Recent Advances in Radical SAM Enzymology: New Structures and Mechanisms
The radical S-adenosylmethionine (SAM) superfamily of enzymes catalyzes an amazingly diverse variety of reactions ranging from simple hydrogen abstraction to complicated multistep rearrangements and insertions. The reactions they catalyze are important for a broad range of biological functions, incl...
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| Veröffentlicht in: | ACS chemical biology 2014-09, Vol.9 (9), p.1929-1938 |
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| container_issue | 9 |
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| container_title | ACS chemical biology |
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| creator | Wang, Jiarui Woldring, Rory P Román-Meléndez, Gabriel D McClain, Alan M Alzua, Brian R Marsh, E. Neil G |
| description | The radical S-adenosylmethionine (SAM) superfamily of enzymes catalyzes an amazingly diverse variety of reactions ranging from simple hydrogen abstraction to complicated multistep rearrangements and insertions. The reactions they catalyze are important for a broad range of biological functions, including cofactor and natural product biosynthesis, DNA repair, and tRNA modification. Generally conserved features of the radical SAM superfamily include a CX3CX2C motif that binds an [Fe4S4] cluster essential for the reductive cleavage of SAM. Here, we review recent advances in our understanding of the structure and mechanisms of these enzymes that, in some cases, have overturned widely accepted mechanisms. |
| doi_str_mv | 10.1021/cb5004674 |
| format | Article |
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Neil G</creatorcontrib><title>Recent Advances in Radical SAM Enzymology: New Structures and Mechanisms</title><title>ACS chemical biology</title><addtitle>ACS Chem. Biol</addtitle><description>The radical S-adenosylmethionine (SAM) superfamily of enzymes catalyzes an amazingly diverse variety of reactions ranging from simple hydrogen abstraction to complicated multistep rearrangements and insertions. The reactions they catalyze are important for a broad range of biological functions, including cofactor and natural product biosynthesis, DNA repair, and tRNA modification. Generally conserved features of the radical SAM superfamily include a CX3CX2C motif that binds an [Fe4S4] cluster essential for the reductive cleavage of SAM. Here, we review recent advances in our understanding of the structure and mechanisms of these enzymes that, in some cases, have overturned widely accepted mechanisms.</description><subject>Amino Acid Motifs</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - metabolism</subject><subject>Binding Sites</subject><subject>DNA Repair</subject><subject>Enzymes - chemistry</subject><subject>Enzymes - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Methylation</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - metabolism</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Reviews</subject><subject>S-Adenosylmethionine - metabolism</subject><subject>Sulfurtransferases - chemistry</subject><subject>Sulfurtransferases - metabolism</subject><issn>1554-8929</issn><issn>1554-8937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>N~.</sourceid><sourceid>EIF</sourceid><recordid>eNptkE1Lw0AQhhdRbK0e_AOSi6CHaJL9yMaDUEq1QlVo9bxMN5s2JdnU3aRSf71bWoOCpxmYh3deHoTOw-AmDKLwVs5oEBAWkwPUDSklPk9wfNjuUdJBJ9YuHYMZT45RJ3J8kpC4i0YTJZWuvX66Bi2V9XLtTSDNJRTetP_sDfXXpqyKar65817UpzetTSPrxjgSdOo9K7kAndvSnqKjDAqrzvazh94fhm-DkT9-fXwa9Mc-kIDWPsOpZAmENOYxD9gsporOgjTDJOMcc8wUliAjTggwwDhSMVAV4ShjMk6ylOMeut_lrppZqdJteQOFWJm8BLMRFeTi70XnCzGv1oKEzL2kLuBqH2Cqj0bZWpS5laooQKuqsSKkDCfcddui1ztUmspao7L2TRiIrXnRmnfsxe9eLfmj2gGXOwCkFcuqMdpp-ifoGyQwiYw</recordid><startdate>20140919</startdate><enddate>20140919</enddate><creator>Wang, Jiarui</creator><creator>Woldring, Rory P</creator><creator>Román-Meléndez, Gabriel D</creator><creator>McClain, Alan M</creator><creator>Alzua, Brian R</creator><creator>Marsh, E. 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Biol</addtitle><date>2014-09-19</date><risdate>2014</risdate><volume>9</volume><issue>9</issue><spage>1929</spage><epage>1938</epage><pages>1929-1938</pages><issn>1554-8929</issn><eissn>1554-8937</eissn><abstract>The radical S-adenosylmethionine (SAM) superfamily of enzymes catalyzes an amazingly diverse variety of reactions ranging from simple hydrogen abstraction to complicated multistep rearrangements and insertions. The reactions they catalyze are important for a broad range of biological functions, including cofactor and natural product biosynthesis, DNA repair, and tRNA modification. Generally conserved features of the radical SAM superfamily include a CX3CX2C motif that binds an [Fe4S4] cluster essential for the reductive cleavage of SAM. 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| subjects | Amino Acid Motifs Archaeal Proteins - chemistry Archaeal Proteins - metabolism Binding Sites DNA Repair Enzymes - chemistry Enzymes - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - metabolism Methylation Methyltransferases - chemistry Methyltransferases - metabolism Proteins - chemistry Proteins - metabolism Reviews S-Adenosylmethionine - metabolism Sulfurtransferases - chemistry Sulfurtransferases - metabolism |
| title | Recent Advances in Radical SAM Enzymology: New Structures and Mechanisms |
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