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Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme
Prodiginines, tripyrrole alkaloids displaying a wide array of bioactivities, occur as linear and cyclic congeners. Identification of an unclustered biosynthetic gene led to the discovery of the enzyme responsible for catalyzing the regiospecific C–H activation and cyclization of prodigiosin to form...
| Autores principales: | , , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
2017
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5677514/ https://www.ncbi.nlm.nih.gov/pubmed/28892091 http://dx.doi.org/10.1038/nchembio.2471 |
| _version_ | 1783277262210072576 |
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| author | de Rond, Tristan Stow, Parker Eigl, Ian Johnson, Rebecca E Chan, Leanne Jade G Goyal, Garima Baidoo, Edward EK Hillson, Nathan J Petzold, Christopher J Sarpong, Richmond Keasling, Jay D |
| author_facet | de Rond, Tristan Stow, Parker Eigl, Ian Johnson, Rebecca E Chan, Leanne Jade G Goyal, Garima Baidoo, Edward EK Hillson, Nathan J Petzold, Christopher J Sarpong, Richmond Keasling, Jay D |
| author_sort | de Rond, Tristan |
| collection | PubMed |
| description | Prodiginines, tripyrrole alkaloids displaying a wide array of bioactivities, occur as linear and cyclic congeners. Identification of an unclustered biosynthetic gene led to the discovery of the enzyme responsible for catalyzing the regiospecific C–H activation and cyclization of prodigiosin to form cycloprodigiosin in Pseudoalteromonas rubra. This enzyme is closely related to alkylglycerol monooxygenase, and unrelated to RedG, the Rieske oxygenase that produces cyclized prodiginines in Streptomyces, implying convergent evolution. |
| format | Online Article Text |
| id | pubmed-5677514 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2017 |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-56775142018-03-11 Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme de Rond, Tristan Stow, Parker Eigl, Ian Johnson, Rebecca E Chan, Leanne Jade G Goyal, Garima Baidoo, Edward EK Hillson, Nathan J Petzold, Christopher J Sarpong, Richmond Keasling, Jay D Nat Chem Biol Article Prodiginines, tripyrrole alkaloids displaying a wide array of bioactivities, occur as linear and cyclic congeners. Identification of an unclustered biosynthetic gene led to the discovery of the enzyme responsible for catalyzing the regiospecific C–H activation and cyclization of prodigiosin to form cycloprodigiosin in Pseudoalteromonas rubra. This enzyme is closely related to alkylglycerol monooxygenase, and unrelated to RedG, the Rieske oxygenase that produces cyclized prodiginines in Streptomyces, implying convergent evolution. 2017-09-11 2017-11 /pmc/articles/PMC5677514/ /pubmed/28892091 http://dx.doi.org/10.1038/nchembio.2471 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
| spellingShingle | Article de Rond, Tristan Stow, Parker Eigl, Ian Johnson, Rebecca E Chan, Leanne Jade G Goyal, Garima Baidoo, Edward EK Hillson, Nathan J Petzold, Christopher J Sarpong, Richmond Keasling, Jay D Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title | Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title_full | Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title_fullStr | Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title_full_unstemmed | Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title_short | Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| title_sort | oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme |
| topic | Article |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5677514/ https://www.ncbi.nlm.nih.gov/pubmed/28892091 http://dx.doi.org/10.1038/nchembio.2471 |
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