6533b821fe1ef96bd127c50d
RESEARCH PRODUCT
Deoxysarpagine Hydroxylase — A Novel Enzyme Closing a Short Side Pathway of Alkaloid Biosynthesis in Rauvolfia
Bingwu YuMartin RuppertJoachim Stöckigtsubject
Deoxysarpagine hydroxylase activityLightCytochromeStereochemistryClinical BiochemistryPharmaceutical ScienceBiochemistryRauwolfiaIndole AlkaloidsHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemRauvolfia serpentinaDrug DiscoveryMolecular BiologyPlant Proteinschemistry.chemical_classificationCarbon MonoxidebiologyChemistryDeoxysarpagine hydroxylaseCytochrome cOrganic ChemistryTemperatureHydrogen-Ion ConcentrationMonooxygenasebiology.organism_classificationSecologanin Tryptamine AlkaloidsKineticsEnzymeBiochemistrybiology.proteinMolecular MedicineAryl Hydrocarbon HydroxylasesNADPdescription
Microsomal preparations from cell suspension cultures of the Indian plant Rauvolfia serpentina catalyze the hydroxylation of deoxysarpagine under formation of sarpagine. The newly discovered enzyme is dependent on NADPH and oxygen. It can be inhibited by typical cytochrome P450 inhibitors such as cytochrome c, ketoconazole, metyrapone, tetcyclacis and carbon monoxide. The CO-effect is reversible with light (450 nm). The data indicate that deoxysarpagine hydroxylase is a novel cytochrome P450-dependent monooxygenase. A pH optimum of 8.0 and a temperature optimum of 35 degrees C were determined. K(m) values were 25 microM for NADPH and 7.4 microM for deoxysarpagine. Deoxysarpagine hydroxylase activity was stable in presence of 20% sucrose at -25 degrees C for3 months. The analysis of presence of the hydroxylase in nine cell cultures of seven different families indicates a very limited taxonomic distribution of this enzyme.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-08-01 | Bioorganic & Medicinal Chemistry |