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Mutation analysis of the human 5-lipoxygenase C-terminus: Support for a stabilizing C-terminal loop
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics .
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2005 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1749, no 1, 123-131 p.Article in journal (Refereed) Published
Abstract [en]

Lipoxygenases contain prosthetic iron, in human 5-lipoxygenase (5LO) the C-terminal isoleucine carboxylate constitutes one of five identified ligands. ATP is one of several factors determining 5LO activity. We compared properties of a series of 5LO C-terminal deletion mutants (one to six amino acid residues deleted). All mutants were enzymatically inactive (expected due to loss of iron), but expression yield (in E. coli) and affinity to ATP-agarose was markedly different. Deletion of up to four C-terminal residues was compatible with good expression and retained affinity to the ATP-column, as for wild-type 5LO. However when also the fifth residue was deleted (Asn-669) expression yield decreased and the affinity to ATP was markedly diminished. This was interpreted as a result of deranged structure and stability, due to loss of a hydrogen bond between Asn-669 and His-399. Mutagenesis of these residues supported this conclusion. In the structure of soybean lipoxygenase-1, a C-terminal loop was pointed out as important for correct orientation of the C-terminus. Accordingly, a hydrogen bond appears to stabilize such a C-terminal loop also in 5LO. © 2005 Elsevier B.V. All rights reserved.

Place, publisher, year, edition, pages
2005. Vol. 1749, no 1, 123-131 p.
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Natural Sciences
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URN: urn:nbn:se:liu:diva-29961DOI: 10.1016/j.bbapap.2005.03.005Local ID: 15388OAI: oai:DiVA.org:liu-29961DiVA: diva2:250780
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2017-12-13

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Persson, Bengt

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  • apa
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