17 results about "Acyltransferase" patented technology

Disclosed are compounds of Formula I as well as pharmaceutically acceptable salts, esters, and prodrugs thereof, which are DGAT2 inhibitors. Also provided are methods of making compounds of Formula I, pharmaceutical compositions comprising compounds of Formula I, and methods of using these compounds to treat hepatic steatosis, nonalcoholic steatohepatitis (NASH), fibrosis, type-2 diabetes mellitus, obesity, hyperlipidemia, hypercholesterolemia, atherosclerosis, cognitive decline, dementia, cardiorenal diseases such as chronic kidney diseases and heart failure and related diseases and conditions, comprising administering a compound of Formula I to a patient in need thereof.

The present application relates to the technical field of genetic engineering, and discloses a recombinant Escherichia coli for high-yield O-acetyl-L-homoserine and application thereof. The recombinant Escherichia coli for high-yield O-acetyl-L-homoserine is obtained by the following combination of modification strategies: in Escherichia coli W3110, a gene encoding homoserine O-acetyltransferase is integrated into a gene site encoding L-arginine ABC transporter ATP binding subunit, then a gene encoding phosphoacetyltransferase is knocked out, then a gene encoding transcriptional anti-terminator and mRNA stability regulator is knocked out, then a gene encoding ATP-NAD kinase is integrated into a gene site encoding NADPH-dependent aldehyde reductase, and finally a gene promoter of acetyl-CoA synthetase is replaced by a Ptrc promoter to obtain the recombinant Escherichia coli. The recombinant Escherichia coli is used for fermentation to produce O-acetyl-L-homoserine, and has the advantage of high yield. metx artp patz cspc ppnk yahk acs ​​​​​​​

This invention relates to the construction and staining application of recombinant Escherichia coli for synthesizing indoleacetic acid ester. The recombinant Escherichia coli for synthesizing indoleacetic acid ester is obtained by using recombinant Escherichia coli MG1655ΔpheAΔtrpRΔtyrAΔyddGΔarsB::tac70-MaFMOΔldhA::tac70-MaFMOΔyghWX::tac70-tnaAΔpoxB::tac70-cav1 as the initial strain. Then, the endogenous acetylesterase is knocked out, and the endogenous tryptophan hydrolase gene tnaA and the flavin monooxygenase gene maFMO are overexpressed, while simultaneously overexpressing the acetyltransferase gene. The indoleacetic acid ester yield of this invention is as high as 195.3 mg / L. Using indoleacetic acid ester for staining eliminates the need for reducing agents and enzyme solutions, significantly reducing staining costs.

Provided is an RNAi agent for inhibiting DGAT2 gene expression in cells, and a pharmaceutical composition thereof. Also provided is a therapeutic use of the RNAi agent.

This invention relates to a recombinant bacterial cell for de novo synthesis of xanthocyanin WGX-50 using glucose as a carbon source, its construction method, and its applications. The recombinant bacterial cell uses *Escherichia coli* as the host strain and integrates the following three heterologous biosynthetic modules: a 3,4-dimethoxyphenylethylamine de novo synthesis module, which contains an enzyme system catalyzing the generation of dopamine from L-tyrosine and further stepwise methylation of dopamine to 3,4-dimethoxyphenylethylamine; a cinnamoyl-CoA synthesis module, which contains an enzyme system catalyzing the generation of cinnamoyl-CoA from phenylalanine or glucose metabolic intermediates; and an amidation module, which contains an acyltransferase capable of catalyzing the condensation of 3,4-dimethoxyphenylethylamine and cinnamoyl-CoA to generate xanthocyanin WGX-50. This invention achieves, for the first time, the de novo biosynthesis of xanthocyanin in microorganisms, completely eliminating dependence on the expensive exogenous precursor 3,4-dimethoxyphenylethylamine and significantly reducing raw material costs.

The present application relates to a kind of synthetic polyunsaturated fatty acid binding phospholipid yeast engineering bacteria and construction method and application, belong to microbial engineering technical field, the engineering bacteria is with Yarrowia lipolytica as bottom cell, knock out the Mhy1, Iro1, IDH1, CEX1 gene in its genome for generating mycelium, synthesis of triglyceride, citric acid metabolism, citric acid efflux;Phospholipid synthesis, pyruvate synthesis, polyunsaturated fatty acid synthesis and acyltransferase CDS1, OPI3, Mce2, LplA, △9Elo, △8Des, △5Des, △17Des, △5Elo, △15Des, LPCAT3 gene are sequentially connected together, as an expression module is integrated in the URA site of genome.The yeast engineering bacteria of the present application obtains polyunsaturated fatty acid binding phospholipid in one step efficiently, and phospholipid yield is 151.19 mg / g, and in binding fatty acid, EPA content is 13.2%.

The application discloses a genetically engineered bacterium for improving the yield of mevalonic acid as well as a construction method and application thereof, and belongs to the technical field of genetic engineering. In order to solve the technical problems of low carbon atom economy and limited theoretical yield of MVA biosynthesis technology, the application takes Escherichia coli as a starting strain, overexpresses a bifunctional acetaldehyde-ethanol dehydrogenase mutant AdhE A267T / E568K gene adhE mut , an acetyl-CoA acyltransferase / HMG-CoA reductase gene mvaE , an HMG-CoA synthetase gene mvaS , and introduces a tetracycline-induced CRISPRi system to inhibit the expression of an orotate-5'-phosphate decarboxylase gene pyrF , so that the carbon flux is led from the growth of the strain to the synthesis of mevalonic acid. The genetically engineered bacterium provided by the application can produce mevalonic acid by fermentation with ethanol as a carbon source, and the yield reaches 0.89 g / g. The application provides a new idea for improving the carbon atom economy of mevalonic acid biological manufacturing.

This invention discloses a BAHD acyltransferase from Camellia oleifera and its applications. It relates to the field of enzyme engineering technology. The amino acid and nucleotide sequences of the BAHD acyltransferase are provided, along with related applications. This invention provides an enzyme with acyl transfer function from Camellia oleifera, which can be directly used as a catalyst for the acylation reaction of C-22 saponins in Camellia oleifera. Furthermore, this enzyme exhibits strong stability and activity, and its preparation method is simple and efficient, making it suitable for use in the biosynthesis of secondary metabolites.

The present application relates to a kind of acyltransferase and its application in the preparation of phenylpropionyl fatty amine compound, the acyltransferase is selected from LbSCT1 And / or LbSCT2, the amino acid sequence of the LbSCT1 As shown in SEQ ID NO:1, the amino acid sequence of the LbSCT2 As shown in SEQ ID NO:2.The present application is screened by acyltransferase in wolfberry, two acyltransferases are successfully identified, both can catalyze coffee acyl-coenzyme A, dihydrocaffeoyl-coenzyme A, p-coumaroyl-coenzyme A, feruloyl-coenzyme A and other phenylpropionyl group and adipylamine, spermine etc.Fatty amine connection, thus establish a kind of efficient with wolfberry spermidine methyl, ethyl, propyl, butyl (Lycibarbarspermidine I-IV) And Kukoamine B as representative phenylpropionyl fatty amine synthesis method, effectively solve the current dihydrocaffeoyl group containing phenylpropionyl fatty amine biosynthesis limited technical bottleneck.

Provided are compounds of Formula (I) and the pharmaceutically acceptable salts, esters, and prodrugs thereof, which are DGAT2 inhibitors. Also provided are methods of making compounds of Formula I, pharmaceutical compositions comprising compounds of Formula I, and methods of using these compounds to treat hepatic steatosis, nonalcoholic steatohepatitis (NASH), metabolic dysfunction-associated steatohepatitis (MASH), hepatic fibrosis, type-2 diabetes mellitus, obesity, hyperlipidemia, hypercholesterolemia, atherosclerosis, cognitive decline, dementia, cardiorenal diseases such as chronic kidney diseases and heart failure and related diseases and conditions, comprising administering a compound of Formula I and the pharmaceutically acceptable salts, esters, and prodrugs thereof, to a patient in need thereof.

This invention discloses a method for enriching protein palmitoyltransferase substrates, belonging to the field of biochemical analysis technology. This invention utilizes a tandem enrichment method integrating APEX2-based proximity labeling technology and Acyl-RAC-based palmitate-assisted capture technology to enrich specific protein palmitoyltransferase substrates. These substrates are then identified using proteomics techniques. This invention improves the specificity of large-scale identification of protein palmitoyltransferase substrates at the cellular level, accelerates the construction of palmitoyltransferase-substrate interaction networks, and advances research progress in palmitoyltransferase modification.

A strain of *Lactiplantibacillus plantarum*, FBEL010, was deposited at the China General Microbiological Culture Collection Center (CGMCC) on November 25, 2025, with accession number CGMCC No. 36687. Its 16S rDNA nucleotide sequence is shown in SEQ ID NO. 1. The genome of strain FBEL010 contains a gene encoding the alcohol-acyltransferase AAT, the nucleotide sequence of which is shown in SEQ ID NO. 2. This strain is used in the preparation of fermented fruit and vegetable juices. The prepared fermented fruit and vegetable juices have a total ester content ≥150 μg / L, and significantly increased levels of hexyl acetate and ethyl butyrate fruit aroma components. Testing according to national standards showed no pathogenic bacteria, and the content of contaminating bacteria was within acceptable limits. The content of heavy metals (lead, arsenic, mercury) and additives meets national standards, making it suitable for use as a beverage. This strain can also be used to prepare fermented fruit and vegetable juices such as strawberry, lychee, pineapple, and cucumber.

This invention belongs to the field of genetic engineering and bioengineering technology, and discloses a recombinant *E. coli* strain capable of de novo synthesis of piperine, its construction method, and its applications. Using *E. coli* MG1655 as the starting strain, this invention constructs a piperine biosynthetic pathway by overexpressing tyrosine ammonia-lyase, carboxylic acid reductase, 4′-phosphopanylthioethylamine transferase, shinol acyltransferase, and eugenol synthase. Further overexpression of DAHP synthase feedback inhibition mutants and prephenylate dehydrogenase can be used to knock out tyrosine metabolism repression genes. tyrR To enhance precursor supply, each heterologous gene was codon-optimized and expressed in modules using different plasmids. This recombinant strain produced piperine by fermentation using glucose as a substrate, achieving a maximum yield of 47.9 mg / L in shake flasks, and can be applied to the microbial fermentation preparation of piperine.

This invention relates to an amino acid ester acyltransferase mutant, its encoding gene, and its application in the synthesis of glutamic-alanine dipeptide. Compared with existing technologies, the amino acid ester acyltransferase mutant disclosed in this invention exhibits high activity, high substrate concentration tolerance, and high selectivity for glutamic-alanine dipeptide synthesis / hydrolysis. In the application of catalyzing the condensation of L-alanine methyl ester and L-glutamine to prepare glutamic-alanine dipeptide, it demonstrates significant advantages in terms of high yield and high space-time yield. Compared with chemical synthesis methods, the synthesis of glutamic-alanine dipeptide using this enzyme does not require group protection and deprotection, the process is simple, the reaction conditions are mild, and the process is environmentally friendly, showing promising application prospects in the industrial production of glutamic-alanine dipeptide.

Provided are compounds of Formula I, Formula Ib or Formula Ic and the pharmaceutically acceptable salts, esters, and prodrugs thereof, which are DGAT2 inhibitors. Also provided are methods of making compounds of Formula I, Formula Ib or Formula Ic, pharmaceutical compositions comprising compounds of Formula I, Formula Ib or Formula Ic, and methods of using these compounds to treat hepatic steatosis, non-alcoholic steatohepatitis (NASH), fibrosis, type-2 diabetes mellitus, obesity, hyperlipidemia, hypercholesterolemia, atherosclerosis, cognitive decline, dementia, cardiorenal diseases such as chronic kidney diseases and heart failure and related diseases and conditions, comprising administering a compound of Formula I to a patient in need thereof.

The application relates to a mutant enzyme of 3-phosphoglyceroyltransferase, a coding gene and application thereof, and belongs to the fields of biochemistry, molecular biology and metabolism. 58 GPAT9 mutant genes are constructed by using a site-directed mutagenesis technique, and the influence of single and multiple amino acid site changes on GPAT9 enzyme activity is analyzed by combining a GPAT-specific yeast genetic complementation method. It is found that the changes of six amino acid residues (85, 114, 119, 230, 237 and 322) located outside the acyltransferase conserved domain in AtGPAT9 can significantly affect the enzyme activity. There is interaction among the amino acids, for example, the simultaneous mutation of Y85W / N119H / S237N of the three sites can greatly increase the activity of AtGPAT9, accelerate the growth of yeast and promote the synthesis of triacylglycerol, and the triacylglycerol content in the yeast cells expressing the mutant enzyme is increased by 45.7% compared with that of the yeast cells expressing the wild type BnGPAT9.

The application discloses a SCPL family acyltransferase EpCYS gene of purple Echinacea purpurea, an amino acid sequence encoded by the EpCYS gene is shown as SEQ ID NO. 2, the gene is heterologously expressed in yeast or Nicotiana benthamiana, and after the expressed protein is used to catalyze a substrate in vitro, the catalyzed product is identified; it is shown that the EpCYS protease can catalyze the generation of Cynarine; more resources are provided for the application of plant acyltransferase in synthetic biology, the biosynthesis production of Cynarine as a medicinal ingredient is promoted, and a new contribution will be made for human health.