Reductive Cleavage of Sulfoxide and Sulfone by Two Radical S-Adenosyl-l-methionine Enzymes.
Identifieur interne : 000099 ( Main/Exploration ); précédent : 000098; suivant : 000100Reductive Cleavage of Sulfoxide and Sulfone by Two Radical S-Adenosyl-l-methionine Enzymes.
Auteurs : Dhanaraju Mandalapu [République populaire de Chine] ; Xinjian Ji [République populaire de Chine] ; Qi Zhang [République populaire de Chine]Source :
- Biochemistry [ 1520-4995 ] ; 2019.
Descripteurs français
- KwdFr :
- Adémétionine (composition chimique), Adémétionine (métabolisme), Carbon-carbon lyases (métabolisme), Methyltransferases (métabolisme), Safrole (analogues et dérivés), Safrole (composition chimique), Safrole (métabolisme), Sulfones (composition chimique), Sulfones (métabolisme), Tryptophane (métabolisme).
- MESH :
- analogues et dérivés : Safrole.
- composition chimique : Adémétionine, Safrole, Sulfones.
- métabolisme : Adémétionine, Carbon-carbon lyases, Methyltransferases, Safrole, Sulfones, Tryptophane.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Safrole.
- chemical , chemistry : S-Adenosylmethionine, Safrole, Sulfones.
- chemical , metabolism : Carbon-Carbon Lyases, Methyltransferases, S-Adenosylmethionine, Safrole, Sulfones, Tryptophan.
Abstract
Sulfoxides and sulfones are commonly found in nature as a result of thioether oxidation, whereas only a very few enzymes have been found to metabolize these compounds. Utilizing the strong reduction potential of the [4Fe-4S] cluster of radical S-adenosyl-l-methionine (SAM) enzymes, we herein report the first enzyme-catalyzed reductive cleavage of sulfoxide and sulfone. We show two radical SAM enzymes, tryptophan lyase NosL and the class C radical SAM methyltransferase NosN, are able to act on a sulfoxide SAHO and a sulfone SAHO2, both of which are structurally similar to SAM. NosL cleaves all of the three bonds (i.e., S-C(5'), S-C(γ), and S-O) connecting the sulfur center of SAHO, with a preference for S-C(5') bond cleavage. Similar S-C cleavage activity was also found for SHAO2, but no S-O cleavage was observed. In contrast to NosL, NosN almost exclusively cleaves the S-C(5') bonds of SAHO and SAHO2 with much higher efficiencies. Our study provides valuable insights into the [4Fe-4S] cluster-mediated reduction reactions and highlights the remarkable catalytic promiscuity of radical SAM enzymes.
DOI: 10.1021/acs.biochem.8b00844
PubMed: 30398855
Affiliations:
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Chine</country><wicri:regionArea>Department of Chemistry , Fudan University , Shanghai 200433 </wicri:regionArea><wicri:noRegion>Shanghai 200433 </wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Qi" sort="Zhang, Qi" uniqKey="Zhang Q" first="Qi" last="Zhang">Qi Zhang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Chemistry , Fudan University , Shanghai 200433 </wicri:regionArea><wicri:noRegion>Shanghai 200433 </wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:30398855</idno><idno type="pmid">30398855</idno><idno type="doi">10.1021/acs.biochem.8b00844</idno><idno type="wicri:Area/Main/Corpus">000185</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" 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first="Xinjian" last="Ji">Xinjian Ji</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Chemistry , Fudan University , Shanghai 200433 </wicri:regionArea><wicri:noRegion>Shanghai 200433 </wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Qi" sort="Zhang, Qi" uniqKey="Zhang Q" first="Qi" last="Zhang">Qi Zhang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Chemistry , Fudan University , Shanghai 200433 </wicri:regionArea><wicri:noRegion>Shanghai 200433 </wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbon-Carbon Lyases (metabolism)</term><term>Methyltransferases (metabolism)</term><term>S-Adenosylmethionine (chemistry)</term><term>S-Adenosylmethionine (metabolism)</term><term>Safrole (analogs & derivatives)</term><term>Safrole (chemistry)</term><term>Safrole (metabolism)</term><term>Sulfones (chemistry)</term><term>Sulfones (metabolism)</term><term>Tryptophan (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adémétionine (composition chimique)</term><term>Adémétionine (métabolisme)</term><term>Carbon-carbon lyases (métabolisme)</term><term>Methyltransferases (métabolisme)</term><term>Safrole (analogues et dérivés)</term><term>Safrole (composition chimique)</term><term>Safrole (métabolisme)</term><term>Sulfones (composition chimique)</term><term>Sulfones (métabolisme)</term><term>Tryptophane (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Safrole</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>S-Adenosylmethionine</term><term>Safrole</term><term>Sulfones</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbon-Carbon Lyases</term><term>Methyltransferases</term><term>S-Adenosylmethionine</term><term>Safrole</term><term>Sulfones</term><term>Tryptophan</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Safrole</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Adémétionine</term><term>Safrole</term><term>Sulfones</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adémétionine</term><term>Carbon-carbon lyases</term><term>Methyltransferases</term><term>Safrole</term><term>Sulfones</term><term>Tryptophane</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sulfoxides and sulfones are commonly found in nature as a result of thioether oxidation, whereas only a very few enzymes have been found to metabolize these compounds. Utilizing the strong reduction potential of the [4Fe-4S] cluster of radical S-adenosyl-l-methionine (SAM) enzymes, we herein report the first enzyme-catalyzed reductive cleavage of sulfoxide and sulfone. We show two radical SAM enzymes, tryptophan lyase NosL and the class C radical SAM methyltransferase NosN, are able to act on a sulfoxide SAHO and a sulfone SAHO<sub>2</sub>, both of which are structurally similar to SAM. NosL cleaves all of the three bonds (i.e., S-C(5'), S-C(γ), and S-O) connecting the sulfur center of SAHO, with a preference for S-C(5') bond cleavage. Similar S-C cleavage activity was also found for SHAO<sub>2</sub>, but no S-O cleavage was observed. In contrast to NosL, NosN almost exclusively cleaves the S-C(5') bonds of SAHO and SAHO<sub>2</sub> with much higher efficiencies. Our study provides valuable insights into the [4Fe-4S] cluster-mediated reduction reactions and highlights the remarkable catalytic promiscuity of radical SAM enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30398855</PMID><DateCompleted><Year>2019</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>58</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>01</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Reductive Cleavage of Sulfoxide and Sulfone by Two Radical S-Adenosyl-l-methionine Enzymes.</ArticleTitle><Pagination><MedlinePgn>36-39</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.8b00844</ELocationID><Abstract><AbstractText>Sulfoxides and sulfones are commonly found in nature as a result of thioether oxidation, whereas only a very few enzymes have been found to metabolize these compounds. Utilizing the strong reduction potential of the [4Fe-4S] cluster of radical S-adenosyl-l-methionine (SAM) enzymes, we herein report the first enzyme-catalyzed reductive cleavage of sulfoxide and sulfone. We show two radical SAM enzymes, tryptophan lyase NosL and the class C radical SAM methyltransferase NosN, are able to act on a sulfoxide SAHO and a sulfone SAHO<sub>2</sub>, both of which are structurally similar to SAM. NosL cleaves all of the three bonds (i.e., S-C(5'), S-C(γ), and S-O) connecting the sulfur center of SAHO, with a preference for S-C(5') bond cleavage. Similar S-C cleavage activity was also found for SHAO<sub>2</sub>, but no S-O cleavage was observed. In contrast to NosL, NosN almost exclusively cleaves the S-C(5') bonds of SAHO and SAHO<sub>2</sub> with much higher efficiencies. Our study provides valuable insights into the [4Fe-4S] cluster-mediated reduction reactions and highlights the remarkable catalytic promiscuity of radical SAM enzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mandalapu</LastName><ForeName>Dhanaraju</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ji</LastName><ForeName>Xinjian</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Qi</ForeName><Initials>Q</Initials><Identifier Source="ORCID">0000-0002-8135-2221</Identifier><AffiliationInfo><Affiliation>Department of Chemistry , Fudan University , Shanghai 200433 , China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>11</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013450">Sulfones</NameOfSubstance></Chemical><Chemical><RegistryNumber>7LP2MPO46S</RegistryNumber><NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.1.-</RegistryNumber><NameOfSubstance UI="D019755">Carbon-Carbon Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>RSB34337V9</RegistryNumber><NameOfSubstance UI="D012451">Safrole</NameOfSubstance></Chemical><Chemical><RegistryNumber>WOR3CS513R</RegistryNumber><NameOfSubstance UI="C005746">sulfoxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019755" MajorTopicYN="N">Carbon-Carbon Lyases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012436" MajorTopicYN="N">S-Adenosylmethionine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012451" MajorTopicYN="N">Safrole</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013450" MajorTopicYN="N">Sulfones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>11</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>11</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30398855</ArticleId><ArticleId IdType="doi">10.1021/acs.biochem.8b00844</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Mandalapu, Dhanaraju" sort="Mandalapu, Dhanaraju" uniqKey="Mandalapu D" first="Dhanaraju" last="Mandalapu">Dhanaraju Mandalapu</name></noRegion><name sortKey="Ji, Xinjian" sort="Ji, Xinjian" uniqKey="Ji X" first="Xinjian" last="Ji">Xinjian Ji</name><name sortKey="Zhang, Qi" sort="Zhang, Qi" uniqKey="Zhang Q" first="Qi" last="Zhang">Qi Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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