Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE
B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical -adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous st...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2022-02, Vol.58 (16), p.2738-2741 |
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| creator | Li, Yaoyang Yao, Yadi Yu, Lu Tian, Changlin Dong, Min |
| description | B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical
-adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous study showed that GD-AE cleaves SAM unconventionally to generate 5'-deoxy-5'-methylthioadenosine. Herein, we show that GD-AE actually cleaves SAM to form 5'-deoxyadenosine, similar to other radical SAM enzymes. Furthermore, with the synthesized glycerol analogue 2-deoxy-2-fluoroglycerol, we demonstrate that B12-independent GD catalyzes the glycerol dehydration reaction by direct elimination of the C-2 hydroxyl group of a ketyl radical rather than 1,2-OH migration. |
| doi_str_mv | 10.1039/d1cc06991h |
| format | Article |
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-adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous study showed that GD-AE cleaves SAM unconventionally to generate 5'-deoxy-5'-methylthioadenosine. Herein, we show that GD-AE actually cleaves SAM to form 5'-deoxyadenosine, similar to other radical SAM enzymes. Furthermore, with the synthesized glycerol analogue 2-deoxy-2-fluoroglycerol, we demonstrate that B12-independent GD catalyzes the glycerol dehydration reaction by direct elimination of the C-2 hydroxyl group of a ketyl radical rather than 1,2-OH migration.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/d1cc06991h</identifier><identifier>PMID: 35118483</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Biocatalysis ; Biotransformation ; Dehydration ; Deoxyadenosines - chemistry ; Deoxyadenosines - metabolism ; Electron Spin Resonance Spectroscopy ; Enzymes ; Glycerol ; Hydro-Lyases - metabolism ; Hydroxyl groups ; Methionine ; Molecular Structure ; S-Adenosylmethionine - chemistry ; S-Adenosylmethionine - metabolism ; Vitamin B 12 - metabolism</subject><ispartof>Chemical communications (Cambridge, England), 2022-02, Vol.58 (16), p.2738-2741</ispartof><rights>Copyright Royal Society of Chemistry 2022</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c315t-d485ecc395680e7eefea54adfc004567b1f107967cd5e644a210231a9c2b489a3</citedby><cites>FETCH-LOGICAL-c315t-d485ecc395680e7eefea54adfc004567b1f107967cd5e644a210231a9c2b489a3</cites><orcidid>0000-0001-6655-2818 ; 0000-0003-2965-8909 ; 0000-0002-2581-4612 ; 0000-0001-9315-900X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35118483$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yaoyang</creatorcontrib><creatorcontrib>Yao, Yadi</creatorcontrib><creatorcontrib>Yu, Lu</creatorcontrib><creatorcontrib>Tian, Changlin</creatorcontrib><creatorcontrib>Dong, Min</creatorcontrib><title>Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical
-adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous study showed that GD-AE cleaves SAM unconventionally to generate 5'-deoxy-5'-methylthioadenosine. Herein, we show that GD-AE actually cleaves SAM to form 5'-deoxyadenosine, similar to other radical SAM enzymes. Furthermore, with the synthesized glycerol analogue 2-deoxy-2-fluoroglycerol, we demonstrate that B12-independent GD catalyzes the glycerol dehydration reaction by direct elimination of the C-2 hydroxyl group of a ketyl radical rather than 1,2-OH migration.</description><subject>Biocatalysis</subject><subject>Biotransformation</subject><subject>Dehydration</subject><subject>Deoxyadenosines - chemistry</subject><subject>Deoxyadenosines - metabolism</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Enzymes</subject><subject>Glycerol</subject><subject>Hydro-Lyases - metabolism</subject><subject>Hydroxyl groups</subject><subject>Methionine</subject><subject>Molecular Structure</subject><subject>S-Adenosylmethionine - chemistry</subject><subject>S-Adenosylmethionine - metabolism</subject><subject>Vitamin B 12 - metabolism</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkElPwzAQhS0EgrJc-AHIEheEFPDES5xjKUuRQFxA4ha59qR1lTolTiuVX49ZD8xh5h2-N5p5hBwDuwDGy0sH1jJVljDbIgPgSmRS6NftTy3LrOBC7pH9GOcsFUi9S_a4BNBC8wExj2hnJvjYe0t9WGMSU9P7NtC2pleQZz44XGJqoafTZmOxaxvqcLZxnelNRGqCo76P1Njer5M1TCmG980C6d11Nrw5JDu1aSIe_cwD8nJ78zwaZw9Pd_ej4UNmOcg-c0JLtJaXUmmGBWKNRgrjasuYkKqYQA2sKFVhnUQlhMmB5RxMafOJ0KXhB-Tse--ya99W6Y9q4aPFpjEB21WscpUrBjrZEnr6D523qy6k6xLFQQEorRN1_k3Zro2xw7padn5huk0FrPoMvrqG0egr-HGCT35WriYLdH_ob9L8A3H9fTQ</recordid><startdate>20220222</startdate><enddate>20220222</enddate><creator>Li, Yaoyang</creator><creator>Yao, Yadi</creator><creator>Yu, Lu</creator><creator>Tian, Changlin</creator><creator>Dong, Min</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6655-2818</orcidid><orcidid>https://orcid.org/0000-0003-2965-8909</orcidid><orcidid>https://orcid.org/0000-0002-2581-4612</orcidid><orcidid>https://orcid.org/0000-0001-9315-900X</orcidid></search><sort><creationdate>20220222</creationdate><title>Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE</title><author>Li, Yaoyang ; Yao, Yadi ; Yu, Lu ; Tian, Changlin ; Dong, Min</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-d485ecc395680e7eefea54adfc004567b1f107967cd5e644a210231a9c2b489a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Biocatalysis</topic><topic>Biotransformation</topic><topic>Dehydration</topic><topic>Deoxyadenosines - chemistry</topic><topic>Deoxyadenosines - metabolism</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Enzymes</topic><topic>Glycerol</topic><topic>Hydro-Lyases - metabolism</topic><topic>Hydroxyl groups</topic><topic>Methionine</topic><topic>Molecular Structure</topic><topic>S-Adenosylmethionine - chemistry</topic><topic>S-Adenosylmethionine - metabolism</topic><topic>Vitamin B 12 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yaoyang</creatorcontrib><creatorcontrib>Yao, Yadi</creatorcontrib><creatorcontrib>Yu, Lu</creatorcontrib><creatorcontrib>Tian, Changlin</creatorcontrib><creatorcontrib>Dong, Min</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yaoyang</au><au>Yao, Yadi</au><au>Yu, Lu</au><au>Tian, Changlin</au><au>Dong, Min</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2022-02-22</date><risdate>2022</risdate><volume>58</volume><issue>16</issue><spage>2738</spage><epage>2741</epage><pages>2738-2741</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical
-adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous study showed that GD-AE cleaves SAM unconventionally to generate 5'-deoxy-5'-methylthioadenosine. Herein, we show that GD-AE actually cleaves SAM to form 5'-deoxyadenosine, similar to other radical SAM enzymes. Furthermore, with the synthesized glycerol analogue 2-deoxy-2-fluoroglycerol, we demonstrate that B12-independent GD catalyzes the glycerol dehydration reaction by direct elimination of the C-2 hydroxyl group of a ketyl radical rather than 1,2-OH migration.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>35118483</pmid><doi>10.1039/d1cc06991h</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0001-6655-2818</orcidid><orcidid>https://orcid.org/0000-0003-2965-8909</orcidid><orcidid>https://orcid.org/0000-0002-2581-4612</orcidid><orcidid>https://orcid.org/0000-0001-9315-900X</orcidid></addata></record> |
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| ispartof | Chemical communications (Cambridge, England), 2022-02, Vol.58 (16), p.2738-2741 |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Biocatalysis Biotransformation Dehydration Deoxyadenosines - chemistry Deoxyadenosines - metabolism Electron Spin Resonance Spectroscopy Enzymes Glycerol Hydro-Lyases - metabolism Hydroxyl groups Methionine Molecular Structure S-Adenosylmethionine - chemistry S-Adenosylmethionine - metabolism Vitamin B 12 - metabolism |
| title | Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE |
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