Biotransformation of Flavone by CYP105P2 from Streptomyces peucetius
| Autor: | Tae-Jin Oh, Na-Rae Lee, Saurabh Bhattarai, Jae Kyung Sohng, Narayan Prasad Niraula |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Stereochemistry
Hydroxylation medicine.disease_cause Applied Microbiology and Biotechnology Mass Spectrometry Metabolic engineering chemistry.chemical_compound Cytochrome P-450 Enzyme System Biotransformation Escherichia coli medicine NADH NADPH Oxidoreductases Chromatography High Pressure Liquid biology Pseudomonas putida Cytochrome P450 General Medicine Flavones biology.organism_classification Streptomyces Metabolic Engineering Biochemistry chemistry Docking (molecular) biology.protein Ferredoxins Streptomyces peucetius Biotechnology |
| Zdroj: | Journal of Microbiology and Biotechnology. 22:1059-1065 |
| ISSN: | 1738-8872 1017-7825 |
| DOI: | 10.4014/jmb.1201.01037 |
| Popis: | Biocatalytic transfer of oxygen in isolated cytochrome P450 or whole microbial cells is an elegant and efficient way to achieve selective hydroxylation. Cytochrome P450 CYP105P2 was isolated from Streptomyces peucetius that showed a high degree of amino acid identity with hydroxylases. Previously performed homology modeling, and subsequent docking of the model with flavone, displayed a reasonable docked structure. Therefore, in this study, in a pursuit to hydroxylate the flavone ring, CYP105P2 was co-expressed in a two-vector system with putidaredoxin reductase (camA) and putidaredoxin (camB) from Pseudomonas putida for efficient electron transport. HPLC analysis of the isolated product, together with LCMS analysis, showed a monohydroxylated flavone, which was further established by subsequent ESI/MS-MS. A successful 10.35% yield was achieved with the whole-cell bioconversion reaction in Escherichia coli. We verified that CYP105P2 is a potential bacterial hydroxylase. |
| Databáze: | OpenAIRE |
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