Abstract
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.
Keywords:
DoxA; hydroxylation; monooxygenase; resveratrol; substrate flexibility.
MeSH terms
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Apigenin / chemistry
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Apigenin / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Cytochrome P-450 Enzyme System / chemistry*
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Cytochrome P-450 Enzyme System / isolation & purification
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Cytochrome P-450 Enzyme System / metabolism*
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Doxorubicin / biosynthesis
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Ferredoxins / metabolism
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Flavanones / chemistry
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Flavanones / metabolism
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Flavones / chemistry
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Flavones / metabolism
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Hydroxylation
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Mixed Function Oxygenases / metabolism
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Models, Molecular
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Molecular Docking Simulation
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Oxidation-Reduction
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Protein Conformation
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Resveratrol
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Stilbenes / chemistry
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Stilbenes / metabolism*
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Streptomyces / enzymology*
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Streptomyces / metabolism
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Substrate Specificity
Substances
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6,7-dihydroxyflavone
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Bacterial Proteins
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Ferredoxins
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Flavanones
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Flavones
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Stilbenes
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3,3',4,5'-tetrahydroxystilbene
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Apigenin
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Doxorubicin
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Cytochrome P-450 Enzyme System
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Mixed Function Oxygenases
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doxA protein, Streptomyces peucetius
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naringenin
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Resveratrol