A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase
Susan Janes(University of California, Berkeley), David Mu(University of California, Berkeley), David E. Wemmer(University of California, Berkeley), Alan Jay Smith(University of California, Davis), Surinder Kaur(University of California, San Francisco), David Maltby(University of California, San Francisco), Alma L. Burlingame(University of California, San Francisco), Judith P. Klinman(University of California, Berkeley)
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Abstract
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.
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