Dimerization of human 5-lipoxygenase
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Date
2011-12
Publication Type
Journal Article
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yes
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Abstract
Human 5-lipoxygenase (5-LO) can form dimers as shown here via native gel electrophoresis, gel filtration chromatography and LILBID (laser induced liquid bead ion desorption) mass spectrometry. After glutathionylation of 5-LO by diamide/glutathione treatment, dimeric 5-LO was no longer detectable and 5-LO almost exclusively exists in the monomeric form which showed full catalytic activity. Incubation of 5-LO with diamide alone led to a disulfide-bridged dimer and to oligomer formation which displays a strongly reduced catalytic activity. The bioinformatic analysis of the 5-LO surface for putative protein-protein interaction domains and molecular modeling of the dimer interface suggests a head to tail orientation of the dimer which also explains the localization of previously reported ATP binding sites. This interface domain was confirmed by the observation that 5-LO dimer formation and inhibition of activity by diamide was largely prevented when four cysteines (C159S, C300S, C416S, C418S) in this domain were mutated to serines. © 2011 by Walter de Gruyter Berlin Boston 2011.
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Publication status
published
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Book title
Journal / series
Volume
392 (12)
Pages / Article No.
1097 - 1111
Publisher
De Gruyter
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Edition / version
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Date collected
Date created
Subject
Diamide; 5-lipoxygenase; LILBID; Leukotrienes; Molecular modeling
Organisational unit
03852 - Schneider, Gisbert / Schneider, Gisbert
Notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher