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 suggest that methylation occurs prior to aromatisation.
Fisch
Katja M
KM
School of Chemistry, University of Bristol, Bristol, UK, BS8 1TS.
Skellam
Elizabeth
E
Ivison
David
D
Cox
Russell J
RJ
Bailey
Andrew M
AM
Lazarus
Colin M
CM
Simpson
Thomas J
TJ
D055162:Biocatalysis; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D008745:Methylation; D015394:Molecular Structure; D010084:Oxidation-Reduction; D048630:Polyketide Synthases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D005656:Fungal Proteins; D048630:Polyketide Synthases