| Issue |
Europhys. Lett.
Volume 57, Number 3, February 2002
|
|
|---|---|---|
| Page(s) | 464 - 470 | |
| Section | Condensed matter: electronic structure, electrical, magnetic, and optical properties | |
| DOI | https://doi.org/10.1209/epl/i2002-00483-y | |
| Published online | 01 September 2002 | |
Phospholipase 
—An enzyme that is
sensitive to the physics of its substrate
1
MEMPHYS - Center for Biomembrane Physics
Department of Chemistry, Technical University of
Denmark DK-2800 Lyngby, Denmark
2
MEMPHYS - Center for Biomembrane Physics
Physics Department, University of Southern Denmark
DK-5230 Odense M, Denmark
Corresponding author: ogm@memphys.sdu.dk
Received:
25
July
2001
Accepted:
13
November
2001
A simple statistical mechanical model of lipid bilayers is proposed to account for the non-equilibrium action of the enzyme phospholipase A2. The enzyme hydrolyses lipid-bilayer substrates and produces product molecules that lead to local variations in the bilayer interfacial pressure. Computer simulation of the model shows, in quantitative agreement with experimental data, that the enzyme activity is modulated by nano-scale lipid-domain formation in the lipid bilayer leading to a characteristic lag-burst behavior.
PACS: 87.16.Dg – Membranes, bilayers, and vesicles / 87.15.Rn – Reactions and kinetics; polymerization / 87.16.Ac – Theory and modeling; computer simulation
© EDP Sciences, 2002
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