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Calcium Binding Site of 5-Lipoxygenase

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Part of the book series: Medical Science Symposia Series ((MSSS,volume 16))

Abstract

5-lipoxygenase (5LO) catalyzes the formation of leukotriene A4 from arachidonic acid. Factors determining 5LO enzyme activity are calcium, phosphatidylcholine (membranes), ATP, the cellular redox status, and phosphorylation events. Ionophores (increase intracellular Ca2+) are effective, and Ca2+ also activates 5LO in vitro. 5LO binds Ca2+ in a reversible manner with a Kd close to 6 µM and maximum binding around two Ca2+ per 5LO [1]. While examining the Ca2+ binding site on 5LO, we noticed similarity between the 5LO N-terminal domain, and calcium binding C2-domains of for example cPLA2. Here, we describe that the N-terminal domain of 5LO binds calcium and mediates calcium stimulation of enzyme activity.

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References

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© 2001 Springer Science+Business Media Dordrecht

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Hammarberg, T., Provost, P., Reddy, K.V., Persson, B., Rådmark, O. (2001). Calcium Binding Site of 5-Lipoxygenase. In: Samuelsson, B., Paoletti, R., Folco, G.C., Granström, E., Nicosia, S. (eds) Advances in Prostaglandin and Leukotriene Research. Medical Science Symposia Series, vol 16. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9721-0_3

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  • DOI: https://doi.org/10.1007/978-94-015-9721-0_3

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-90-481-5881-2

  • Online ISBN: 978-94-015-9721-0

  • eBook Packages: Springer Book Archive

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