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

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Standard

Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate. / Høyrup, P.; Jørgensen, K.; Mouritsen, O. G.

In: Europhysics Letters, Vol. 57, No. 3, 19.08.2002, p. 464-470.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Høyrup, P, Jørgensen, K & Mouritsen, OG 2002, 'Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate', Europhysics Letters, vol. 57, no. 3, pp. 464-470. https://doi.org/10.1209/epl/i2002-00483-y

APA

Høyrup, P., Jørgensen, K., & Mouritsen, O. G. (2002). Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate. Europhysics Letters, 57(3), 464-470. https://doi.org/10.1209/epl/i2002-00483-y

Vancouver

Høyrup P, Jørgensen K, Mouritsen OG. Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate. Europhysics Letters. 2002 Aug 19;57(3):464-470. https://doi.org/10.1209/epl/i2002-00483-y

Author

Høyrup, P. ; Jørgensen, K. ; Mouritsen, O. G. / Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate. In: Europhysics Letters. 2002 ; Vol. 57, No. 3. pp. 464-470.

Bibtex

@article{d75d21dba67842ee9a540c27b65fa1bd,
title = "Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate",
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.",
author = "P. H{\o}yrup and K. J{\o}rgensen and Mouritsen, {O. G.}",
year = "2002",
month = aug,
day = "19",
doi = "10.1209/epl/i2002-00483-y",
language = "English",
volume = "57",
pages = "464--470",
journal = "Lettere Al Nuovo Cimento",
issn = "0295-5075",
publisher = "IOP Publishing",
number = "3",

}

RIS

TY - JOUR

T1 - Phospholipase A2 - An enzyme that is sensitive to the physics of its substrate

AU - Høyrup, P.

AU - Jørgensen, K.

AU - Mouritsen, O. G.

PY - 2002/8/19

Y1 - 2002/8/19

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=1842696213&partnerID=8YFLogxK

U2 - 10.1209/epl/i2002-00483-y

DO - 10.1209/epl/i2002-00483-y

M3 - Journal article

AN - SCOPUS:1842696213

VL - 57

SP - 464

EP - 470

JO - Lettere Al Nuovo Cimento

JF - Lettere Al Nuovo Cimento

SN - 0295-5075

IS - 3

ER -

ID: 230986604