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Evidence for a Carbocation Intermediate in the Enzymatic Transformation of Leukotriene A4 Into Leukotriene B4

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Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 4

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 469))

Abstract

Leukotriene (LT) A4 hydrolase is a soluble enzyme that catalyzes the production of 5S,12R-dihydroxy-6, 14-cis-8,10-trans-eicosatetraenoic acid (LTB4) from the transient allylic epoxide 5S-trans-5, 6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid (LTA4). LTB4 elicits chemotaxis and adherence of leukocytes in only nM concentrations and is regarded as an important chemical mediator in a variety of inflammatory disorders.

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Refferences

  1. J.Z. Haeggström, A. Wetterholm, J.F. Medina, and B. Samuelsson, Leukotriene A4 hydrolase: Structural and functional properties of the active center, Journal of Lipid Mediators6:1 (1993).

    PubMed  Google Scholar 

  2. M. Minami, H. Bito, N. Ohishi, H. Tsuge, M. Miyano, M. Mori, H. Wada, H. Mutoh, S. Shimada, T. Izumi, K. Abe, and T. Shimizu, Leukotriene A4 hydrolase, a bifunctional enzyme: Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297, FEBS Lett.309:353 (1992).

    Article  PubMed  CAS  Google Scholar 

  3. M. Blomster, A. Wetterholm, M.J. Mueller, and J.Z. Haeggström, Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase, Eur. J. Biochem. 231:528 (1995).

    Article  PubMed  CAS  Google Scholar 

  4. M. Blomster Andberg, M. Hamberg, and J.Z. Haeggström, Mutation of tyrosine 383 in leukotriene A4 hydrolase allows formation of 5S,6S-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid: Implications for the epoxide hydrolase mechanism, J. Biol. Chem. 272:23057 (1997).

    Article  Google Scholar 

  5. P. Borgeat, and B. Samuelsson, Metabolism of arachidonic acid in polymorphonuclear leukocytes. Structural analysis of novel hydroxylated compounds, J. Biol. Chem. 254:7865 (1979).

    CAS  Google Scholar 

  6. J. Haeggström, J. Meijer, and O. Rådmark, Leukotriene A4: Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase, J. Biol. Chem. 261:6332 (1986).

    PubMed  Google Scholar 

  7. P. Borgeat, and B. Samuelsson, Arachidonic acid metabolism in polymorphonuclear leukocytes: unstable intermediate in formation of dihydroxy acids, Proc. Natl. Acad. Sci. USA 76:3213 (1979).

    Article  PubMed  CAS  Google Scholar 

  8. M. Arand, H. Wagner, and F. Oesch, Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase, J. Biol. Chem. 271:4223 (1996).

    Article  PubMed  CAS  Google Scholar 

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© 1999 Springer Science+Business Media New York

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Andberg, M., Hamberg, M., Haeggström, J.Z. (1999). Evidence for a Carbocation Intermediate in the Enzymatic Transformation of Leukotriene A4 Into Leukotriene B4 . In: Honn, K.V., Marnett, L.J., Nigam, S., Dennis, E.A. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 4. Advances in Experimental Medicine and Biology, vol 469. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4793-8_47

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  • DOI: https://doi.org/10.1007/978-1-4615-4793-8_47

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7171-7

  • Online ISBN: 978-1-4615-4793-8

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