13 results about "Methyltransferase Gene" patented technology

The invention belongs to the technical field of environmental biology, and particularly relates to a prothioconazole methyltransferase gene proS38 and application thereof. The prothioconazole methyltransferase proS38 gene in the Sphingomonas sp.AJ-1 strain and the prothioconazole methyltransferase which is a protein expression substance thereof are found through analysis, screening, identification and verification, the prothioconazole methyltransferase proS38 gene and the prothioconazole methyltransferase which is a protein expression substance thereof are proved to have efficient and specific degradation catalysis capability on the existing pesticide prothioconazole which is used in a large amount, and a foundation is laid for biodegradation of prothioconazole.

The present application belongs to the technical field of genetic engineering, and particularly relates to a methyltransferase gene CmCMT2 and CmDRM2 application in regulating chrysanthemum flowering. The present application constructs an RNAi silencing expression vector by isolating CmCMT2 and CmDRM2 genes in a chrysanthemum variety "Jinma", and obtains CmCMT2 -RNAi and CmDRM2 -RNAi transgenic "Jinma" plants by using a genetic transformation method, then performs phenotype observation and statistics on the transgenic plants, and explores CmCMT2 and CmDRM2 the mechanism of the genes affecting early flowering of chrysanthemum by using an RNA-seq method. The CmCMT2 and CmDRM2 genes are cloned from the chrysanthemum variety "Jinma", and spatiotemporal expression analysis shows that CmCMT2 and CmDRM2 the genes are highly expressed during the process of "Jinma" from bud development to color change; and CmCMT2 and CmDRM2 the expression level in leaves gradually decreases during the growth and development of "Jinma". The research results show that CmCMT2 and CmDRM2 the content of GA1 is changed by negatively regulating the expression of CmG20ox2a and CmG20ox2b , so that the flowering period of chrysanthemum is advanced by 15 and 8 days, respectively.

The present application belongs to the field of environmental biotechnology, and particularly relates to prothioconazole methyltransferase gene pmt80 from mycobacterium and application thereof. The present application finds a methyltransferase gene pmt80 for effective degradation of prothioconazole and a corresponding enzyme pmt80 expressed by recombination of the methyltransferase gene pmt80, and the catalytic efficiency of the enzyme for (R)-PTC reaches 3.4 x 10 ‑3 min ‑1 μM ‑1 The optimal temperature of the enzyme for catalyzing (R)-PTC is 37 DEG C, and the reaction condition is mild; meanwhile, the pmt80 of the present application can catalyze degradation of PTC and 4-ethyl-5-phenyl-4H-[1,2,4]triazole-3-thiol which is an analog of PTC. In summary, the prothioconazole methyltransferase found by the present application has good industrial application potential in environmental pollution control.

The application belongs to the technical field of genetic engineering and enzyme engineering, and discloses a dragon blood tree flavone compound O-methyltransferase gene and application thereof. Three functionally differentiated O-methyltransferase genes DcOMT1, DcOMT2 and DcOMT3 are cloned from dragon blood tree, and the coded proteins can catalyze O-methylation reaction of flavonoids. The three enzymes show different catalytic modes for dracorhodin D: DcOMT1 preferentially catalyzes 4,4'-dihydroxy-2,6-dimethoxydihydrochalcone to generate dracorhodin B and further catalyzes dracorhodin B; DcOMT2 catalyzes dracorhodin B; and DcOMT3 catalyzes 4,4'-dihydroxy-2,6-dimethoxydihydrochalcone. The functions of the three enzymes are complementary, and can be used alone or in combination to realize precise synthesis of multiple different methylated flavones from a single substrate.

This invention belongs to the field of environmental biotechnology, specifically, it relates to a prothioconazole methyltransferase gene. proS38 And its applications. This invention, through analysis, screening, identification, and verification, discovered... Sphingomonas Prothiozoxystrobin methyltransferase in sp. AJ-1 strain proS38 The gene and its protein expression product, prothioconazole methyltransferase, have been shown to have a highly efficient and specific degradation catalytic ability for the widely used pesticide prothioconazole, laying the foundation for the biodegradation of prothioconazole.

The invention relates to a dactylicapnos root O-methyltransferase DsOMT018 gene and application thereof, and belongs to the technical field of biology. The nucleotide sequence of the DsOMT018 gene is shown as SEQ ID NO.1, the amino acid sequence of the encoded protein of the DsOMT018 gene is shown as SEQ ID NO.2, and the DsOMT018 gene can be used for preparing isocorydine and corydine. The separation and identification of the DsOMT018 not only breaks through the technical bottleneck of non-model plant gene mining, but also provides a new normal form for sustainable manufacturing of high-added-value alkaloids through full-chain innovation of'precise catalysis-metabolic network-green production '. The advantages of the isocorydine and corydine in synthesis of isocorydine and corydine can promote the leap-wise development of the fields of natural medicine development and synthetic biology.

The invention belongs to the technical field of environmental biology, and particularly relates to a prothioconazole methyltransferase gene proS32 and application thereof. According to the invention, a key enzyme prothioconazole methyltransferase proS32 gene of the strain Sphingomonas sp. AJ-1 for degrading prothioconazole is found through biological information analysis and gene cloning, the prothioconazole methyltransferase ProS32 is obtained through expression of an expression vector, and the prothioconazole methyltransferase ProS32 is proved to have efficient and specific degradation catalysis capability on prothioconazole by utilizing HPLC (High Performance Liquid Chromatography) and enzymatic detection; and a foundation is laid for developing a corresponding biodegradation reagent or developing efficient degradation bacteria.

The invention relates to a dactylicapnos root O-methyltransferase DsOMT014 gene and application thereof, and belongs to the technical field of biology. The nucleotide sequence of the dactylicapnos root O-methyltransferase DsOMT014 gene is shown as SEQ ID NO.1, the amino acid sequence of the encoded protein of the dactylicapnos root O-methyltransferase DsOMT014 gene is shown as SEQ ID NO.2, and the dactylicapnos root O-methyltransferase DsOMT014 gene can be The method is a key step for synthesizing the isoquinoline alkaloid in the dactylicapnos scandens and is a key node for regulating and controlling a metabolic pathway, and functional analysis of the DsOMT014 provides a key clue for understanding biosynthesis logic of the dactylicapnos scandens alkaloid.

The invention discloses O-methyltransferase, a gene, a mutant, a fusion enzyme and application of the O-methyltransferase, and belongs to the technical field of bioengineering. The O-methyltransferase SmOMT has substrate mixing property and regioselectivity, and the amino acid sequence of the O-methyltransferase SmOMT is as shown in SEQ ID NO. 1. The mutant SmOMTM2 is obtained by carrying out double mutation of E152A and I306A on the basis of SmOMT, so that the mutant SmOMTM2 has higher catalytic activity. Meanwhile, the invention constructs an SAM independent methylation system, and the system comprises a fusion enzyme AtHMTV140T-L95-SmOMTM2 which is formed by the mutant SmOMTM2 and a mutant halide methyltransferase AtHMTV140T, and the fusion enzyme AtHMTV140T-L95-SmOMTM2 can be used for preparing the SAM. The fusion enzyme can realize methylation of various substrates without exogenous SAM, has higher catalytic efficiency than a free enzyme cascade system, and can be used for synthesizing methylated compounds with enhanced anti-inflammatory activity.

The invention belongs to the technical field of environmental biology, and particularly relates to a prothioconazole methyltransferase gene proS18 and application thereof. According to the invention, a key enzyme prothioconazole methyltransferase proS18 gene of the strain Sphingomonas sp. AJ-1 for degrading prothioconazole is found through biological information analysis and gene cloning, the prothioconazole methyltransferase ProS18 is obtained through expression of an expression vector, and the prothioconazole methyltransferase ProS18 is proved to have efficient and specific degradation catalysis capability on prothioconazole by utilizing HPLC (High Performance Liquid Chromatography) and enzymatic detection; and a foundation is laid for developing a corresponding biodegradation reagent or developing efficient degradation bacteria.

This invention belongs to the field of environmental biotechnology, and in particular, it relates to the prothioconazole methyltransferase gene. proS18 Its applications. This invention discovered strains through bioinformatics analysis and gene cloning. Sphingomonas The key enzyme in sp. AJ-1 that degrades prothioconazole is prothioconazole methyltransferase. proS18 The gene was obtained and prothioconazole methyltransferase ProS18 was expressed through an expression vector. HPLC and enzymatic detection confirmed its efficient and specific degradation catalytic ability for prothioconazole, laying the foundation for the development of corresponding biodegradation reagents or efficient degrading bacteria.

This invention belongs to the field of environmental biotechnology, and in particular, it relates to the prothioconazole methyltransferase gene. proS32 Its applications. This invention discovered strains through bioinformatics analysis and gene cloning. Sphingomonas The key enzyme in sp. AJ-1 that degrades prothioconazole is prothioconazole methyltransferase. proS32 The gene was obtained and prothioconazole methyltransferase ProS32 was expressed through an expression vector. HPLC and enzymatic detection confirmed its efficient and specific degradation catalytic ability for prothioconazole, laying the foundation for the development of corresponding biodegradation reagents or efficient degrading bacteria.

This invention provides an application of the camptothecin oxygen methyltransferase CaOMT3 in catalyzing the oxygen methylation modification of hydroxycamptothecin and quercetin. Through transcriptomic and genomic analysis, four oxygen methyltransferases (CaOMT3) were identified. BECAUSE OF Genes were found to be clustered together; further analysis of metabolite and transcriptome co-expression revealed a gene significantly positively correlated with rhamnine accumulation. BECAUSE OF Genes, that is CaOMT3 Biochemical functional verification showed that CaOMT1, CaOMT2, and CaOMT3 can all catalyze the reaction of 9- and 10-hydroxycamptothecin. O Methylation yields the corresponding methoxycamptothecin. When quercetin is used as a substrate, CaOMT1 and CaOMT3 exhibit bifunctional catalytic activity, capable of simultaneously catalyzing the methylation of the 4'- and 7'-hydroxyl sites. O α-methylation yields rhamnosin, tamarindin, and phytoflavin; while CaOMT2 only catalyzes the 4'-hydroxyl site. Enzymatic kinetic analysis showed that CaOMT3's catalytic efficiency for quercetin ( k cat / K (m) is the highest. This invention provides a new enzyme tool and technological foundation for the synthetic biology research and industrial fermentation production of rhamnine and methoxycamptothecin.