morten Ø. Jensen, Kent Jørgensen, Thomas Kaasgaard, Chad Leidy, Adam Cohen Simonsen, Günther H.J. Peters, Matthias Weiss

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

A host of water-soluble enzymes are active at membrane surfaces and in association with membranes. Some of these enzymes are involved in signalling and in modification and remodelling of the membranes. A special class of enzymes, the phospholipases, and in particular secretory phospholipase A2 (sPLA2), are only activated at the interface between water and membrane surfaces, where they lead to a break-down of the lipid molecules into lysolipids and free fatty acids. The activation is critically dependent on the physical properties of the lipid-membrane substrate. A topical review is given of our current understanding of the physical mechanisms responsible for activation of sPLA2 as derived from a range of different experimental and theoretical investigations.
Original languageEnglish
JournalJournal of Physics: Condensed Matter
Volume18
Issue number28
Pages (from-to)S1293-S1304
Number of pages12
ISSN0953-8984
DOIs
Publication statusPublished - 2006

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