Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-16729-0 |
| _version_ | 1818735667109167104 |
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| author | April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan |
| author_facet | April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan |
| author_sort | April L. Lukowski |
| collection | DOAJ |
| description | Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin analog-bound crystal structures and by using mutagenesis experiments identify residues, which are important for substrate positioning and reaction selectivity. |
| first_indexed | 2024-12-18T00:24:54Z |
| format | Article |
| id | doaj.art-b69e299e06b4475ab6229373dc78b546 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-18T00:24:54Z |
| publishDate | 2020-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-b69e299e06b4475ab6229373dc78b5462022-12-21T21:27:16ZengNature PortfolioNature Communications2041-17232020-06-0111111010.1038/s41467-020-16729-0Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenasesApril L. Lukowski0Jianxin Liu1Jennifer Bridwell-Rabb2Alison R. H. Narayan3Program in Chemical Biology, University of MichiganDepartment of Chemistry, University of MichiganProgram in Chemical Biology, University of MichiganProgram in Chemical Biology, University of MichiganRieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin analog-bound crystal structures and by using mutagenesis experiments identify residues, which are important for substrate positioning and reaction selectivity.https://doi.org/10.1038/s41467-020-16729-0 |
| spellingShingle | April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases Nature Communications |
| title | Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases |
| title_full | Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases |
| title_fullStr | Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases |
| title_full_unstemmed | Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases |
| title_short | Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases |
| title_sort | structural basis for divergent c h hydroxylation selectivity in two rieske oxygenases |
| url | https://doi.org/10.1038/s41467-020-16729-0 |
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