Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase
Microsomes from the marine mussel Mytilusedulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1985-03, Vol.127 (3), p.773-778 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Kurelec, Branko |
| description | Microsomes from the marine mussel
Mytilusedulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified pig liver FAD-containing monooxygenase (EC 1.14.13.8, dimethylaniline monooxygenase). The exposure of mussels to Diesel-2 oil does not induce the enzyme activity. These results are discussed in terms of possible ecological and environmental significance. |
| doi_str_mv | 10.1016/S0006-291X(85)80010-3 |
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Mytilusedulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified pig liver FAD-containing monooxygenase (EC 1.14.13.8, dimethylaniline monooxygenase). The exposure of mussels to Diesel-2 oil does not induce the enzyme activity. These results are discussed in terms of possible ecological and environmental significance.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(85)80010-3</identifier><identifier>PMID: 3985956</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amines - metabolism ; Animals ; Applied sciences ; Benzo(a)pyrene - pharmacology ; Bivalvia - enzymology ; Digestive System - enzymology ; Exact sciences and technology ; Fuel Oils ; Hydrogen-Ion Concentration ; Marine ; Microsomes - enzymology ; Microsomes, Liver - enzymology ; Mytilus edulis ; NADP - metabolism ; Other techniques and industries ; Oxidation-Reduction ; Oxygenases - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1985-03, Vol.127 (3), p.773-778</ispartof><rights>1985 Academic Press, Inc.</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-a34cca2626a07a50c633dc646c9f199b58079ab5cb0fd638e6cbdd0faac1f1f53</citedby><cites>FETCH-LOGICAL-c420t-a34cca2626a07a50c633dc646c9f199b58079ab5cb0fd638e6cbdd0faac1f1f53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(85)80010-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8027780$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3985956$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kurelec, Branko</creatorcontrib><title>Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Microsomes from the marine mussel
Mytilusedulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified pig liver FAD-containing monooxygenase (EC 1.14.13.8, dimethylaniline monooxygenase). The exposure of mussels to Diesel-2 oil does not induce the enzyme activity. These results are discussed in terms of possible ecological and environmental significance.</description><subject>Amines - metabolism</subject><subject>Animals</subject><subject>Applied sciences</subject><subject>Benzo(a)pyrene - pharmacology</subject><subject>Bivalvia - enzymology</subject><subject>Digestive System - enzymology</subject><subject>Exact sciences and technology</subject><subject>Fuel Oils</subject><subject>Hydrogen-Ion Concentration</subject><subject>Marine</subject><subject>Microsomes - enzymology</subject><subject>Microsomes, Liver - enzymology</subject><subject>Mytilus edulis</subject><subject>NADP - metabolism</subject><subject>Other techniques and industries</subject><subject>Oxidation-Reduction</subject><subject>Oxygenases - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EKkvhI1TyASE4BMZJ7CQnhKryRyriAEjcrMlkXAyJXeJk1f32eLurvfY0Gs3vzYzeE-JCwVsFyrz7DgCmKDv163Wr37QACorqkdgo6KAoFdSPxeaEPBXPUvqTGVWb7kycVV2rO2024u_VHY1r8luWSIvf4uJjkNFJnOOUG5I4-cBJ-iCX3ywnnHMrpzUlHuXX3eKzWvKwjj7JficdDgXFsKAPPtzIKYYY73Y3HDDxc_HE4Zj4xbGei58fr35cfi6uv336cvnhuqC6hKXAqibC0pQGoUENZKpqIFMb6pzqul630HTYa-rBDaZq2VA_DOAQSTnldHUuXh323s7x38ppsZNPxOOIgeOabGNAa6ObB0FVl2VTlXtQH0CaY0ozO3s7-2zFziqw-zTsfRp2b7Vttb1Pw1ZZd3E8sPYTDyfV0f48f3mcYyIc3YyBfDphLZRN00LG3h8wzq5tPc82kedAPPiZabFD9A888h95q6j_</recordid><startdate>19850329</startdate><enddate>19850329</enddate><creator>Kurelec, Branko</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7U7</scope><scope>C1K</scope><scope>F1W</scope><scope>H97</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19850329</creationdate><title>Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase</title><author>Kurelec, Branko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-a34cca2626a07a50c633dc646c9f199b58079ab5cb0fd638e6cbdd0faac1f1f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Amines - metabolism</topic><topic>Animals</topic><topic>Applied sciences</topic><topic>Benzo(a)pyrene - pharmacology</topic><topic>Bivalvia - enzymology</topic><topic>Digestive System - enzymology</topic><topic>Exact sciences and technology</topic><topic>Fuel Oils</topic><topic>Hydrogen-Ion Concentration</topic><topic>Marine</topic><topic>Microsomes - enzymology</topic><topic>Microsomes, Liver - enzymology</topic><topic>Mytilus edulis</topic><topic>NADP - metabolism</topic><topic>Other techniques and industries</topic><topic>Oxidation-Reduction</topic><topic>Oxygenases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kurelec, Branko</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>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kurelec, Branko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1985-03-29</date><risdate>1985</risdate><volume>127</volume><issue>3</issue><spage>773</spage><epage>778</epage><pages>773-778</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Microsomes from the marine mussel
Mytilusedulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified pig liver FAD-containing monooxygenase (EC 1.14.13.8, dimethylaniline monooxygenase). The exposure of mussels to Diesel-2 oil does not induce the enzyme activity. These results are discussed in terms of possible ecological and environmental significance.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3985956</pmid><doi>10.1016/S0006-291X(85)80010-3</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1985-03, Vol.127 (3), p.773-778 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amines - metabolism Animals Applied sciences Benzo(a)pyrene - pharmacology Bivalvia - enzymology Digestive System - enzymology Exact sciences and technology Fuel Oils Hydrogen-Ion Concentration Marine Microsomes - enzymology Microsomes, Liver - enzymology Mytilus edulis NADP - metabolism Other techniques and industries Oxidation-Reduction Oxygenases - metabolism |
| title | Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase |
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