Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate

P. Høyrup; K. Jørgensen; O. G. Mouritsen

doi:10.1209/epl/i2002-00483-y

Phospholipase A₂ - An enzyme that is sensitive to the physics of its substrate

P. Høyrup^*, K. Jørgensen, O. G. Mouritsen

^*Corresponding author af dette arbejde

25 Citationer (Scopus)

Abstract

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 interracial 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.

Originalsprog	Engelsk
Tidsskrift	Europhysics Letters
Vol/bind	57
Udgave nummer	3
Sider (fra-til)	464-470
Antal sider	7
ISSN	0295-5075
DOI	https://doi.org/10.1209/epl/i2002-00483-y
Status	Udgivet - 19 aug. 2002

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Citationsformater

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abstract = "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 interracial 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.",

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AB - 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 interracial 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.

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