ALIPHATIC EPOXIDE CARBOXYLATION
Aliphatic epoxides (epoxyalkanes) are highly reactive electrophilic molecules that are formed from the monooxygenase-catalyzed epoxidation of aliphatic alkenes. The bacterial metabolism of short-chain epoxyalkanes occurs by a three-step pathway resulting in net carboxylation to β-ketoacids. This pat...
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| Veröffentlicht in: | Annual review of biochemistry 2003-01, Vol.72 (1), p.55-76 |
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| creator | Ensign, Scott A Allen, Jeffrey R |
| description | Aliphatic epoxides (epoxyalkanes) are highly reactive electrophilic
molecules that are formed from the monooxygenase-catalyzed epoxidation of
aliphatic alkenes. The bacterial metabolism of short-chain epoxyalkanes occurs
by a three-step pathway resulting in net carboxylation to β-ketoacids.
This pathway uses the atypical cofactor coenzyme M (CoM;
2-mercaptoethanesulfonic acid) as the nucleophile for the epoxide ring opening
and as the carrier of 2-hydroxyalkyl- and 2-ketoalkyl-CoM intermediates. Four
enzymes are involved in epoxide carboxylation: a zinc-dependent
alkyltransferase, two short-chain dehydrogenases with specificities for the
chiral products of the R- and S-1,2-epoxyalkane ring opening, and an
NADPH:disulfide oxidoreductase/carboxylase that reduces the thioether bond of
the 2-ketoalkyl-CoM conjugate and carboxylates the resulting carbanion. In this
review, we summarize the biochemical, mechanistic, and structural features of
the enzymes of epoxide carboxylation and show how these enzymes, together with
CoM, work in concert to achieve this highly unusual carboxylation reaction. |
| doi_str_mv | 10.1146/annurev.biochem.72.121801.161820 |
| format | Article |
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molecules that are formed from the monooxygenase-catalyzed epoxidation of
aliphatic alkenes. The bacterial metabolism of short-chain epoxyalkanes occurs
by a three-step pathway resulting in net carboxylation to β-ketoacids.
This pathway uses the atypical cofactor coenzyme M (CoM;
2-mercaptoethanesulfonic acid) as the nucleophile for the epoxide ring opening
and as the carrier of 2-hydroxyalkyl- and 2-ketoalkyl-CoM intermediates. Four
enzymes are involved in epoxide carboxylation: a zinc-dependent
alkyltransferase, two short-chain dehydrogenases with specificities for the
chiral products of the R- and S-1,2-epoxyalkane ring opening, and an
NADPH:disulfide oxidoreductase/carboxylase that reduces the thioether bond of
the 2-ketoalkyl-CoM conjugate and carboxylates the resulting carbanion. In this
review, we summarize the biochemical, mechanistic, and structural features of
the enzymes of epoxide carboxylation and show how these enzymes, together with
CoM, work in concert to achieve this highly unusual carboxylation reaction.</description><identifier>ISSN: 0066-4154</identifier><identifier>EISSN: 1545-4509</identifier><identifier>DOI: 10.1146/annurev.biochem.72.121801.161820</identifier><identifier>PMID: 12524213</identifier><identifier>CODEN: ARBOAW</identifier><language>eng</language><publisher>Palo Alto, CA 94303-0139: Annual Reviews</publisher><subject>Alkenes ; Alkenes - metabolism ; Alkyl and Aryl Transferases - chemistry ; Alkyl and Aryl Transferases - metabolism ; Bacteria - metabolism ; Biochemistry ; Carbon ; Carboxy-Lyases - metabolism ; carboxylase ; coenzyme M ; dehydrogenase/reductase ; disulfide oxidoreductase ; Enzymes ; Epoxy Compounds - chemistry ; Epoxy Compounds - metabolism ; epoxyalkane ; Mesna - metabolism ; Models, Molecular ; NAD - metabolism ; NADP - metabolism ; Oxidoreductases - chemistry ; Oxidoreductases - metabolism ; short-chain ; Stereoisomerism</subject><ispartof>Annual review of biochemistry, 2003-01, Vol.72 (1), p.55-76</ispartof><rights>Copyright © 2003 by Annual Reviews. All rights reserved</rights><rights>Copyright Annual Reviews, Inc. 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a416t-c1c40a4ec316b5f5a5775f03813f7ba021e29c07830355103a455aa056c185a33</citedby><cites>FETCH-LOGICAL-a416t-c1c40a4ec316b5f5a5775f03813f7ba021e29c07830355103a455aa056c185a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biochem.72.121801.161820?crawler=true&mimetype=application/pdf$$EPDF$$P50$$Gannualreviews$$H</linktopdf><linktohtml>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biochem.72.121801.161820$$EHTML$$P50$$Gannualreviews$$H</linktohtml><link.rule.ids>70,315,781,785,4183,27929,27930,78259,78260</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12524213$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ensign, Scott A</creatorcontrib><creatorcontrib>Allen, Jeffrey R</creatorcontrib><title>ALIPHATIC EPOXIDE CARBOXYLATION</title><title>Annual review of biochemistry</title><addtitle>Annu Rev Biochem</addtitle><description>Aliphatic epoxides (epoxyalkanes) are highly reactive electrophilic
molecules that are formed from the monooxygenase-catalyzed epoxidation of
aliphatic alkenes. The bacterial metabolism of short-chain epoxyalkanes occurs
by a three-step pathway resulting in net carboxylation to β-ketoacids.
This pathway uses the atypical cofactor coenzyme M (CoM;
2-mercaptoethanesulfonic acid) as the nucleophile for the epoxide ring opening
and as the carrier of 2-hydroxyalkyl- and 2-ketoalkyl-CoM intermediates. Four
enzymes are involved in epoxide carboxylation: a zinc-dependent
alkyltransferase, two short-chain dehydrogenases with specificities for the
chiral products of the R- and S-1,2-epoxyalkane ring opening, and an
NADPH:disulfide oxidoreductase/carboxylase that reduces the thioether bond of
the 2-ketoalkyl-CoM conjugate and carboxylates the resulting carbanion. In this
review, we summarize the biochemical, mechanistic, and structural features of
the enzymes of epoxide carboxylation and show how these enzymes, together with
CoM, work in concert to achieve this highly unusual carboxylation reaction.</description><subject>Alkenes</subject><subject>Alkenes - metabolism</subject><subject>Alkyl and Aryl Transferases - chemistry</subject><subject>Alkyl and Aryl Transferases - metabolism</subject><subject>Bacteria - metabolism</subject><subject>Biochemistry</subject><subject>Carbon</subject><subject>Carboxy-Lyases - metabolism</subject><subject>carboxylase</subject><subject>coenzyme M</subject><subject>dehydrogenase/reductase</subject><subject>disulfide oxidoreductase</subject><subject>Enzymes</subject><subject>Epoxy Compounds - chemistry</subject><subject>Epoxy Compounds - metabolism</subject><subject>epoxyalkane</subject><subject>Mesna - metabolism</subject><subject>Models, Molecular</subject><subject>NAD - metabolism</subject><subject>NADP - metabolism</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - metabolism</subject><subject>short-chain</subject><subject>Stereoisomerism</subject><issn>0066-4154</issn><issn>1545-4509</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkE1Lw0AQQBdRbK3-BS0exEvizH4luVljtYVii1Sop2W7brClSWq2Ufz3bklA8OZpYXi8mX2EXCOEiFze6KKoK_sZLlelebd5GNEQKcaAIUqMKRyQLgouAi4gOSRdACkD7icdcuLcGgBYwukx6SAVlFNkXXIxmIxno8F8nPaHs-lifD_sp4Pnu-nideKH06dTcpTpjbNn7dsjLw_DeToKJtPHcTqYBJqj3AUGDQfNrWEolyITWkSRyIDFyLJoqYGipYmBKGbAhEBgmguhNQhpMBaasR65arzbqvyordupfOWM3Wx0YcvaqUhE_mOIHrz8A67Luir8bYpSJpMkYdJDtw1kqtK5ymZqW61yXX0rBLUvqdqSqi2pIqqakqop6RXn7Z56mdu3X0GbzgPDBtir9MbLVvbL_X_RDxv3hd0</recordid><startdate>20030101</startdate><enddate>20030101</enddate><creator>Ensign, Scott A</creator><creator>Allen, Jeffrey R</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20030101</creationdate><title>ALIPHATIC EPOXIDE CARBOXYLATION</title><author>Ensign, Scott A ; Allen, Jeffrey R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a416t-c1c40a4ec316b5f5a5775f03813f7ba021e29c07830355103a455aa056c185a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Alkenes</topic><topic>Alkenes - metabolism</topic><topic>Alkyl and Aryl Transferases - chemistry</topic><topic>Alkyl and Aryl Transferases - metabolism</topic><topic>Bacteria - metabolism</topic><topic>Biochemistry</topic><topic>Carbon</topic><topic>Carboxy-Lyases - metabolism</topic><topic>carboxylase</topic><topic>coenzyme M</topic><topic>dehydrogenase/reductase</topic><topic>disulfide oxidoreductase</topic><topic>Enzymes</topic><topic>Epoxy Compounds - chemistry</topic><topic>Epoxy Compounds - metabolism</topic><topic>epoxyalkane</topic><topic>Mesna - metabolism</topic><topic>Models, Molecular</topic><topic>NAD - metabolism</topic><topic>NADP - metabolism</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - metabolism</topic><topic>short-chain</topic><topic>Stereoisomerism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ensign, Scott A</creatorcontrib><creatorcontrib>Allen, Jeffrey R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Annual review of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ensign, Scott A</au><au>Allen, Jeffrey R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ALIPHATIC EPOXIDE CARBOXYLATION</atitle><jtitle>Annual review of biochemistry</jtitle><addtitle>Annu Rev Biochem</addtitle><date>2003-01-01</date><risdate>2003</risdate><volume>72</volume><issue>1</issue><spage>55</spage><epage>76</epage><pages>55-76</pages><issn>0066-4154</issn><eissn>1545-4509</eissn><coden>ARBOAW</coden><abstract>Aliphatic epoxides (epoxyalkanes) are highly reactive electrophilic
molecules that are formed from the monooxygenase-catalyzed epoxidation of
aliphatic alkenes. The bacterial metabolism of short-chain epoxyalkanes occurs
by a three-step pathway resulting in net carboxylation to β-ketoacids.
This pathway uses the atypical cofactor coenzyme M (CoM;
2-mercaptoethanesulfonic acid) as the nucleophile for the epoxide ring opening
and as the carrier of 2-hydroxyalkyl- and 2-ketoalkyl-CoM intermediates. Four
enzymes are involved in epoxide carboxylation: a zinc-dependent
alkyltransferase, two short-chain dehydrogenases with specificities for the
chiral products of the R- and S-1,2-epoxyalkane ring opening, and an
NADPH:disulfide oxidoreductase/carboxylase that reduces the thioether bond of
the 2-ketoalkyl-CoM conjugate and carboxylates the resulting carbanion. In this
review, we summarize the biochemical, mechanistic, and structural features of
the enzymes of epoxide carboxylation and show how these enzymes, together with
CoM, work in concert to achieve this highly unusual carboxylation reaction.</abstract><cop>Palo Alto, CA 94303-0139</cop><cop>4139 El Camino Way, P.O. Box 10139</cop><cop>USA</cop><pub>Annual Reviews</pub><pmid>12524213</pmid><doi>10.1146/annurev.biochem.72.121801.161820</doi><tpages>22</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0066-4154 |
| ispartof | Annual review of biochemistry, 2003-01, Vol.72 (1), p.55-76 |
| issn | 0066-4154 1545-4509 |
| language | eng |
| recordid | cdi_pubmed_primary_12524213 |
| source | Annual Reviews Complete A-Z List; MEDLINE |
| subjects | Alkenes Alkenes - metabolism Alkyl and Aryl Transferases - chemistry Alkyl and Aryl Transferases - metabolism Bacteria - metabolism Biochemistry Carbon Carboxy-Lyases - metabolism carboxylase coenzyme M dehydrogenase/reductase disulfide oxidoreductase Enzymes Epoxy Compounds - chemistry Epoxy Compounds - metabolism epoxyalkane Mesna - metabolism Models, Molecular NAD - metabolism NADP - metabolism Oxidoreductases - chemistry Oxidoreductases - metabolism short-chain Stereoisomerism |
| title | ALIPHATIC EPOXIDE CARBOXYLATION |
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