1. Catalytic role of the C-terminal domains of a fungal non-reducing polyketide synthase
- Author
-
David Ivison, Andy M. Bailey, Katja M. Fisch, Thomas J. Simpson, Colin M. Lazarus, Russell J. Cox, and Elizabeth Skellam
- Subjects
Stereochemistry ,Methylation ,Catalysis ,Fungal Proteins ,Hydrolysis ,In vivo ,Polyketide synthase ,Materials Chemistry ,Cloning, Molecular ,Glutamine amidotransferase ,ATP synthase ,biology ,Molecular Structure ,Chemistry ,Metals and Alloys ,General Chemistry ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,Biochemistry ,Terpene synthase N terminal domain ,Ceramics and Composites ,biology.protein ,Biocatalysis ,Oxidation-Reduction ,Polyketide Synthases - 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.
- Published
- 2010