Catalytic role of the C-terminal domains of a fungal non-reducing polyketide synthase
The in vivo activity of truncated forms of methylorcinaldehyde synthase shows that the synthase retains a hydrolytic release activity in the absence of reductive chain release and that chain-length is not controlled by the reductive release domain; experiments using a methyltransferase inhibitor sug...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2010-01, Vol.46 (29), p.5331-5333 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | The in vivo activity of truncated forms of methylorcinaldehyde synthase shows that the synthase retains a hydrolytic release activity in the absence of reductive chain release and that chain-length is not controlled by the reductive release domain; experiments using a methyltransferase inhibitor suggest that methylation occurs prior to aromatisation. |
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ISSN: | 1359-7345 1364-548X |
DOI: | 10.1039/c0cc01162b |