A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase

DOI Web Site 被引用文献35件
  • Susan M. Janes
    Department of Chemistry, University of California, Berkeley, CA 94720.
  • David Mu
    Department of Chemistry, University of California, Berkeley, CA 94720.
  • David Wemmer
    Department of Chemistry, University of California, Berkeley, CA 94720.
  • Alan J. Smith
    Protein Structure Laboratory, Department of Biochemistry and Biophysics, University of California, Davis, CA 95616.
  • Surinder Kaur
    Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
  • David Maltby
    Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
  • Alma L. Burlingame
    Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
  • Judith P. Klinman
    Department of Chemistry, University of California, Berkeley, CA 94720.

抄録

<jats:p>An active site, cofactor-containing peptide has been obtained in high yield from bovine serum amine oxidase. Sequencing of this pentapeptide indicates: Leu-Asn-X-Asp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6-hydroxydopa. This result indicates that, contrary to previous proposals, pyrroloquinoline quinone is not the active site cofactor in mammalian copper amine oxidases. Although 6-hydroxydopa has been implicated in neurotoxicity, the data presented suggest that this compound has a functional role at an enzyme active site.</jats:p>

収録刊行物

  • Science

    Science 248 (4958), 981-987, 1990-05-25

    American Association for the Advancement of Science (AAAS)

被引用文献 (35)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ