P450.sub.BM3 fused to phosphite dehydrogenase allows phosphite-driven selective oxidations

P450.sub.BM3 fused to phosphite dehydrogenase allows phosphite-driven selective oxidations

To facilitate the wider application of the NADPH-dependent P450.sub.BM3, we fused the monooxygenase with a phosphite dehydrogenase (PTDH). The resulting monooxygenase-dehydrogenase fusion enzyme acts as a self-sufficient bifunctional catalyst, accepting phosphite as a cheap electron donor for the re...

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Veröffentlicht in:Applied microbiology and biotechnology 2017-03, Vol.101 (6), p.2319
Hauptverfasser: Beyer, Nina, Kulig, Justyna K, Bartsch, Anette, Hayes, Martin A, Janssen, Dick B, Fraaije, Marco W
Format: Artikel
Sprache:eng
Schlagworte:
Analysis
Enzymes
Hydroxylation
Physiological aspects
Saturated fatty acids
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Zusammenfassung:To facilitate the wider application of the NADPH-dependent P450.sub.BM3, we fused the monooxygenase with a phosphite dehydrogenase (PTDH). The resulting monooxygenase-dehydrogenase fusion enzyme acts as a self-sufficient bifunctional catalyst, accepting phosphite as a cheap electron donor for the regeneration of NADPH.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-016-7993-7