title: Catalytic role of the C-terminal domains of a fungal non-reducing polyketide synthase.
abstract: 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.
authors.affiliation: School of Chemistry, University of Bristol, Bristol, UK, BS8 1TS.
authors.forename: Katja M
authors.initials: KM
authors.lastname: Fisch
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Skellam
authors.forename: David
authors.initials: D
authors.lastname: Ivison
authors.forename: Russell J
authors.initials: RJ
authors.lastname: Cox
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Bailey
authors.forename: Colin M
authors.initials: CM
authors.lastname: Lazarus
authors.forename: Thomas J
authors.initials: TJ
authors.lastname: Simpson
mesh_terms: 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
chemical_list: D005656:Fungal Proteins; D048630:Polyketide Synthases