309 results about "Mutated protein" patented technology

The present disclosure provides compounds having activity as inhibitors of the G12C mutant KRAS protein, pharmaceutical compositions comprising the compounds, and methods of treating certain disorders, such as cancer, including but not limited to lung cancer, pancreatic cancer, colorectal cancer, and solid tumors. In particular, the disclosure provides compounds of Formula (I):, and pharmaceutically acceptable salts thereof, wherein the substituents are as described.

The present application relates to a novel tricyclic derivative compound as a KRAS mutant protein inhibitor, and use thereof. The compound according to one embodiment of the present application inhibits the activity of a KRAS mutant protein and thus can be used in the prevention or treatment of diseases induced by KRAS mutation.

This invention provides a nitrile hydrolase mutant and its application in the synthesis of p-cyanobenzoic acid. The invention provides a nitrile hydrolase mutant that enhances the catalytic activity for the synthesis of p-cyanobenzoic acid. The mutant protein is a non-natural protein, and it exhibits significantly enhanced activity in catalyzing the conversion of terephthalonitrile to p-cyanobenzoic acid. Furthermore, the mutant protein contains mutations in two or more core amino acids related to the enzyme's catalytic activity in the wild-type nitrile hydrolase. The nitrile hydrolase mutant of this invention can significantly improve the yield of the synthesized product catalyzed by the nitrile hydrolase.

The application discloses efficient expression of Aspergillus oryzae beta-galactoside enzyme mutant and application thereof in dairy products, and belongs to the technical fields of enzyme engineering and dairy product processing, and particularly relates to efficient expression of Aspergillus oryzae beta-galactoside enzyme mutant and application thereof in dairy products.The mutant protein can be as follows: A1) a protein with an amino acid sequence of SEQ ID No.2; A2) a fusion protein with the same function obtained by connecting a label to the N terminal and / or C terminal of A1).The mutant protein is subjected to high-density fermentation in a 5L fermentation tank, and the enzyme activity of the fermentation liquor can reach 4628U / mL, and the recovery rate of the mutant enzyme is increased by 1.7 times.Compared with the wild type, the optimal pH of the mutant is increased from 4.5 to 5.5, the optimal temperature is decreased from 60 DEG C to 50 DEG C, the lactose hydrolysis efficiency is increased by 11%, and the mutant is more suitable for the production process of low / zero lactose dairy products.

The invention provides an infectious bronchitis virus subunit vaccine as well as a preparation method and application thereof, and belongs to the technical field of genetic engineering vaccines. According to the chicken infectious bronchitis virus mutant protein disclosed by the invention, the amino acid sequence of the mutant protein is shown as SEQ ID NO.5. According to the avian infectious bronchitis virus subunit vaccine containing the recombinant avian infectious bronchitis virus mutant protein Kozak-IgKsp-IBV-M41-S-core-6His as an effective component, the glycosylation level of the vaccine is relatively high, the expression level is relatively stable, the virus return risk of a live vaccine does not exist, the safety is high, large-scale industrial preparation can be achieved, and the vaccine has good application prospects. The cost is low.

The present invention relates to the fields of agriculture, plant biotechnology, and molecular biology. Specifically, the present invention relates to a wheat EPSPS mutant protein and use thereof in improving the tolerance of wheat to glyphosate. The mutant protein comprises an amino acid sequence having the following mutations compared to the EPSPS amino acid sequence of any genome of wild-type wheat: in the amino acid sequence set forth in SEQ ID NO: 2, the amino acid at position 168 is mutated from threonine to isoleucine, the amino acid at position 169 is mutated from alanine to valine, and the amino acid at position 172 is mutated from proline to serine. The mutant protein enables the production of stable glyphosate-resistant wheat, showing important significance for wheat breeding.

The invention relates to a method for regulating and controlling the color of wheat grains and reducing the germination rate of the grains, a related TaMyb10 mutant protein, a gene, a gene editing vector and application of the TaMyb10 mutant protein. The invention discloses a method for regulating and controlling the color of wheat grains and reducing the germination rate of the grains. The method comprises the step of inhibiting or destroying the interaction of TaMyb10 protein and bHLH protein in wheat to obtain white-grain pre-harvest germination resistant wheat. The invention further discloses a functional segment which is combined with bHLH in the TaMyb10 protein and can influence the color and the pre-harvest germination resistance of wheat grains, application of a variant of the functional segment, TaMyb10 mutant protein containing substitution and / or deletion and / or addition of amino acid residues at one or more functional sites of the functional segment, and application of the TaMyb10 mutant protein. The interaction between the TaMyb10 and the bHLH protein is weakened or does not interact with the bHLH protein through the mutation of the amino acid at the functional site, so that the wheat shows the characteristic of white-grain pre-harvest sprouting resistance, and the cultivation of the white-grain pre-harvest sprouting resistance wheat variety is facilitated.

Disclosed are a new interleukin-2 (IL-2) mutant protein and the use thereof. Compared with wild-type IL-2, the IL-2 mutant protein has improved properties, such as an improved IL-2 receptor binding property and improved druggability. Also provided are a fusion protein, dimer and immunoconjugate comprising the IL-2 mutant protein, nucleic acids encoding the IL-2 mutant protein, the dimer and the immunoconjugate, and a vector and host cell comprising the nucleic acid. Further provided are methods for preparing the IL-2 mutant protein, the fusion protein, the dimer and the immunoconjugate, a pharmaceutical composition containing same, and the therapeutic use thereof.

The invention provides a method for improving the expression level of a meat toxin light chain. The method comprises the following steps: connecting a dissolution-promoting tag to an N end or a C end of meat toxin light chain protein to form soluble meat toxin light chain recombinant protein; the dissolution-promoting tag is a wild dissolution-promoting tag NT11 or a mutant protein mut7 of the wild dissolution-promoting tag NT11, enzyme digestion removal is not needed, the activity of a meat toxin light chain is hardly influenced and interfered, and the fusion protein can keep 93% of substrate enzyme digestion activity. The method further comprises overexpressing a molecular chaperone htpG in the genome of the host bacterium. According to the invention, a BoNT / A-LC high-efficiency expression system is constructed through multi-strategy optimization, so that the yield of BoNT / A-LC is increased by nearly 20% compared with that of wild type NT11-Lc, the yield reaches 647 mg / L through overexpression of a molecular chaperone htpG, and after combinatorial optimization, the yield is 8.5 times that of only expressed BoNT / A Lc, 1.79 times that of NT11-Lc and 1.43 times that of Mut7-Lc.

This invention discloses a method for the bioenzymatic synthesis of deoxynucleoside monophosphate. The invention provides a mutant protein of dNK, comprising mutating amino acid residues at positions 84, 88, 110, and 172 of the amino acid sequence shown in SEQ ID NO:1, while leaving other amino acid residues unchanged, to obtain a protein with deoxynucleoside kinase activity. This invention obtains a deoxynucleoside kinase mutant capable of stably and efficiently catalyzing the synthesis of 3'-O-NH2-deoxynucleoside monophosphate using 3'-O-NH2-deoxynucleoside as a substrate, providing a new approach and pathway for nucleotide production. The bioenzymatic synthesis of (deoxy)nucleoside monophosphate of this invention has advantages such as high conversion rate, mild reaction conditions, simple production process, environmental friendliness, and ease of large-scale production.

The application discloses application of SbWOX gene and SbBBM gene in corn breeding and a corn genetic transformation method, and relates to a bioengineering technology.The application provides a nucleic acid molecule with co-expression of SbWOX protein gene and SbBBM protein gene, and corresponding gene co-expression vectors and microbial transformants.The application also provides application of the co-expression of the SbWOX gene and the SbBBM gene in the corn genetic transformation method.The application obtains corresponding genes and mutant proteins based on the SbWOX gene and the SbBBM gene of sorghum, the two genes are co-expressed in the corn genetic transformation process, even without adding plant growth hormones in the antibiotic screening medium in the tissue culture process, the plant genetic transformation process can be normally completed, and the transformation efficiency and the regeneration efficiency of the corn can be remarkably improved, the transformation rate reaches 10.42%, and the differentiation rate reaches 32.89%.

The application discloses a LCC with enhanced hydrophobicity ICCG The application discloses a mutant protein and application thereof ICCG The mutant protein is obtained by mutating an amino acid residue at the 266th amino acid residue in a protein amino acid sequence into phenylalanine, and is a mutant N266F. Compared with a wild-type protein, the mutant protein has significantly enhanced hydrophobicity, and is verified by a PET depolymerization experiment. The mutant protein has significantly improved PET depolymerization efficiency compared with the wild-type protein under the condition of low enzyme load, is economically feasible, and has product selectivity.

The application discloses a five-heterocycle compound, a preparation method and application thereof. Specifically disclosed are a compound as shown in formula I, a pharmaceutically acceptable salt or solvate thereof, a composition containing the compound, and a pharmaceutical use of the compound for preparing a drug for treating a disease or disorder related to the mechanism of action of KRAS G12C mutant protein. The five-heterocycle compound in the application has the activity of inhibiting the proliferation of Ba / F3 KRAS-G12C cells, NCI-H358 cells and MIA PaCa-2 cells expressing KRAS G12C mutant protein, and has a good inhibitory effect on the growth of a subcutaneous transplanted tumor of a NCI-H358 nude mouse.

The invention discloses a lactic dehydrogenase LdLDH mutant and application thereof, a wild type LdLDH enzyme derived from Lactobacillus delbrueckii subsp. Bulgaricus is taken as a research object, the amino acid sequence of the wild type LdLDH enzyme is designed and modified to obtain a mutant protein, the mutant protein is named as LdLDH-M, the amino acid sequence of the mutant protein is shown as SEQ ID NO.2, the Tm value of the LdLDH-M is 77.1 DEG C, the Tm value of the LdLDH-M is 77.1 DEG C, and the Tm value of the LdLDH-M is 77.1 DEG C; compared with the wild type LdLDH enzyme, the Tm value of the LdLDH enzyme is increased by 27.4 DEG C, and the enzyme activity of the LdLDH enzyme is increased by 1.4 times. Therefore, compared with the wild type LdLDH enzyme, the LdLDH-M has remarkably improved thermal stability and enzymatic activity, and is more beneficial to widening the application range of the LdLDH-M in the fields of high-temperature biological research, industrial biological catalysis and the like.

The invention discloses a glycolaldehyde synthetase mutant and application of the glycolaldehyde synthetase mutant in improving the thermal stability of glycolaldehyde synthetase, and belongs to the technical field of biological catalysis application. According to the glycolaldehyde synthetase mutant disclosed by the invention, on the basis of an amino acid sequence as shown in SEQ ID NO.1, the glycolaldehyde synthetase mutant has the following mutations: A381P / E509F, A381P / K290P, A381P, S61A, A381P / K290P / E509F, A381P / C49A, A381P / T100V, A381P / S61A or A381P / K290P / S61A. The mutant protein can catalyze formaldehyde to prepare hydroxyacetaldehyde (glycolaldehyde). In addition, the mutant protein can also improve the catalytic efficiency from formaldehyde to glycolaldehyde, and due to the improvement of the thermal stability, continuous catalysis of industrial enzyme in actual reaction is facilitated, so that the mutant has a good industrial application prospect.

A long-acting FGF21 derivative, specifically relating to an FGF21 derivative comprising an FGF21 mutant protein and a fatty acid chain. The FGF21 derivative, which is obtained by coupling the fatty acid chain to a cysteine residue at position 172 of an FGF21 protein by means of a linker, has relatively high FGF21 activity, and has a better weight loss effect in model mice. The FGF21 mutant protein not only retains the activity of mature FGF21, but also has significantly improved stability in serum.

The present application relates to the application of Klenow mutant fragments in the synthesis of nucleic acids, and belongs to the technical field of biological modification and synthesis.The present application provides the application of Klenow mutant fragments with an amino acid sequence as shown in SEQ ID NO.8 or SEQ ID NO.14 in the synthesis of nucleic acids.The mutant protein F762A expressed by the Klenow mutant fragments of the present application can efficiently synthesize deoxyribonucleic acid, ribonucleic acid, deoxyribonucleic acid analogs and ribonucleic acid analogs with different lengths of DNA templates and DNA / RNA primers at 37 DEG C, and has a wide synthesis range and universality.

This invention pertains to fusion protein mutants comprising a Prime Editing enzyme having a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence comprises a SpCas9 H840A nickase mutant protein of SEQ ID NO:152 and the second amino acid sequence comprises a Moloney Murine Leukemia Virus reverse transcriptase protein mutant (MMLV RTase mutant), wherein the fusion protein mutant displays at least the equivalent or greater activity of a reference Prime Editing enzyme in genome editing.

The application discloses a novel trimeric recombinant protein vaccine. Specifically disclosed are a mutant protein RBD8M with an amino acid sequence of SEQ ID No. 1 and a fusion protein of positions 26-277, positions 1-277 and SEQ ID No. 4. The application also discloses a vaccine containing the fusion protein, and further develops a trimeric recombinant protein vaccine containing the fusion protein and a double adjuvant. Experiments show that the vaccine prepared in the application can effectively induce cellular immunity and humoral immunity of the body in animals, a trace amount of the protein can stimulate a very high immune response of mice, has a good protection effect, can simultaneously produce high-titer neutralizing antibodies against various epidemic strains of the novel coronavirus, is a broad-spectrum effective new coronavirus vaccine, and has important significance for preventing novel coronavirus infection and a wide clinical application prospect.

The present invention relates to a novel interleukin-2 (IL-2) mutant protein. The present invention further provides a fusion protein and an immunoconjugate comprising the IL-2 mutant protein, a nucleic acid encoding the IL-2 mutant protein, and a vector and a host cell comprising the nucleic acid. The present invention further provides a method for preparing the IL-2 mutant protein, a pharmaceutical composition comprising the IL-2 mutant protein, and therapeutic use of the mutant protein.

The present application relates to a herbicide-resistant HPPD mutant protein. At least three excellent mutants are obtained by gene editing technology, which express different HPPD mutant proteins and can confer herbicide resistance or tolerance to plants.

This invention discloses a mutant of glycolaldehyde synthase and its application in improving the thermostability of glycolaldehyde synthase, belonging to the field of biocatalysis application technology. The glycolaldehyde synthase mutant disclosed in this invention, based on the amino acid sequence shown in SEQ ID NO.1, contains the following mutations: A381P / E509F, A381P / K290P, A381P, S61A, A381P / K290P / E509F, A381P / C49A, A381P / T100V, A381P / S61A, or A381P / K290P / S61A. This mutant protein can catalyze the preparation of hydroxyacetaldehyde (glycoaldehyde) from formaldehyde. The mutant protein of this invention also improves the catalytic efficiency of the formaldehyde-to-glycoaldehyde conversion. Due to the improved thermostability, it is beneficial for continuous catalysis in actual industrial reactions, thus the mutant shows good prospects for industrial applications.

Mutant Cas9 proteins are described that have one or more mutations in a Keap1 degron sequence of the Cas9 protein. The one or more mutations can increase the half-life of the mutant proteins. Nucleic acid sequences and constructs comprising a sequence that encode a mutant Cas9 protein, as well as methods of enhancing CRISPR efficiency by administering one or more guide RNAs (gRNAs) to a cell comprising the mutant Cas9 proteins are also disclosed herein.

The invention discloses a method, device and equipment for predicting the property of a mutant protein, and the method comprises the steps: carrying out the fusion processing of the embedding characteristics and physicochemical characteristics of an original protein, the embedding characteristics and physicochemical characteristics of the mutant protein generated by the mutation of the original protein, and the interaction characteristics of residues of the mutant protein, obtaining initial node characteristics of the mutant protein; the interaction characteristic represents the interaction between every two residues in the mutant protein; the embedded feature represents an amino acid sequence of the protein, the physicochemical feature represents physicochemical properties of residues forming the protein, and a prediction model is used for processing initial node features and structural features of the original protein so as to predict multiple properties of the mutant protein; and predicting model loss of the model, wherein the model loss is determined according to a sample property predicted value representing multiple properties and a plurality of sample property measured values of the sample, wherein the sample property predicted value and the sample property measured values are obtained by the prediction model.

The invention discloses a carbohydrate molecule sequencing method based on glycosidase and nanopores and a system and application thereof. The invention also discloses a nanopore mutant protein and application thereof. The invention also discloses a glycosequencer containing the nanopore protein, a sequencing method, a system and application thereof. The invention also discloses a data processing method and a processing system for glycosidase hydrolysis assisted nanopore sugar sequencing, a computer related product and the like. According to the method, the detection limit can be remarkably reduced, the sensitivity can be improved, the accuracy of sugar sequencing can be improved, the analysis accuracy exceeds 98%, the sensitivity is improved by more than 50 times, the time is saved by more than 5 times, the analysis period is short, the sequencing process is simplified, and the cost is reduced. And a new technical approach is provided for rapid analysis of complex sugar sequence information.

The invention discloses a preparation method and application of natural nucleotide. The mutant protein of the MrPPK2 is prepared by the following steps: A1) mutating amino acid residues at sites 93 and 127 on an amino acid sequence as shown in SEQ ID NO: 1 to obtain a protein with polyphosphate kinase activity; a2) a protein with the same function, wherein the identity of other amino acid residues in the protein shown in A1) except the mutated amino acid residues is more than 80%; according to the present invention, sodium hexametaphosphate is adopted as a main phosphate group donor, the MrPPK2 mutant improves the generation rate of dGTP and dATP, and under the combination of the SMC mutant and dTMP-K or dCMP-K, sodium hexametaphosphate is adopted as the main phosphate group donor, dTTP / dCTP is adopted as a secondary donor, and the generation rate of dTTP and dCTP is improved.

An NCg12747 gene mutant and the use thereof in the preparation of L-lysine are provided. The NCg12747 gene mutant is a DNA molecule shown in SEQ ID NO: 3, which encodes the NCg12747 mutant protein shown in SEQ ID NO: 4. Mutating the NCg12747 gene into the NCg12747 gene mutant shown in SEQ ID NO: 3 or overexpressing NCg12747 gene mutant contributes to increase in the yield and the growth rate of L-lysine. However, when the gene is weakened or knocked out, accumulation of the L-lysine is not facilitated, and the growth rate of a strain can be reduced. The NCg12747 gene mutant and the NCg12747 mutant protein encoded thereby can be used for preparing L-lysine.

The application discloses a mutant Cas12i nuclease and application thereof, and belongs to the technical field of gene editing. The Cas mutant protein provided by the application is a mutant protein in which the 7th, 168th, 273rd, 332nd, 478th, 505th and 551st amino acids of SEQ ID NO:1 are all mutated into arginine, and other amino acid sequences remain unchanged. The application improves the editing efficiency by mutating multiple amino acids of the wild-type Cas12i protein, and can be used for multi-gene editing.

The invention belongs to the technical field of directed evolution modification and biological catalysis application of enzymes, and relates to a Candida antarctica lipase B mutant protein and application thereof, the sequence of the mutant protein comprises one or more of the mutation of the 195 S and F, the mutation of the 195 S and Y and the mutation of the 283 A and Y from the N terminal to the C terminal of the amino acid sequence shown in SEQ ID NO.1 of the original CALB; on the basis of a wild type lipase gene sequence, through rational design and site-specific mutagenesis, mutants S195F, S195Y, A283Y, S195F-A283Y and S195Y-A283Y, of which the Tm value and the optimal reaction temperature are obviously improved and the catalytic activity is improved by 1-2 times, are finally obtained; when the mutant is used for catalyzing synthesis of docosahexaenoic acid (DHA) glyceride, higher catalytic efficiency is shown, and the yield of the DHA glyceride is effectively improved.

The present disclosure pertains to the field of genetic engineering of plants. Specifically, the present disclosure relates to use of a mutant GmLn protein and a gene encoding same in the regulation of soybean yield, particularly to, but not limited to, a method for obtaining a soybean tolerant of dense planting, a method for detecting a soybean tolerant of dense planting, and a related primer and kit, and further to a soybean plant tolerant of dense planting and a method for improving soybean planting density. The methods provided by the present disclosure involve expressing a gene editing tool in a soybean to genetically edit a target sequence in the soybean, resulting in a soybean tolerant of dense planting with increased yield.