Catalytic role of the C-terminal domains of a fungal non-reducing polyketide synthaseElectronic supplementary information (ESI) available: experimental details. See DOI: 10.1039/c0cc01162b

• Main Authors: Fisch, Katja M, Skellam, Elizabeth, Ivison, David, Cox, Russell J, Bailey, Andrew M, Lazarus, Colin M, Simpson, Thomas J
• Format: Article
• Language: English
• ISSN: 1359-7345; 1364-548X
• DOI: 10.1039/c0cc01162b

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. Truncated methylorcinaldehyde synthase retains a hydrolytic release activity in the absence of reductive chain release and chain-length is not controlled by the reductive release domain; experiments using a methyltransferase inhibitor suggest that methylation occurs prior to aromatisation.