Hydroxylation of Resveratrol with DoxA In Vitro: An Enzyme with the Potential for the Bioconversion of a Bioactive Stilbene
العنوان: | Hydroxylation of Resveratrol with DoxA In Vitro: An Enzyme with the Potential for the Bioconversion of a Bioactive Stilbene |
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المؤلفون: | Tae-Jin Oh, Joo-Ho Lee, Hemraj Rimal, Sang-Cheol Yu, Yamaguchi Tokutaro |
المصدر: | Journal of Microbiology and Biotechnology. 28:561-565 |
بيانات النشر: | Journal of Microbiology and Biotechnology, 2018. |
سنة النشر: | 2018 |
مصطلحات موضوعية: | Models, Molecular, 0301 basic medicine, Protein Conformation, Reductase, Resveratrol, Hydroxylation, Applied Microbiology and Biotechnology, Mixed Function Oxygenases, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Cytochrome P-450 Enzyme System, Biosynthesis, Stilbenes, Apigenin, Ferredoxin, chemistry.chemical_classification, Piceatannol, biology, organic chemicals, food and beverages, General Medicine, Flavones, biology.organism_classification, Streptomyces, Molecular Docking Simulation, 030104 developmental biology, Enzyme, chemistry, Biochemistry, Doxorubicin, Flavanones, Ferredoxins, Streptomyces peucetius, Oxidation-Reduction, Biotechnology |
الوصف: | The late-stage doxorubicin biosynthesis pathway acting enzyme (DoxA) from Streptomyces peucetius CYP129A2 exhibited substrate promiscuity towards the stilbene group of compounds such as resveratrol. DoxA along with two accessory enzymes ferrdoxin reductase and ferredoxin from spinach hydroxylated resveratrol at the 3'-position in vitro to produce piceatannol. The product was identified by HPLC-PDA and high-resolution HR-qTOF-ESI/MS analyses in positive mode. The ESI/MS fragments resembled the hydroxylated product of resveratrol. |
تدمد: | 1738-8872 1017-7825 |
DOI: | 10.4014/jmb.1711.11047 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::862a6673c2cd37a68dccd5f279a78b16 https://doi.org/10.4014/jmb.1711.11047 |
Rights: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....862a6673c2cd37a68dccd5f279a78b16 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 17388872 10177825 |
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DOI: | 10.4014/jmb.1711.11047 |