Insights into the stereospecificity of ketoreduction in a modular polyketide synthase
| Autor: | Peter F. Leadlay, David H. Kwan, Nadin Schläger, Frank Schulz, Manuela Tosin |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Stereochemistry
Context (language use) Stereoisomerism Biochemistry Polyketide chemistry.chemical_compound Stereospecificity Biosynthesis Polyketide synthase Catalytic Domain Physical and Theoretical Chemistry chemistry.chemical_classification biology Molecular Structure Organic Chemistry Active site Ketones Amino acid Kinetics chemistry Mutation biology.protein Oxidation-Reduction Polyketide Synthases Saccharopolyspora |
| Zdroj: | Organicbiomolecular chemistry. 9(7) |
| ISSN: | 1477-0539 |
| Popis: | Ketoreductase enzymes are responsible for the generation of hydroxyl stereocentres during the biosynthesis of complex polyketide natural products. Previous studies of isolated polyketide ketoreductases have shown that the stereospecificity of ketoreduction can be switched by mutagenesis of selected active site amino acids. We show here that in the context of the intact polyketide synthase multienzyme the same changes do not alter the stereochemical outcome in the same way. These findings point towards additional factors that govern ketoreductase stereospecificity on intact multienzymes in vivo. |
| Databáze: | OpenAIRE |
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