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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/F4F6Q5_MICM1 F4F6Q5_MICM1] | | [https://www.uniprot.org/uniprot/F4F6Q5_MICM1 F4F6Q5_MICM1] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Abyssomicin C and its atropisomer are potent inhibitors of bacterial folate metabolism. They possess complex polycyclic structures, and their biosynthesis has been shown to involve several unusual enzymatic transformations. Using a combination of synthesis and in vitro assays we reveal that AbyV, a cytochrome P450 enzyme from the aby gene cluster, catalyses a key late-stage epoxidation required for the installation of the characteristic ether-bridged-core of abyssomicin C. The X-ray crystal structure of AbyV has been determined, which in combination with molecular dynamics simulations provides a structural framework for our functional data. This work demonstrates the power of combining selective carbon-13 labelling with NMR spectroscopy as a sensitive tool to interrogate enzyme-catalysed reactions in vitro with no need for purification.
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| The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis.,Devine AJ, Parnell AE, Back CR, Lees NR, Johns ST, Zulkepli AZ, Barringer R, Zorn K, Stach JEM, Crump MP, Hayes MA, van der Kamp MW, Race PR, Willis C Angew Chem Int Ed Engl. 2022 Oct 31. doi: 10.1002/anie.202213053. PMID:36314667<ref>PMID:36314667</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 7qan" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
