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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A182DWE5_9ACTN A0A182DWE5_9ACTN] | | [https://www.uniprot.org/uniprot/A0A182DWE5_9ACTN A0A182DWE5_9ACTN] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.
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| Structure and specificity of a permissive bacterial C-prenyltransferase.,Elshahawi SI, Cao H, Shaaban KA, Ponomareva LV, Subramanian T, Farman ML, Spielmann HP, Phillips GN Jr, Thorson JS, Singh S Nat Chem Biol. 2017 Feb 6. doi: 10.1038/nchembio.2285. PMID:28166207<ref>PMID:28166207</ref>
| | ==See Also== |
| | | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| 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 5inj" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
