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  • 1
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    A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-25
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janes, S M -- Mu, D -- Wemmer, D -- Smith, A J -- Kaur, S -- Maltby, D -- Burlingame, A L -- Klinman, J P -- GM 39296/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 May 25;248(4958):981-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2111581" target="_blank"〉PubMed〈/a〉
    Keywords: *Amine Oxidase (Copper-Containing) ; Amino Acid Sequence ; Animals ; Binding Sites ; Cattle ; Copper ; Dihydroxyphenylalanine/*analogs & derivatives/metabolism ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Molecular Sequence Data ; Oxidoreductases/metabolism ; Oxidoreductases Acting on CH-NH Group Donors/blood/*metabolism ; Peptide Fragments/analysis/chemical synthesis ; Quinones/metabolism ; Spectrophotometry, Ultraviolet
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: A previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra, and resonance Raman studies showed that this cofactor is a quinone. Its structure is derived from the crosslinking of the epsilon-amino group of a peptidyl lysine with the modified side chain of a tyrosyl residue, and it has been designated lysine tyrosylquinone. This quinone appears to be the only example of a mammalian cofactor formed from the crosslinking of two amino acid side chains. This discovery expands the range of known quino-cofactor structures and has implications for the mechanism of their biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, S X -- Mure, M -- Medzihradszky, K F -- Burlingame, A L -- Brown, D E -- Dooley, D M -- Smith, A J -- Kagan, H M -- Klinman, J P -- GM27659/GM/NIGMS NIH HHS/ -- GM39296/GM/NIGMS NIH HHS/ -- P41 RR01614/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1078-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aorta/enzymology ; Binding Sites ; Cattle ; Chromatography, High Pressure Liquid ; Lysine/*analogs & derivatives/chemistry/metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein-Lysine 6-Oxidase/*chemistry/genetics/isolation & purification/metabolism ; Quinones/*chemistry/metabolism ; Spectrophotometry, Ultraviolet ; Spectrum Analysis, Raman
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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    PAPER CURRENT
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