Role of lipid protrusions in the function of interfacial enzymes

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Role of lipid protrusions in the function of interfacial enzymes. / Halperin, Avi; Mouritsen, Ole G.

In: European Biophysics Journal, Vol. 34, No. 7, 01.10.2005, p. 967-971.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Halperin, A & Mouritsen, OG 2005, 'Role of lipid protrusions in the function of interfacial enzymes', European Biophysics Journal, vol. 34, no. 7, pp. 967-971. https://doi.org/10.1007/s00249-005-0466-z

APA

Halperin, A., & Mouritsen, O. G. (2005). Role of lipid protrusions in the function of interfacial enzymes. European Biophysics Journal, 34(7), 967-971. https://doi.org/10.1007/s00249-005-0466-z

Vancouver

Halperin A, Mouritsen OG. Role of lipid protrusions in the function of interfacial enzymes. European Biophysics Journal. 2005 Oct 1;34(7):967-971. https://doi.org/10.1007/s00249-005-0466-z

Author

Halperin, Avi ; Mouritsen, Ole G. / Role of lipid protrusions in the function of interfacial enzymes. In: European Biophysics Journal. 2005 ; Vol. 34, No. 7. pp. 967-971.

Bibtex

@article{d64ba2e100ac41c788186bf43e0988f9,
title = "Role of lipid protrusions in the function of interfacial enzymes",
abstract = "Secretory phospholipase A2 (sPLA2) is a class of interfacially active enzymes that selectively hydrolyze lipid molecules organized at interfaces like membranes. We present a simple theoretical model that relates the sPLA2 action to the protrusions of the lipid molecules. The model explains (1) the observed enhancement of enzymatic activity by lipids with flexible, neutral, water-soluble polymers linked to their head groups and (2) the lag-burst kinetics of sPLA2. It yields qualitative predictions of the effect of the initial composition of the membrane, the molecular weight of the polymer, and the composition of the hydrolysis products.",
author = "Avi Halperin and Mouritsen, {Ole G.}",
year = "2005",
month = "10",
day = "1",
doi = "10.1007/s00249-005-0466-z",
language = "English",
volume = "34",
pages = "967--971",
journal = "European Biophysics Journal",
issn = "0175-7571",
publisher = "Springer",
number = "7",

}

RIS

TY - JOUR

T1 - Role of lipid protrusions in the function of interfacial enzymes

AU - Halperin, Avi

AU - Mouritsen, Ole G.

PY - 2005/10/1

Y1 - 2005/10/1

N2 - Secretory phospholipase A2 (sPLA2) is a class of interfacially active enzymes that selectively hydrolyze lipid molecules organized at interfaces like membranes. We present a simple theoretical model that relates the sPLA2 action to the protrusions of the lipid molecules. The model explains (1) the observed enhancement of enzymatic activity by lipids with flexible, neutral, water-soluble polymers linked to their head groups and (2) the lag-burst kinetics of sPLA2. It yields qualitative predictions of the effect of the initial composition of the membrane, the molecular weight of the polymer, and the composition of the hydrolysis products.

AB - Secretory phospholipase A2 (sPLA2) is a class of interfacially active enzymes that selectively hydrolyze lipid molecules organized at interfaces like membranes. We present a simple theoretical model that relates the sPLA2 action to the protrusions of the lipid molecules. The model explains (1) the observed enhancement of enzymatic activity by lipids with flexible, neutral, water-soluble polymers linked to their head groups and (2) the lag-burst kinetics of sPLA2. It yields qualitative predictions of the effect of the initial composition of the membrane, the molecular weight of the polymer, and the composition of the hydrolysis products.

UR - http://www.scopus.com/inward/record.url?scp=26444578399&partnerID=8YFLogxK

U2 - 10.1007/s00249-005-0466-z

DO - 10.1007/s00249-005-0466-z

M3 - Journal article

C2 - 15883844

AN - SCOPUS:26444578399

VL - 34

SP - 967

EP - 971

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - 7

ER -

ID: 230985105