A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase
An active site, cofactor-containing peptide has been obtained in high yield from bovine serum amine oxidase. Sequencing of this pentapeptide indicates: Leu-Asn-XAsp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1990-05, Vol.248 (4958), p.981-987 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Janes, Susan M. Mu, David Wemmer, David Smith, Alan J. Kaur, Surinder Maltby, David Burlingame, Alma L. Klinman, Judith P. |
| 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-XAsp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6hydroxydopa. 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. |
| doi_str_mv | 10.1126/science.2111581 |
| format | Article |
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Sequencing of this pentapeptide indicates: Leu-Asn-XAsp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6hydroxydopa. 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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.2111581</identifier><identifier>PMID: 2111581</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Active sites ; Amine Oxidase (Copper-Containing) ; Amines ; Amino Acid Sequence ; Analysis ; Analytical, structural and metabolic biochemistry ; Animals ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Cattle ; Cells ; Cells (Biology) ; Chemical research ; Chemistry ; Copper ; Dihydroxyphenylalanine - analogs & derivatives ; Dihydroxyphenylalanine - metabolism ; Enzymes ; Enzymes and enzyme inhibitors ; Eukaryotes ; Eukaryotic cells ; Fundamental and applied biological sciences. Psychology ; Hydrogen ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Mass spectroscopy ; Molecular Sequence Data ; Oxidases ; Oxidoreductases ; Oxidoreductases - metabolism ; Oxidoreductases Acting on CH-NH Group Donors - blood ; Oxidoreductases Acting on CH-NH Group Donors - metabolism ; Peptide Fragments - analysis ; Peptide Fragments - chemical synthesis ; Peptides ; Phenylhydrazines ; Quinones ; Quinones - metabolism ; Research Article ; Solvents ; Spectrophotometry, Ultraviolet ; Ungulates</subject><ispartof>Science (American Association for the Advancement of Science), 1990-05, Vol.248 (4958), p.981-987</ispartof><rights>Copyright 1990 American Association for the Advancement of Science</rights><rights>1991 INIST-CNRS</rights><rights>COPYRIGHT 1990 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1990 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science May 25, 1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c735t-cd69b01563bb42e059af564832b043df1cf1a33e7633e7550c7689502cdb32063</citedby><cites>FETCH-LOGICAL-c735t-cd69b01563bb42e059af564832b043df1cf1a33e7633e7550c7689502cdb32063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2874400$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2874400$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19261056$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2111581$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Janes, Susan M.</creatorcontrib><creatorcontrib>Mu, David</creatorcontrib><creatorcontrib>Wemmer, David</creatorcontrib><creatorcontrib>Smith, Alan J.</creatorcontrib><creatorcontrib>Kaur, Surinder</creatorcontrib><creatorcontrib>Maltby, David</creatorcontrib><creatorcontrib>Burlingame, Alma L.</creatorcontrib><creatorcontrib>Klinman, Judith P.</creatorcontrib><title>A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><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-XAsp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6hydroxydopa. 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.</description><subject>Active sites</subject><subject>Amine Oxidase (Copper-Containing)</subject><subject>Amines</subject><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cells</subject><subject>Cells (Biology)</subject><subject>Chemical research</subject><subject>Chemistry</subject><subject>Copper</subject><subject>Dihydroxyphenylalanine - analogs & derivatives</subject><subject>Dihydroxyphenylalanine - metabolism</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Eukaryotes</subject><subject>Eukaryotic cells</subject><subject>Fundamental and applied biological sciences. 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Mu, David ; Wemmer, David ; Smith, Alan J. ; Kaur, Surinder ; Maltby, David ; Burlingame, Alma L. ; Klinman, Judith P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c735t-cd69b01563bb42e059af564832b043df1cf1a33e7633e7550c7689502cdb32063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Active sites</topic><topic>Amine Oxidase (Copper-Containing)</topic><topic>Amines</topic><topic>Amino Acid Sequence</topic><topic>Analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cells</topic><topic>Cells (Biology)</topic><topic>Chemical research</topic><topic>Chemistry</topic><topic>Copper</topic><topic>Dihydroxyphenylalanine - analogs & derivatives</topic><topic>Dihydroxyphenylalanine - metabolism</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Eukaryotes</topic><topic>Eukaryotic cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mass Spectrometry</topic><topic>Mass spectroscopy</topic><topic>Molecular Sequence Data</topic><topic>Oxidases</topic><topic>Oxidoreductases</topic><topic>Oxidoreductases - metabolism</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - blood</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - metabolism</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptides</topic><topic>Phenylhydrazines</topic><topic>Quinones</topic><topic>Quinones - metabolism</topic><topic>Research Article</topic><topic>Solvents</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Janes, Susan M.</creatorcontrib><creatorcontrib>Mu, David</creatorcontrib><creatorcontrib>Wemmer, David</creatorcontrib><creatorcontrib>Smith, Alan J.</creatorcontrib><creatorcontrib>Kaur, Surinder</creatorcontrib><creatorcontrib>Maltby, David</creatorcontrib><creatorcontrib>Burlingame, Alma L.</creatorcontrib><creatorcontrib>Klinman, Judith P.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: High School</collection><collection>Gale in Context : Biography</collection><collection>Opposing Viewpoints Resource Center</collection><collection>Gale In Context: Canada</collection><collection>ProQuest Social Sciences Premium Collection【Remote access available】</collection><collection>ProQuest Central (Corporate)</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Education Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Social Science Premium Collection</collection><collection>Advanced Technologies & Aerospace Database (1962 - 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Sequencing of this pentapeptide indicates: Leu-Asn-XAsp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6hydroxydopa. 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.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>2111581</pmid><doi>10.1126/science.2111581</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1990-05, Vol.248 (4958), p.981-987 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743372920 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Active sites Amine Oxidase (Copper-Containing) Amines Amino Acid Sequence Analysis Analytical, structural and metabolic biochemistry Animals Binding Sites Biochemistry Biological and medical sciences Cattle Cells Cells (Biology) Chemical research Chemistry Copper Dihydroxyphenylalanine - analogs & derivatives Dihydroxyphenylalanine - metabolism Enzymes Enzymes and enzyme inhibitors Eukaryotes Eukaryotic cells Fundamental and applied biological sciences. Psychology Hydrogen Magnetic Resonance Spectroscopy Mass Spectrometry Mass spectroscopy Molecular Sequence Data Oxidases Oxidoreductases Oxidoreductases - metabolism Oxidoreductases Acting on CH-NH Group Donors - blood Oxidoreductases Acting on CH-NH Group Donors - metabolism Peptide Fragments - analysis Peptide Fragments - chemical synthesis Peptides Phenylhydrazines Quinones Quinones - metabolism Research Article Solvents Spectrophotometry, Ultraviolet Ungulates |
| title | A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-12T01%3A32%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20New%20Redox%20Cofactor%20in%20Eukaryotic%20Enzymes:%206-Hydroxydopa%20at%20the%20Active%20Site%20of%20Bovine%20Serum%20Amine%20Oxidase&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Janes,%20Susan%20M.&rft.date=1990-05-25&rft.volume=248&rft.issue=4958&rft.spage=981&rft.epage=987&rft.pages=981-987&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.2111581&rft_dat=%3Cgale_proqu%3EA9067057%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213561806&rft_id=info:pmid/2111581&rft_galeid=A9067057&rft_jstor_id=2874400&rfr_iscdi=true |