Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group
In addition to the metal ion, copper-containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until no...
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| Veröffentlicht in: | FEBS letters 1984-05, Vol.170 (2), p.305-309 |
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| creator | Lobenstein-Verbeek, C.L. Jongejan, J.A. Frank, J. Duine, J.A. |
| description | In addition to the metal ion, copper-containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until now the coenzyme PQQ has been found in several bacterial dehydrogenases. Thus the finding reported here is the first example of a quinoprotein oxidoreductase discovered in a eukaryotic organism. |
| doi_str_mv | 10.1016/0014-5793(84)81333-2 |
| format | Article |
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We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until now the coenzyme PQQ has been found in several bacterial dehydrogenases. Thus the finding reported here is the first example of a quinoprotein oxidoreductase discovered in a eukaryotic organism.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(84)81333-2</identifier><identifier>PMID: 6723967</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amine Oxidase (Copper-Containing) ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Bovine serum amine oxidase ; Cattle ; Chemical Phenomena ; Chemistry ; Chromatography, High Pressure Liquid ; Coenzymes ; Copper-containing amine oxidase ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Oxidoreductases ; Oxidoreductases Acting on CH-NH Group Donors - antagonists & inhibitors ; Oxidoreductases Acting on CH-NH Group Donors - blood ; Phenylhydrazines - pharmacology ; PQQ Cofactor ; Prosthetic group ; pyrroloquinoline quinone ; Pyrroloquinoline quinone (PQQ) ; Quinolines - blood ; Quinoprotein ; serum ; Spectrophotometry</subject><ispartof>FEBS letters, 1984-05, Vol.170 (2), p.305-309</ispartof><rights>1984</rights><rights>FEBS Letters 170 (1984) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5922-524e97702e540b92c5fc1afd11120ad4e1d5c93b3b018ccd35771f8f350e49bb3</citedby><cites>FETCH-LOGICAL-c5922-524e97702e540b92c5fc1afd11120ad4e1d5c93b3b018ccd35771f8f350e49bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(84)81333-2$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8989291$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6723967$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lobenstein-Verbeek, C.L.</creatorcontrib><creatorcontrib>Jongejan, J.A.</creatorcontrib><creatorcontrib>Frank, J.</creatorcontrib><creatorcontrib>Duine, J.A.</creatorcontrib><title>Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>In addition to the metal ion, copper-containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until now the coenzyme PQQ has been found in several bacterial dehydrogenases. Thus the finding reported here is the first example of a quinoprotein oxidoreductase discovered in a eukaryotic organism.</description><subject>Amine Oxidase (Copper-Containing)</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bovine serum amine oxidase</subject><subject>Cattle</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Coenzymes</subject><subject>Copper-containing amine oxidase</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Oxidoreductases</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - antagonists & inhibitors</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - blood</subject><subject>Phenylhydrazines - pharmacology</subject><subject>PQQ Cofactor</subject><subject>Prosthetic group</subject><subject>pyrroloquinoline quinone</subject><subject>Pyrroloquinoline quinone (PQQ)</subject><subject>Quinolines - blood</subject><subject>Quinoprotein</subject><subject>serum</subject><subject>Spectrophotometry</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1v1DAQQC0EKkvhH4DkA0JwCPgzsTkg0aoLSJWgElyxHHvSGsXJ1k4Wll-P013tETjZnnkznnkIPaXkNSW0fkMIFZVsNH-pxCtFOecVu4dWVDW84qJW99HqiDxEj3L-QcpbUX2CTuqGcV03K_T9bNyGAXCGNEds43IffwVvM7zFFkcbo-2DHTAMv3cR8I0t-DV249b2MEz9DrfjPHj85eoK24w3aczTDUzB4es0zpvH6EFn-wxPDucp-ra--Hr-sbr8_OHT-fvLyknNWCWZAN00hIEUpNXMyc5R23lKKSPWC6BeOs1b3pYFnPNcNg3tVMclAaHblp-iF_u-ZYDbGfJkYsgO-t4OMM7ZKEoapoqZf4GUKyVVrQoo9qArK-UEndmkEG3aGUrM4t8scs0i1yhh7vwbVsqeHfrPbQR_LDoIL_nnh7zNzvZdsoML-YgprTTTtGDrPfYz9LD7r6_N-uKMLYklrsRddJnn3b4RFPvbAMlkF2Bw4EMCNxk_hr8v9AevyLQt</recordid><startdate>19840521</startdate><enddate>19840521</enddate><creator>Lobenstein-Verbeek, C.L.</creator><creator>Jongejan, J.A.</creator><creator>Frank, J.</creator><creator>Duine, J.A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19840521</creationdate><title>Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group</title><author>Lobenstein-Verbeek, C.L. ; Jongejan, J.A. ; Frank, J. ; Duine, J.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5922-524e97702e540b92c5fc1afd11120ad4e1d5c93b3b018ccd35771f8f350e49bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amine Oxidase (Copper-Containing)</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bovine serum amine oxidase</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Coenzymes</topic><topic>Copper-containing amine oxidase</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Oxidoreductases</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - antagonists & inhibitors</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - blood</topic><topic>Phenylhydrazines - pharmacology</topic><topic>PQQ Cofactor</topic><topic>Prosthetic group</topic><topic>pyrroloquinoline quinone</topic><topic>Pyrroloquinoline quinone (PQQ)</topic><topic>Quinolines - blood</topic><topic>Quinoprotein</topic><topic>serum</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lobenstein-Verbeek, C.L.</creatorcontrib><creatorcontrib>Jongejan, J.A.</creatorcontrib><creatorcontrib>Frank, J.</creatorcontrib><creatorcontrib>Duine, J.A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lobenstein-Verbeek, C.L.</au><au>Jongejan, J.A.</au><au>Frank, J.</au><au>Duine, J.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1984-05-21</date><risdate>1984</risdate><volume>170</volume><issue>2</issue><spage>305</spage><epage>309</epage><pages>305-309</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>In addition to the metal ion, copper-containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until now the coenzyme PQQ has been found in several bacterial dehydrogenases. Thus the finding reported here is the first example of a quinoprotein oxidoreductase discovered in a eukaryotic organism.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>6723967</pmid><doi>10.1016/0014-5793(84)81333-2</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1984-05, Vol.170 (2), p.305-309 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amine Oxidase (Copper-Containing) Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Bovine serum amine oxidase Cattle Chemical Phenomena Chemistry Chromatography, High Pressure Liquid Coenzymes Copper-containing amine oxidase Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Oxidoreductases Oxidoreductases Acting on CH-NH Group Donors - antagonists & inhibitors Oxidoreductases Acting on CH-NH Group Donors - blood Phenylhydrazines - pharmacology PQQ Cofactor Prosthetic group pyrroloquinoline quinone Pyrroloquinoline quinone (PQQ) Quinolines - blood Quinoprotein serum Spectrophotometry |
| title | Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group |
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