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Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury pp 47–50Cite as

Effects of Anions on the Peptidase Activity of Leukotriene A4 Hydrolase

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Part of the book series: Developments in Oncology ((DION,volume 71))

Abstract

Leukotriene A4 (LTA4) hydrolase catalyzes the hydrolysis of the unstable epoxide LTA4 into the proinflammatory substance LTB4 (review in 1). Recently a sequence similarity between LTA4 hydrolase and certain zinc metalloenzymes, e.g. aminopeptidase M and thermolysin, was demonstrated, revealing the presence of a zinc binding motif in the enzyme (2, 3). Accordingly, LTA4 hydrolase was found to contain one atom of zinc per enzyme molecule, essential for the catalytic activity (4–6) and also to exhibit peptidase activity towards synthetic substrates (5–7). Here we report some effects of anions on this novel enzymatic activity of LTA4 hydrolase.

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Author information

Authors and Affiliations

  1. Department of Physiological Chemistry, Karolinska Institutet, S-104 01, Stockholm, Sweden

    A. Wetterholm & J. Z. HaeggströM

Authors
  1. A. Wetterholm
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  2. J. Z. HaeggströM
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Editor information

Editors and Affiliations

  1. Department of Gynecological Endocrinology, Klinikum Steglitz, Free University Berlin, Berlin, Germany

    Santosh Nigam

  2. Department of Radiation Oncology, Wayne State University, Detroit, MI, USA

    Kenneth V. Honn

  3. Department of Biochemistry, Vanderbilt University, Nashville, TN, USA

    Lawrence J. Marnett

  4. Department of Radiation Biochemistry, Armed Forces Radiobiology Research Institute, Bethesda, MD, USA

    Thomas L. Walden Jr.

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© 1993 Springer Science+Business Media New York

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Wetterholm, A., HaeggströM, J.Z. (1993). Effects of Anions on the Peptidase Activity of Leukotriene A4 Hydrolase. In: Nigam, S., Honn, K.V., Marnett, L.J., Walden, T.L. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury. Developments in Oncology, vol 71. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3520-1_11

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  • DOI: https://doi.org/10.1007/978-1-4615-3520-1_11

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6562-4

  • Online ISBN: 978-1-4615-3520-1

  • eBook Packages: Springer Book Archive

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