16 results about "Isoamoenylin" patented technology

This invention provides a chalcone isopentenyltransferase gene. GiPT16 This invention relates to the GiPT16 protein, amplification primer set, and applications, belonging to the field of biogenetics technology. It is based on *Glycyrrhiza inflata* (GiPT16 protein, amplification primer set, and applications). Glycyrrhiza inflata Using whole-genome sequencing data and a reverse genetics strategy, the key aromatic isopentenyltransferase GiPT16, involved in the isopentenylation modification of chalcone active ingredients, was successfully identified and functionally characterized. This enzyme was confirmed to specifically catalyze the biosynthesis of psoralen and glycyrrhizin C using DMAPP as a donor. It is the first chalcone isopentenyltransferase characterized in *Glycyrrhiza inflata*, filling a gap in the study of key enzymes in the chalcone isopentenylation metabolic pathway of this species and providing important evidence for further elucidating the molecular mechanisms of quality formation in *Glycyrrhiza inflata* medicinal materials.

This invention belongs to the field of synthetic biology and microbial engineering, and discloses a chemical-biological method for preparing the isopentenyl bibenzyl compound 2-isopentenyl-3,3',4',5-tetrahydroxybibenzyl (NPB-1575) which has anti-ischemic stroke activity. The specific disclosed method includes: (1) chemically synthesizing the substrate dihydropiperidine; (2) constructing an engineered Escherichia coli strain based on the isopentenyl utilization pathway, co-expressing hydroxyethylthiazol kinase, isopentenyl phosphokinase, isopentenyl pyrophosphate isomerase and specific isopentenyl transferase, and efficiently synthesizing the isopentenyl donor; (3) using this strain to catalyze dihydropiperidine in whole cells, the yield in a 200L fermenter can reach 2.54g / L, which is nearly 40 times higher than the existing method; (4) obtaining NPB-1575 with a purity >98.5% by macroporous adsorption resin and normal / reversed phase chromatography and recrystallization. This method uses readily available raw materials, involves simple steps, is environmentally friendly, and yields high purity, laying the foundation for the development of NPB-1575 as a new drug for ischemic stroke and showing significant application potential.

The application provides a fusariobutenolide derivative 4''-O-isopentenyl fusariobutenolide C, and a structural formula of the compound is provided.The 4''-O-isopentenyl fusariobutenolide C can significantly inhibit the growth of seven human routine pathogenic bacteria in antibacterial activity testing, and the MIC is 8.6-28.3 μg / mL, and the antibacterial effect on one strain of human drug-resistant pathogenic bacteria, methicillin-resistant Staphylococcus aureus, is significant, and the MIC is 16.8 μg / mL, and the 4''-O-isopentenyl fusariobutenolide C can be applied to preparation of antibacterial drug precursors, and lays a material foundation for next-step biological medicine development and application of antibacterial components.

The invention discloses a preparation method of all-trans-farnesol through a three-enzyme cascade reaction. The invention firstly provides a mutant of farnesyl pyrophosphate synthase, and the amino acid sequence of the mutant is shown as SEQ ID No.3. Compared with a wild type, the mutant is applied to enzyme catalytic synthesis of farnesol, so that the conversion rate of a gold product is remarkably improved. The invention also provides a three-enzyme cascade reaction preparation method of farnesol, which comprises the following steps: in the same reaction system, dimethyl allyl diphosphate is used as a substrate; according to the method, isopentenyl diphosphate isomerase, farnesyl pyrophosphate synthase or a mutant thereof and farnesyl pyrophosphatase are used as catalytic enzymes for enzymatic reaction to prepare all-trans-farnesyl alcohol. According to the invention, in a single reaction system, three key enzymes are combined for application, so that continuous catalysis, high-efficiency and high-selectivity preparation of all-trans-farnesol is realized, process steps are simplified, and a new way is provided for green and efficient preparation of farnesol.

The invention discloses an isopentenyl transferase and an application of the isopentenyl transferase in synthesis of bakuchiol. Specifically, recombinant saccharomyces cerevisiae for expressing the isopentenyl transferase is constructed, the isopentenyl transferase CcPT6 from fructus psoraleae is obtained through screening, the isopentenyl transferase CcPT6 can catalyze an isopentenylation reaction of a coumaric acid substrate to generate bakuchiol, and the activity of the isopentenyl transferase CcPT6 is higher than that of a reported sequence BAK36. The CcPT7 is obtained by truncating 54 amino acids at the N end of the CcPT6, the catalytic activity is improved by 74%, and the activity of the CcPT7 is higher than that of a reported BAK36 mutant. In addition, the invention also provides a recombinant saccharomyces cerevisiae and yarrowia lipolytica engineering strain for integrally expressing the isopentenyl transferase CcPT6 or CcPT7, so that the artificial biosynthesis of the bakuchiol is realized. The discovery of the isopentenyl transferase and the construction of the recombinant engineering strain have important meanings for promoting the biosynthesis of the bakuchiol.

The invention discloses an oxygen isopentenyl transferase participating in synthesis of sesquiterpene coumarin and an application of the oxygen isopentenyl transferase. Belongs to the technical field of gene engineering. The invention discloses an open reading frame sequence of a Xinjiang ferula oxygen isopentenyl transferase FsPT9 gene and an amino acid sequence coded by the Xinjiang ferula oxygen isopentenyl transferase FsPT9 gene. The FsPT9 gene is obtained by screening and cloning based on combined analysis of multi-omics data of ferula sinkiang, a yeast expression vector is constructed, and a catalytic mechanism of the FsPT9 is identified in vitro by taking 7-hydroxycoumarin and farnesyl pyrophosphate as substrates. A yeast heterologous expression system proves that the FsPT9 can catalyze 7-hydroxycoumarin and farnesyl pyrophosphoric acid to generate umbelliferone. The invention discloses a key enzyme for initial synthesis of sesquiterpene coumarin for the first time, and the key enzyme is an oxygen isopentenyl transferase which is reported for the first time and is used for catalyzing three isopentenyl units at the same time, so that theoretical guidance is provided for synthesis and transformation of pharmacodynamic substances of asafetida sesquiterpene coumarin.

The application discloses a synthetic method of natural product Moracin N and belongs to the technical field of organic synthesis. The application takes an aldehyde containing a benzene ring as a starting raw material, introduces an isopentenyl group on the benzene ring through a Friedel-Crafts reaction, connects a hydroxyl protecting group to a No. 4 position hydroxyl group of the benzene ring to obtain an intermediate II, then uses a phosphorus ylide reagent to prepare the intermediate II into gem-dibromo olefin to obtain an intermediate III, then under the catalysis of a base and a copper catalyst, the gem-dibromo vinyl group is coupled with an ortho hydroxyl group to form a benzofuran ring to obtain an intermediate IV, then 3,5-dihydroxy bromobenzene is introduced to the right side of the benzofuran ring of the intermediate IV through a Suzuki-Miyaura reaction to obtain an intermediate VI, and finally the hydroxyl protecting group of the intermediate VI is removed to obtain Moracin N. The synthetic route of the application is simple, the reaction condition is mild, the safety is high, the required raw material is cheap and easy to obtain, the total cost is low, and the application is suitable for industrialized preparation.

This invention discloses a protein with O-isopentenyltransferase activity, related biomaterials, and applications, belonging to the field of biotechnology. This invention screened and cloned an O-isopentenyltransferase gene (GlOPT), which can be used to prepare O-isopentenyltransferase. Experiments have confirmed that this O-isopentenyltransferase can catalyze the in vitro conversion of 8-hydroxybergamot lactone to arugulatin; catalyze the conversion of bergamotol to isoimperatorin; and catalyze the conversion of xanthotoxin to imperatorin. This provides technical support for the production of isopentenyl furanocoumarin-like active ingredients from arugula, lays the foundation for research on the biosynthetic pathways of coumarin compounds, and has significant theoretical and practical implications.

This invention relates to isopentenyl flavonoids, their preparation methods, and applications, belonging to the field of natural product chemistry. Specifically, it involves the separation of five isopentenyl flavonoids—daphengiratriprenylone D, (3"'R)-daphnegiravone F, (3"'S)-daphnegiravone F, daphnegiravone E, and daphnegiralin H—from *Daphne giraldii* Nitsche, a plant in the Thymelaeaceae family, using silica gel column chromatography, macroporous resin chromatography, ODS column chromatography, and HPLC. Their inhibitory activity against HepG2 and Hep3B cells was tested. Ultimately, it was found that these compounds exert their antitumor effect by inhibiting the growth activity of tumor cells. The preparation method of this invention is simple, reproducible, and yields high-purity compounds with significant antitumor activity.

The invention discloses a method for extracting isopentenyl flavonoid compounds from black mulberries, which adopts an ultrasonic-assisted ionic liquid extraction method and comprises the following steps: crushing the black mulberries, mixing the crushed black mulberries with ionic liquid, soaking the mixed black mulberries, and carrying out ultrasonic extraction. Compared with a traditional water extraction method, the total content of the extracted isopentenyl flavonoid compounds sanggenone D and sanggenone C is increased by about 3.00 times. Meanwhile, the extraction method is green, efficient and energy-saving, and avoids environmental pollution to a greater extent.

The application relates to application of an isopentenyl transferase FnPT1 and belongs to the technical field of enzymology. The isopentenyl transferase FnPT1 screened and verified by the application is different from most reported flavonoid isopentenyl transferases, the isopentenyl transferase FnPT1 can catalyze isopentenyl modification reaction of flavonoid glycoside which is a relatively large substrate, the isopentenyl transferase FnPT1 has potential application in flavonoid glycoside synthetic biology, and has important application value.

The invention provides a method for selectively synthesizing an isopentenyl phenolic compound, relates to the technical field of a preparation method of the isopentenyl phenolic compound, and particularly relates to a novel method for highly selectively converting a phenolic compound and an allyl alcohol compound into the isopentenyl phenolic compound by taking lewis acid and hexafluorophosphate as a composite catalyst. On one hand, the hexafluorophosphate and the lewis acid cooperate to activate the allyl alcohol compound, so that the oxygen alkylation side reaction is remarkably inhibited, the carbon alkylation product is specifically generated, and the yield of the target product is high; meanwhile, the catalyst dosage is small, conditions are mild, reaction is rapid, and the principle of green chemistry is better met; and on the other hand, the preparation method disclosed by the invention is wide in applicable substrate range, and the substrate is easy to obtain.

The invention provides an isopentenyl phenol compound and a preparation method and application thereof.The structural formula of the isopentenyl phenol compound is a formula A or a formula B. The isopentenyl phenol compound is obtained through separation from shiitake mushrooms, has no non-specific toxicity to T cells, B cells and keratinocytes, can effectively inhibit proliferation activity of the T cells, the B cells and the keratinocytes, and has a good application prospect. The compound also has antioxidant activity, can be used for preparing drugs for resisting autoimmune diseases, such as psoriasis, can inhibit the development of psoriasis from multiple ways, and has a multi-target synergistic effect mechanism.

To provide a fibroblast growth factor-5 production inhibitor having excellent fibroblast growth factor-5 production inhibitory action and high safety.SOLUTION: The fibroblast growth factor-5 (FGF-5) production inhibitor includes at least one selected from the group consisting of pinobanksin, pinocembrin, quercetin, rutin, isoquercetin, genistein, 6-prenylnaringenin, isosakuranetin, and biochanin A.SELECTED DRAWING: None

The invention belongs to the technical field of genetic engineering and enzymology, and particularly relates to isopentenyl transferase and application thereof to preparation of isopentenyl isoflavone. The isopentenyl transferase FoPT2 with the amino acid sequence shown as SEQ ID NO.2 is verified for the first time to show catalytic activity on 6 isoflavone compounds (genistein, dihydrogenistein, biochanin A, calycosin, genistin and 3 ', 4', 7-trihydroxy isoflavone), 21 isopentenyl products are generated in total, the structures of 10 products are analyzed, and 3 products are synthesized for the first time. The isopentenylation modification comprises 13 kinds of mono-isopentenylation (C- / O-connection) and 8 kinds of diisopentenylation (C-O connection / C-C connection), modification sites comprise C-6, 7-O, C-8, 4 '-O and the like, and wide regioselectivity is shown. By optimizing reaction conditions, the catalytic efficiency of FoPT2 is improved, the preparation of isopentenyl isoflavone with various structures is facilitated, and a new possibility is provided for isopentenyl isoflavone products.

The invention provides a chalcone isopentenyl transferase gene GiPT16, a GiPT16 protein, an amplification primer group and application, and belongs to the technical field of biological genes. The key aromatic isopentenyl transferase GiPT16, which participates in isopentenylation modification of chalcone active ingredients, is successfully mined and functionally identified by adopting a reverse genetics strategy on the basis of whole genome sequencing data of Glycyrrhiza inflata (Glycyrrhiza inflata). The chalcone isopentenyl transferase is proved to be capable of specifically catalyzing biosynthesis of psoralen B and licochalcone C by taking DMAPP as a donor, is the first represented chalcone isopentenyl transferase in glycyrrhiza inflate, fills the blank of key enzyme research of the species in a chalcone isopentenyl metabolic pathway, and has a wide application prospect. An important basis is provided for deeply analyzing a molecular mechanism formed by the quality of the glycyrrhiza inflate medicinal material.