Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

Originalpublikation

Piech, Oliver; Cox, Russell J.: Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase. In: RSC Advances 31 (2020), Nr. 10, 18469. DOI: https://doi.org/10.1039/D0RA04026F

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Zusammenfassung:
A structural model of the enoyl reductase (ER) catalytic domain of the fungal highly-reducing polyketide synthase squalestatin tetraketide synthase (SQTKS) was developed. Simulated docking of substrates and inhibitors allowed the definition of active site residues involved in catalysis and substrate selectivity. These were investigated in silico with the aim of extending the substrate scope. Residues were identified which limit the substrate selectivity of the SQTKS ER, and these were mutated and the engineered ER domain assayed in vitro. Significant changes to the programming of the mutant SQTKS ER domains were observed allowing the processing of longer and more methylated substrates.
Lizenzbestimmungen: CC BY-NC 4.0 Unported - https://creativecommons.org/licenses/by-nc/3.0/
Publikationstyp: Article
Publikationsstatus: publishedVersion
Erstveröffentlichung: 2020
Schlagwörter (englisch): enoyl reductase (ER) catalytic domain, squalestatin tetraketide synthase (SQTKS), model
Fachliche Zuordnung (DDC): 540 | Chemie

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