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https://doi.org/10.21256/zhaw-22632Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Papadopoulou, Athena | - |
| dc.contributor.author | Meierhofer, Jasmin | - |
| dc.contributor.author | Meyer, Fabian | - |
| dc.contributor.author | Hayashi, Takahiro | - |
| dc.contributor.author | Schneider, Samuel | - |
| dc.contributor.author | Sager, Emine | - |
| dc.contributor.author | Buller, Rebecca | - |
| dc.date.accessioned | 2021-06-11T13:09:58Z | - |
| dc.date.available | 2021-06-11T13:09:58Z | - |
| dc.date.issued | 2021-06-07 | - |
| dc.identifier.issn | 1867-3880 | de_CH |
| dc.identifier.issn | 1867-3899 | de_CH |
| dc.identifier.uri | https://digitalcollection.zhaw.ch/handle/11475/22632 | - |
| dc.description.abstract | Non-heme iron/ α -ketoglutarate dependent halogenases acting on freestanding substrates catalyze the regio- and stereoselective halogenation of inactivated C(sp 3 )-H bonds. Yet, with only a handful of these halogenases characterized, the biosynthetic potential of enzymatic radical halogenation remains limited. Herein, we describe the remodeling of L -proline cis -4-hydroxylase from Sinorhizobium meliloti into a halogenase by introduction of a single point mutation ( D108G) into the enzyme’s active site. The re-programmed halogenase displays a striking regio-divergent reaction chemistry: While halogenation of L -proline exclusively occurs at the C3-position, the retained hydroxylation activity leads to derivatization at the C-4 position, corresponding to the regioselectivity of the wildtype enzyme. By employing several rounds of directed evolution, an optimized halogenase variant with 98-fold improved apparent k cat / K m for chlorination of L -proline compared to the parental enzyme SmP4H ( D108G) was identified. The development and optimization of this novel halogenation biocatalyst highlights the possibility to rationally harness the chemical versatility of non-heme Fe/ α KG dependent dioxygenases for C-H functionalization . | de_CH |
| dc.language.iso | en | de_CH |
| dc.publisher | Wiley | de_CH |
| dc.relation.ispartof | ChemCatChem | de_CH |
| dc.rights | http://creativecommons.org/licenses/by/4.0/ | de_CH |
| dc.subject.ddc | 660.6: Biotechnologie | de_CH |
| dc.title | Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate | de_CH |
| dc.type | Beitrag in wissenschaftlicher Zeitschrift | de_CH |
| dcterms.type | Text | de_CH |
| zhaw.departement | Life Sciences und Facility Management | de_CH |
| zhaw.organisationalunit | Institut für Chemie und Biotechnologie (ICBT) | de_CH |
| dc.identifier.doi | 10.1002/cctc.202100591 | de_CH |
| dc.identifier.doi | 10.21256/zhaw-22632 | - |
| zhaw.funding.eu | No | de_CH |
| zhaw.issue | 18 | de_CH |
| zhaw.originated.zhaw | Yes | de_CH |
| zhaw.pages.end | 3919 | de_CH |
| zhaw.pages.start | 3914 | de_CH |
| zhaw.publication.status | publishedVersion | de_CH |
| zhaw.volume | 13 | de_CH |
| zhaw.embargo.end | 2022-06-08 | de_CH |
| zhaw.publication.review | Peer review (Publikation) | de_CH |
| zhaw.webfeed | Biokatalyse | de_CH |
| zhaw.author.additional | No | de_CH |
| zhaw.display.portrait | Yes | de_CH |
| Appears in collections: | Publikationen Life Sciences und Facility Management | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| 2021_Papadopoulou-etal_Re-programming-and-optimization_VoR.pdf | Published Version | 1.84 MB | Adobe PDF |  View/Open |
| 2021_Papadopoulou-etal_Re-programming-and-optimization.pdf | Accepted Version | 885.69 kB | Adobe PDF |  View/Open |
Show simple item record
Papadopoulou, A., Meierhofer, J., Meyer, F., Hayashi, T., Schneider, S., Sager, E., & Buller, R. (2021). Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate. ChemCatChem, 13(18), 3914–3919. https://doi.org/10.1002/cctc.202100591
Papadopoulou, A. et al. (2021) ‘Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate’, ChemCatChem, 13(18), pp. 3914–3919. Available at: https://doi.org/10.1002/cctc.202100591.
A. Papadopoulou et al., “Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate,” ChemCatChem, vol. 13, no. 18, pp. 3914–3919, Jun. 2021, doi: 10.1002/cctc.202100591.
PAPADOPOULOU, Athena, Jasmin MEIERHOFER, Fabian MEYER, Takahiro HAYASHI, Samuel SCHNEIDER, Emine SAGER und Rebecca BULLER, 2021. Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate. ChemCatChem. 7 Juni 2021. Bd. 13, Nr. 18, S. 3914–3919. DOI 10.1002/cctc.202100591
Papadopoulou, Athena, Jasmin Meierhofer, Fabian Meyer, Takahiro Hayashi, Samuel Schneider, Emine Sager, and Rebecca Buller. 2021. “Re‐Programming and Optimization of a L‐Proline Cis‐4‐Hydroxylase for the Cis‐3‐Halogenation of Its Native Substrate.” ChemCatChem 13 (18): 3914–19. https://doi.org/10.1002/cctc.202100591.
Papadopoulou, Athena, et al. “Re‐Programming and Optimization of a L‐Proline Cis‐4‐Hydroxylase for the Cis‐3‐Halogenation of Its Native Substrate.” ChemCatChem, vol. 13, no. 18, June 2021, pp. 3914–19, https://doi.org/10.1002/cctc.202100591.
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