barks of Taxus chinensis
Baccatin III/(2α,5β,7β,10β,13α)-4,10-Diacetoxy-1,7,13-trihydroxy-9-oxo-5,20-epoxytax-11-en-2-yl benzoate/7,11-Methano-5H-cyclodeca[3,4]benz[1,2-b]oxet-5-one, 6,12b-bis(acetyloxy)-12-(benzoyloxy)-1,2a,3,4,4a,6,9,10,11,12,12a,12b-dodecahydro-4,9,11-trihydroxy-4a,8,13,13-tetramethyl-, (2aR,4S,4aS,6R,9S,11S,12S,12aR,12bS)-
713.6±60.0 °C at 760 mmHg
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For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:27548-93-2) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Breast and colon cancers are leading causes of cancer-related deaths globally. Plants are a potential source of natural products that may be used for the treatment of cancer. Ferula hermonis (FH) is reported to have diverse therapeutic effects. However, there are few reports on the in vitro anticancer potential of FH extract. Our results showed that the Ferula hermonis root hexane extract (FHRH) can induce dose-dependent cytotoxic effects in breast and colon cancer cells with MTT IC50 values of 18.2 and 25 μg/ml, respectively. The FHRH extract induced apoptosis in both breast and colon cancer cells; this was confirmed by light and nuclear staining, q-PCR, and caspase 3/7 activation. This study also demonstrated the antitumor activity of FHRH in 9,10-dimethylbenz[α]anthracene DMBA-induced rodent mammary tumor model. The GC/MS analysis revealed the presence of 3,5-Dimethylbenzenemethanol, Alpha-Bisabolol, Alpha-pinene, Beta-pinene, and Baccatin III that have various pharmacological potentials. Overall, the present study suggests that FHRH extract possesses anticancer potential which is mediated through apoptotic effects in MDA-MB-231 and LoVo cells. The present study also considered a basis for further investigations into the potential use of FHRH extract as an anticancer therapy for breast and colon cancers.
Effects of Hexane Root Extract of Ferula hermonis Boiss. on Human Breast and Colon Cancer Cells: An In Vitro and In Vivo Study.
Abutaha N1, Nasr FA2, Al-Zharani M3, Alqahtani AS2, Noman OM2, Mubarak M4, Abdelhabib S5, Wadaan MA1.
2019 Jul 15
Taxoid 10β-O-acetyltransferase (DBAT) is the key enzyme to produce baccatin III, a key precursor in paclitaxel synthesis, by acetyl group transfer from acetyl-CoA to the C10 hydroxyl of 10-deacetylbaccatin III. In this study, the recombinant DBAT (rDBAT) was immobilized by cross-linked enzyme aggregates (CLEAs). To further optimize the enzyme recovery, single-factor experiment and response surface methodology were applied. 60% ammonium sulfate as precipitant, 0.05% glutaraldehyde as fixing agent, pH 7.0, 2 h as cross-linking time, 30 °C as cross-linking temperature were confirmed to be the optimum conditions to prepare the CLEAs-rDBAT in single-factor experiment. In addition, 62% for ammonium sulfate saturation, 0.15% for glutaraldehyde, and pH 6.75 were confirmed to be the optimum conditions with averagely 73.9% activity recovery in 3 replications, which was consistent with the prediction of response surface methodology. After cross-linking, the optimum temperature of CLEAs-rDBAT rose up to 70 °C and CLEAs-rDBAT could be recycled for three times.
Baccatin III; CLEAs; Cross-linking; DBAT; Response surface methodology
Optimization of Baccatin III Production by Cross-Linked Enzyme Aggregate of Taxoid 10β-O-Acetyltransferase.
You LF1,2, Wei T1,3, Zheng QW1,3, Jiang BH4, Lin JF5,6, Guo LQ7,8.
Taxoid 10β-O-acetyl transferase (DBAT) is a key enzyme in the biosynthesis of the famous anticancer drug paclitaxel, which catalyses the formation of baccatin III from 10-deacetylbaccatin III (10-DAB). However, the activity essential residues of the enzyme are still unknown, and the acylation mechanism from its natural substrate 10-deacetylbaccatin III and acetyl CoA to baccatin III remains unclear. In this study, the homology modelling, molecular docking, site-directed mutagenesis, and kinetic parameter determination of the enzyme were carried out. The results showed that the enzyme mutant DBATH162A resulted in complete loss of enzymatic activity, suggesting that the residue histidine at 162 was essential to DBAT activity. Residues D166 and R363 which were located in the pocket of the enzyme by homology modelling and molecular docking were also important for DBAT activity through the site-directed mutations. Furthermore, four amino acid residues including S31 and D34 from motif SXXD, D372 and G376 from motif DFGWG also played important roles on acylation. This was the first report of the elucidation of the activity essential residues of DBAT, making it possible for the further structural-based re-design of the enzyme for efficient biotransformation of baccatin III and paclitaxel.
Baccatin III; Homology modelling; Molecular docking; Site-directed mutagenesis; Taxoid 10β-O-acetyl transferase
Activity Essential Residue Analysis of Taxoid 10β-O-Acetyl Transferase for Enzymatic Synthesis of Baccatin.
You LF1,2, Wei T1,3, Zheng QW1,3, Lin JF4,5, Guo LQ6,7, Jiang BH8, Huang JJ1.
Baccatin III is a natural product isolated from Pacific yew tree and related species. Baccatin III reduces tumor progression by inhibiting the accumulation and suppressive function of MDSCs.