Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
The first identified covalent flavoprotein, a component of mammalian succinate dehydrogenase, was reported 42 years ago. Since that time, more than 20 covalent flavoenzymes have been described, each possessing one of five modes of FAD or FMN linkage to protein. Despite the early identification of co...
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| Veröffentlicht in: | Protein science 1998-01, Vol.7 (1), p.7-20 |
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| creator | Mewies, Martin McIntire, William S. Scrutton, Nigel S. |
| description | The first identified covalent flavoprotein, a component of mammalian succinate dehydrogenase, was reported 42 years ago. Since that time, more than 20 covalent flavoenzymes have been described, each possessing one of five modes of FAD or FMN linkage to protein. Despite the early identification of covalent flavoproteins, the mechanisms of covalent bond formation and the roles of the covalent links are only recently being appreciated. The main focus of this review is, therefore, one of mechanism and function, in addition to surveying the types of linkage observed and the methods employed for their identification. Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge. |
| doi_str_mv | 10.1002/pro.5560070102 |
| format | Article |
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Since that time, more than 20 covalent flavoenzymes have been described, each possessing one of five modes of FAD or FMN linkage to protein. Despite the early identification of covalent flavoproteins, the mechanisms of covalent bond formation and the roles of the covalent links are only recently being appreciated. The main focus of this review is, therefore, one of mechanism and function, in addition to surveying the types of linkage observed and the methods employed for their identification. Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.5560070102</identifier><identifier>PMID: 9514256</identifier><language>eng</language><publisher>Bristol: Cold Spring Harbor Laboratory Press</publisher><subject>Amino Acid Sequence ; covalent flavoproteins ; Enzymes - chemistry ; flavin adenine dinucleotide ; flavin mononucleotide ; Flavin Mononucleotide - chemistry ; Flavin-Adenine Dinucleotide - chemistry ; flavinylation ; Flavoproteins - chemistry ; Flavoproteins - physiology ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Oxidation-Reduction ; Oxidoreductases - chemistry ; Oxidoreductases - metabolism ; redox cofactors</subject><ispartof>Protein science, 1998-01, Vol.7 (1), p.7-20</ispartof><rights>Copyright © 2008 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5012-8fc9a366004d6ab2181168f0c9d70828a0b7de8528b48ef91bfbe54355aef9333</citedby><cites>FETCH-LOGICAL-c5012-8fc9a366004d6ab2181168f0c9d70828a0b7de8528b48ef91bfbe54355aef9333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143808/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143808/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,1414,1430,27907,27908,45557,45558,46392,46816,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9514256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mewies, Martin</creatorcontrib><creatorcontrib>McIntire, William S.</creatorcontrib><creatorcontrib>Scrutton, Nigel S.</creatorcontrib><title>Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>The first identified covalent flavoprotein, a component of mammalian succinate dehydrogenase, was reported 42 years ago. Since that time, more than 20 covalent flavoenzymes have been described, each possessing one of five modes of FAD or FMN linkage to protein. Despite the early identification of covalent flavoproteins, the mechanisms of covalent bond formation and the roles of the covalent links are only recently being appreciated. The main focus of this review is, therefore, one of mechanism and function, in addition to surveying the types of linkage observed and the methods employed for their identification. Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge.</description><subject>Amino Acid Sequence</subject><subject>covalent flavoproteins</subject><subject>Enzymes - chemistry</subject><subject>flavin adenine dinucleotide</subject><subject>flavin mononucleotide</subject><subject>Flavin Mononucleotide - chemistry</subject><subject>Flavin-Adenine Dinucleotide - chemistry</subject><subject>flavinylation</subject><subject>Flavoproteins - chemistry</subject><subject>Flavoproteins - physiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - metabolism</subject><subject>redox cofactors</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EKkvLlRuST4gesvgjdmwOlaqlhUqFVqhI3CwnGbNGib3YyVbLjf-crHbpx4nTePTe_Gash9ArSuaUEPZuleJcCElIRShhT9CMllIXSsvvT9GMaEkLxaV6jl7k_JMQUlLGD9CBFrRkQs7Qn0Vc2w7CgO0w2GbZb5_RYdfZtQ_YthB8ANz6MDYdxMG3gN-en344xja0_1x9DPGR_vnLMR4ihvB700N-j2-WgJsxpS08D3aA7QrrnPUpH6FnznYZXu7rIfp2fnaz-FRcXn28WJxeFo0glBXKNdpyOX20bKWtGVWUSuVIo9uKKKYsqasWlGCqLhU4TWtXgyi5EHbqOOeH6GTHXY11D20z3ZJsZ1bJ9zZtTLTePFaCX5ofcW0YLbkiagK82QNS_DVCHkzvcwNdZwPEMZtKV1zzUk7G-c7YpJhzAne3hBKzDW3qo7kPbRp4_fC0O_s-pUnXO_3Wd7D5D81cf716wP4LWtWlhw</recordid><startdate>199801</startdate><enddate>199801</enddate><creator>Mewies, Martin</creator><creator>McIntire, William S.</creator><creator>Scrutton, Nigel S.</creator><general>Cold Spring Harbor Laboratory Press</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199801</creationdate><title>Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs</title><author>Mewies, Martin ; McIntire, William S. ; Scrutton, Nigel S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5012-8fc9a366004d6ab2181168f0c9d70828a0b7de8528b48ef91bfbe54355aef9333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>covalent flavoproteins</topic><topic>Enzymes - chemistry</topic><topic>flavin adenine dinucleotide</topic><topic>flavin mononucleotide</topic><topic>Flavin Mononucleotide - chemistry</topic><topic>Flavin-Adenine Dinucleotide - chemistry</topic><topic>flavinylation</topic><topic>Flavoproteins - chemistry</topic><topic>Flavoproteins - physiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - metabolism</topic><topic>redox cofactors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mewies, Martin</creatorcontrib><creatorcontrib>McIntire, William S.</creatorcontrib><creatorcontrib>Scrutton, Nigel S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mewies, Martin</au><au>McIntire, William S.</au><au>Scrutton, Nigel S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>1998-01</date><risdate>1998</risdate><volume>7</volume><issue>1</issue><spage>7</spage><epage>20</epage><pages>7-20</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>The first identified covalent flavoprotein, a component of mammalian succinate dehydrogenase, was reported 42 years ago. Since that time, more than 20 covalent flavoenzymes have been described, each possessing one of five modes of FAD or FMN linkage to protein. Despite the early identification of covalent flavoproteins, the mechanisms of covalent bond formation and the roles of the covalent links are only recently being appreciated. The main focus of this review is, therefore, one of mechanism and function, in addition to surveying the types of linkage observed and the methods employed for their identification. Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>9514256</pmid><doi>10.1002/pro.5560070102</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0961-8368 |
| ispartof | Protein science, 1998-01, Vol.7 (1), p.7-20 |
| issn | 0961-8368 1469-896X |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence covalent flavoproteins Enzymes - chemistry flavin adenine dinucleotide flavin mononucleotide Flavin Mononucleotide - chemistry Flavin-Adenine Dinucleotide - chemistry flavinylation Flavoproteins - chemistry Flavoproteins - physiology Models, Molecular Molecular Sequence Data Molecular Structure Oxidation-Reduction Oxidoreductases - chemistry Oxidoreductases - metabolism redox cofactors |
| title | Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs |
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