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

Janes, Susan M., Mu, David, Wemmer, David, Smith, Alan J., Kaur, Surinder, Maltby, David, Burlingame, Alma L., Klinman, Judith P.·1990·Science

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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Metadata

Authors
Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., & Klinman, J. P.
Venue
Science
Published
1990-05-25
Volume
248
Issue
4958
Pages
981-987
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2069350944
Cited by
659
References
0
FWCI
53.83
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase. https://app.cochat.ai/papers/10.1126/science.2111581
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Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., & Klinman, J. P. (1990). A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase. Science. https://doi.org/10.1126/science.2111581

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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