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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A401MXE6_9ACTN A0A401MXE6_9ACTN] | | [https://www.uniprot.org/uniprot/A0A401MXE6_9ACTN A0A401MXE6_9ACTN] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Stereoselective carbon-carbon bond forming reactions are quintessential transformations in organic synthesis. One example is the Diels-Alder reaction, a [4+2] cycloaddition between a conjugated diene and a dienophile to form cyclohexenes. The development of biocatalysts for this reaction is paramount for unlocking sustainable routes to a plethora of important molecules. To obtain a comprehensive understanding of naturally evolved [4+2] cyclases, and to identify hitherto uncharacterised biocatalysts for this reaction, we constructed a library comprising forty-five enzymes with reported or predicted [4+2] cycloaddition activity. Thirty-one library members were successfully produced in recombinant form. In vitro assays employing a synthetic substrate incorporating a diene and a dienophile revealed broad-ranging cycloaddition activity amongst these polypeptides. The hypothetical protein Cyc15 was found to catalyse an intramolecular cycloaddition to generate a novel spirotetronate. The crystal structure of this enzyme, along with docking studies, establishes the basis for stereoselectivity in Cyc15, as compared to other spirotetronate cyclases.
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| Interrogation of an Enzyme Library Reveals the Catalytic Plasticity of Naturally Evolved [4+2] Cyclases.,Zorn K, Back CR, Barringer R, Chadimova V, Manzo-Ruiz M, Mbatha SZ, Mobarec JC, Williams SE, van der Kamp MW, Race PR, Willis CL, Hayes MA Chembiochem. 2023 Jun 12:e202300382. doi: 10.1002/cbic.202300382. PMID:37305956<ref>PMID:37305956</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8of7" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |