Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate
| Autor: | Katarzyna Kuczek, Hubert Bartosz-Bechowski, Magdalena Kotowska, Krzysztof Pawlik, Aleksandra Smulczyk-Krawczyszyn |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Hydrolases DNA Mutational Analysis Molecular Sequence Data Streptomyces coelicolor Acetates Applied Microbiology and Biotechnology Substrate Specificity Polyketide Thioesterase Bacterial Proteins Polyketide synthase Catalytic Domain Hydrolase Amino Acid Sequence Enzymology and Protein Engineering chemistry.chemical_classification Ecology biology Active site Streptomyces fradiae biology.organism_classification Protein Structure Tertiary Butyrates Kinetics Biochemistry chemistry biology.protein Propionate Thiolester Hydrolases Fatty Acid Synthases Propionates Polyketide Synthases Sequence Alignment Food Science Biotechnology |
| Zdroj: | Applied and environmental microbiology. 75(4) |
| ISSN: | 1098-5336 |
| Popis: | Type II thioesterases (TE IIs) were shown to maintain the efficiency of polyketide synthases (PKSs) by removing acyl residues blocking extension modules. However, the substrate specificity and kinetic parameters of these enzymes differ, which may have significant consequences when they are included in engineered hybrid systems for the production of novel compounds. Here we show that thioesterase ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3(2) is able to hydrolyze acetyl, propionyl, and butyryl residues, which is consistent with its editing function. This enzyme clearly prefers propionate, in contrast to the TE IIs tested previously, and this indicates that it may have a role in control of the starter unit. We also determined activities of ScoT mutants and concluded that this enzyme is an α/β hydrolase with Ser90 and His224 in its active site. |
| Databáze: | OpenAIRE |
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