| Literature DB >> 2111581 |
S M Janes1, D Mu, D Wemmer, A J Smith, S Kaur, D Maltby, A L Burlingame, J P Klinman.
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.Entities:
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Year: 1990 PMID： 2111581 DOI： 10.1126/science.2111581
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728