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28 results for “Catharanthus roseus”
Phytochemical Screening, Antioxidant and Antimicrobial Activity of Fabric Coated with Catharanthus Roseus Ethanolic Flowers Extract
<p>The aim of the present study was to evaluate the free radical scavenging and antimicrobial activity of fabric coated of the Catharanthus Roseus. Ethanol flowers extract. Free radical scavenging was determined by using 1, 1-diphenyl-2-picrylhydrazyl (DPPH), Reducing power, Hydroxyl radical scavenging assay and antimicrobial activity of Staphylococcus aureus, Escherichia coli and standard drug of Streptomycin using disc diffusion method. This inhibition was observed with the individual extracts and when they were used in lower concentrations with ineffective antibiotics. The present investigation clearly indicates that the Catharanthus Roseus possesses antioxidant properties and serve as free radical inhibitors or scavengers, acting possibly as primary antioxidants.</p><p>Keywords</p><p>Catharanthus Roseus, Fabric coated, DPPH, Staphylococcus aureus Escherichia coli, Streptomycin, Antioxidant,</p>
Catharanthus roseus
<p>This plant produces terpenoids called indole alkaloids. <br> The plant sections contain indole alkaloids, which constitute a significant source of the compound. <br> Leaves have substantial anti-hyperglycemic action and are widely used in traditional medicine to lower blood sugar levels. <br> ajmalicine, serpentine, and antihypertensive roots. <br> Stems and Leaves: Vincristine and vinblastine are two essential dimeric alkaloids that treat cancer. <br> Various forms of lymphoma and leukaemia are treated using vincristine and vinblastine alkaloids. <br> In traditional medicine, it is used by many civilizations to treat conditions including diabetes, cancer, ulcers, hypertension, Alzheimer's, fever, and hemostasis.</p>
Data for: Single-cell multi-omics in the medicinal plant Catharanthus roseus
<p>Advances in omics technologies now permit the generation of highly contiguous genome assemblies, detection of transcripts and metabolites at the level of single cells and high-resolution determination of gene regulatory features. Here, using a complementary, multi-omics approach, we interrogated the monoterpene indole alkaloid (MIA) biosynthetic pathway in <em>Catharanthus roseus</em>, a source of leading anticancer drugs. We identified clusters of genes involved in MIA biosynthesis on the eight <em>C. roseus</em> chromosomes and extensive gene duplication of MIA pathway genes. Clustering was not limited to the linear genome, and through chromatin interaction data, MIA pathway genes were present within the same topologically associated domain, permitting the identification of a secologanin transporter. Single-cell RNA-sequencing revealed sequential cell-type-specific partitioning of the leaf MIA biosynthetic pathway that, when coupled with a single-cell metabolomics approach, permitted the identification of a reductase that yields the bis-indole alkaloid anhydrovinblastine. We also revealed cell-type-specific expression in the root MIA pathway.</p>
Fig. 4 in Molecular and biochemical characterization of Catharanthus roseus perivine-N -methyltransferase
Fig. 4. The organs of C. roseus display similar CrPeNMT and DhtNMT enzyme activities. A) Enzyme activity profiles of C. roseus leaf pairs 1(LP1), 2 (LP2), 3 (LP3), flowers (FL) and roots (RT) for CrPeNMT (A) and DhtNMT B) are displayed.
Fig. 3 in Molecular and biochemical characterization of Catharanthus roseus perivine-N -methyltransferase
Fig. 3. Recombinant CrPeNMT converts perivine to Vobasine. UPLC-MS analyses show that commercially available perivine (Rt 2.05, m/z+ 339) is not modified when assayed with empty vector (pET 30b) expressing bacterial extracts in the presence of 2 mM AdoMet. Perivine is completely converted to Vobasine (Rt 3.40, m/z+ 353) by bacterial extracts expressing recombinant CrPeNMT under the same conditions. The insets contain the UV and MS spectra of perivine and Vobasine, respectively.
Fig. 2 in Molecular and biochemical characterization of Catharanthus roseus perivine-N -methyltransferase
Fig. 2. Identification of MIAs in C. roseus MIA extracts that were methylated by recombinant CrPeNMT. Ultra performance liquid chromatography combined with MS showed that recombinant CrPeNMT converted an MIA (Rt 2.05, m/z+ 339) present in Catharanthus extracts into a methylated MIA (Rt 3.40, m/z+ 353) when assays are provided with 2 mM S-adenosyl-L-methionine. The UPLC elution and mass profiles of the MIA substrate and its methylated product suggested that perivine might be a possible substrate for CrPeNMT to generate a methylated form of this MIA.
Fig. 1 in Molecular and biochemical characterization of Catharanthus roseus perivine-N -methyltransferase
Fig. 1. The assembly of monoterpenoid indole alkaloids in different plant species involve substrate specific N-methylations catalysed by members of a recently described tocopherol-like methyltransferase gene family. The formation of strictosidine from secologanin and tryptamine involves the enzyme, strictosidine synthase (STR), while strictosidine-β-glucosidase (SGD) generates reactive intermediates, including 4, 21-dhydrogeissoschizine that is converted to 19Egeissoschizine by geissoschizine synthases (GS). This MIA is converted via multiple known enzyme reactions to 16-methoxy-2,3-dihydro-3-hydroxytabersonine which is N-methylated via dihydrotabersonine-N-methyltransferase (DhtNMT) to form 16-methoxy-2,3-dihydro-3-hydroxy-N-methyltabersonine that is ultimately converted into vindoline. While the conversion of 19E-geissoschizine to picrinine remains to be established, both Rauvolfia serpentina and Vinca minor express picrinine- N-methyltransferases (PiNMT) that converts picrinine to N-methypicrinine (ervincine). The formation of polyneuridine aldehyde from 19E-geissoschizine involves sarpagan bridge enzyme (SBE). Additional enzymes [polyneuridine aldehyde esterase (PNAE), vinorine synthase (VS), vinorine hydrolase, vinorine reductase and acetyajmaline esterase (AAE) convert vinorine to norajmaline. Two separate tocopherol-like methyltransferases (norajmaline N-methyltransferase (NNMT) and ajmaline N-methyltransferase convert norajmaline to ajmaline and Nβ-ajmaline, respectively. C. roseus and related species accumulate periformylene, an oxidixed form of Nβ-methylperivine. This MIA is derived from uncharacterized biochemical conversions of polyneuridine aldehyde to pericyclivine and to perivine. The formation of vobasine from perivine involves CrPeNMT found in C. roseus.
Fig. 4 in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 4. GOLD's highest rated poses for (¡)-tabersonine and (þ)-vincadifformine into the V19H model generated from the 3ruk template with and without increased flexibility in the binding site residues. ()-tabersonine (B) and (+)-vincadifformine (A) best poses are shown in a rigid binding site (top) and a flexible binding site (bottom). The 19C is labelled in both ligands (arrows), and neither ligand is docked in the correct orientation for oxidation in a rigid binding site (top. However, in a flexible binding site, (+)-vincadifformine is in the correct orientation for 19C oxidation (bottom; B), whereas ()-tabersonine is not (bottom; A). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 5 in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 5. The four residues in the V19H (left) and T3O (right) binding sites that were predicted to affect the opposite enantioselectivity of these highly homologous enzymes using models created on the 3ruk template. Residues shown in the V19H pocket are K106, S312, A376, and F377. Residues shown in the T3O pocket are R105, T311, P375, and L377. The model generated for T19H (3ruk template) looks identical to the T3O pocket, and the correlating residues are R101, T310, P374, and L375.
Fig. 3 in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 3. Saturation kinetics of V19H: comparative (þ)-vincadifformine saturation curve in the absence or presence of (¡)-vincadifformine. The rate of (+)-vincadifformine consumption by V19H was reduced in the presence of 3 μM of ()-vincadifformine within the range of 15–20 μM of substrate yet remains unchanged at low and saturated concentrations. Error bars indicate the standard deviation from three technical replicate assays.
Fig. 7. The V19H four-point mutant coupled with T3R in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 7. The V19H four-point mutant coupled with T3R converts (¡)-tabersonine to 2,3-dihydro-3-hydroxytabersonine. Traces from in vitro experiments with ()-tabersonine (1) and V19H four-point mutant microsomes or T3O microsomes in the absence or presence of purified recombinant T3R are shown. Yeast microsomes containing the V19H 4-point mutant (red) (V19HL106R–S312T-A376P–F377L) convert ()-tabersonine to tabersonine 2,3-epoxides (5) in the absence of T3R, and to 2,3-dihydro-3-hydroxytabersonine in the presence of T3R. Yeast microsomes containing wild-type T3O (blue) were used as positive controls for tabersonine-2,3-epoxide (5) and 2,3-dihydro-3-hydroxytabersonine biosynthesis in the absence and presence of T3R, respectively. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 2 in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 2. Representation of the 3ruk V19H model superimposed onto the 3ruk template and the location of the catalytic heme. V19H model (purple) is shown in purple, and the 3ruk template is shown in pink with the heme binding site in yellow. The H-bond interaction (green) between PHE443 and CYS450, the first and eighth residues of the heme binding site, which is responsible for the beta bulge (yellow) around the heme cofactor (black). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 1 in Site directed mutagenesis of Catharanthus roseus (+)-vincadifformine 19-hydroxylase (CYP71BY3) results in two distinct enzymatic functions
Fig. 1. The formation of (þ)- and (¡)-aspidosperma MIAs in Catharanthus roseus. In multiple C. roseus tissues, the ()-aspidosperma pathways begin with the biosynthesis of ()-tabersonine (1) from O-acetylstemmadenine (18) through acetylstemmadenine oxygenase (ASO), geissoschizine synthase (GS), and hydrolase 1 (HL1), whereas the (+)-aspidosperma pathway requires hydrolase 3 or 4 (HL3/4) to produce (+)-vincadifformine (15). Leaf-specific enzymes (black) convert ()-tabersonine (1) to vindoline (6), which accumulates in the leaves, while root-specific enzymes (purple) are responsible for the formation of two major root alkaloids, lochnericine (7) and h¨orhammericine (8). A third major root alkaloid, (+)-echitovenine (17) is derived from (+)-vincadifformine (15) via (+)-minovincinine (16) by separate root-specific (blue) enzymes. The remaining ()-aspidosperma alkaloids shown are derived chemically (grey box) from ()-tabersonine (1) to generate ()-vincadifformine (12) or enzymatic conversion by T19H to form 19-hydroxytabersonine (10) or its 19-O acetyltabersonine (11) by the action of TAT. These MIAs [()-vincadifformine (12), 19-hydroxytabersonine (10) and 19-O acetyltabersonine (11)] do not naturally accumulate in C. roseus. T16H: tabersonine 16-hydroxylase [CYP71D12 (T16H1) or CYP71D351 (T16H2); 16OMT: tabersonine 16-O-methyltransferase; T3O: tabersonine 3-oxygenase (CYP71D1V2); T3R: tabersonine 3-reductase; NMT: N-methyltransferase; D4H: desacetoxyvindoline 4-hydroxylase; DAT: deacetylvindoline O-acetyltransferase; TEX: tabersonine epoxidase [CYP71D521 (TEX1) or CYP71D347 (TEX2)]; T19H: tabersonine 19-hydroxylase (CYP71BJ1); TAT: tabersonine 19-acetyltranferase; V19H: (+)-vincadifformine 19-hydroxylase (CYP71BY3); MAT: minovincinine 19-O-acetyltransferase. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4 in The complexity of sound quantification of specialized metabolite biosynthesis: The stress related impact on the alkaloid content of Catharanthus roseus
Fig. 4. The stress-related increase of the concentration of natural products. In principle, two major effects are responsible for the stress-related increase, i. e., the decrease of the reference value (e.g. dry weight), and an enhancement of biosynthetic activity. The latter one is due either to stress-related up-regulation ("active increase" of enzymatic activity) or a "passive shift" cause by the stress-related overreduction due to stomatal closure. Decreases of factors are displayed in red, the related enhancements in blue. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3 in The complexity of sound quantification of specialized metabolite biosynthesis: The stress related impact on the alkaloid content of Catharanthus roseus
Fig. 3. Dry weight, alkaloid concentration, and alkaloid content in leaves of Catharanthus roseus plants under salt stress. (a): Dry weight of the entire leaves; (b): Concentration of alkaloids in old leaves; (c): Concentration of alkaloids in young leaves; (d): Total alkaloids content in all aerial plant parts. Differentiation between young and old leaves is mentioned in the Materials and methods section. Different lower-case letters on top of the columns for each period of time (10 and 20 days) indicate significant differences (P ≤ 0.05) as calculated using the least significant difference (LSD) test; n = 8. Every period has 5 bars, and these bars from left to right are control, 100 mM, 200 mM, 300 mM, 400 mM NaCl solution, respectively. The bars display the standard deviation.
Fig. 1 in The complexity of sound quantification of specialized metabolite biosynthesis: The stress related impact on the alkaloid content of Catharanthus roseus
Fig. 1. Evapotranspiration rate of drought-stressed Catharanthus roseus plants. The evapotranspiration rates for mild (20% watering) and severe drought stress (40% watering) were obtained by calculating the amount of water lost. Control plant results were used as a reference to normalize the rate. Arrows indicate the days of sampling.
Fig. 7 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 7. Molecular models of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565. (A) Backbone overlays of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565 models are shown with the alpha-carbon RMSD amongst CYP72A1, CYP72A564 and CYP72A565 depicted from green (0.0 Å) to yellow (3.0 Å) to red (4.5 Å). (B) SRS regions in CYP72A proteins shown with predicted substrate contact residues (gray fill). (C) Identical versus (D) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A564 (orange). (E) Identical versus (F) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A565 (rose).
Fig. 5 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 5. Area of loganic acid, loganin and products from in vitro reconstitution assays conducted with full-length Camptotheca His6-tagged CPR1. Integrated areas from LC-MS analyses of purified His6-tagged CYP72A proteins reconstituted with full-length His6-tagged Caa CPR1 are shown for no NADPH (gray) and plus NADPH (gray slashed) reactions.
Fig. 2. CYP72A in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 2. CYP72A multiple sequence alignment. Signal anchor domain fusion of CYP72A565 into CYP72A564 is underlined; SRS regions are underlined in bold; predicted substrate contacts within 4.5 Å of loganic acid/loganin are gray-filled.
Fig. 1 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 1. Proposed divergence of the TIA pathway between Camptotheca and Catharanthus. After 7-deoxyloganic acid hydroxylase (7DLH) converts 7-deoxyloganic acid to loganic acid, the pathways in these two species diverge. The Catharanthus pathway uses loganic acid methyltransferase (LAMT) to convert loganic acid into loganin and secologanin synthase (SLS) to convert loganin into secologanin. The Camptotheca pathway bypasses LAMT and uses secologanic acid synthase (SLAS) to metabolize loganic acid directly to secologanic acid.
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