51 results about "Asparagine" patented technology

The application provides an arginine mutant and application thereof in 1,4-butanediamine biosynthesis, and belongs to the field of bioengineering. Escherichia coli The mutant is obtained by site-directed mutagenesis of key site amino acid residues based on wild-type EcAdiA from strain The application improves the enzyme activity stability of arginine decarboxylase in neutral environment, improves the conversion rate and conversion speed of 1,4-butanediamine in neutral environment, and lays a foundation for high-efficiency biosynthesis of 1,4-butanediamine.

This application relates to the field of tumor treatment technology, specifically to a drug combination and evaluation method for improving the sensitivity of MSS CRC to anti-PD-1 / PD-L1 therapy. The drug combination comprises vancomycin and an immune checkpoint inhibitor. Vancomycin is used to remodel the gut microbiota and reduce L-asparagine levels; the immune checkpoint inhibitor is used to activate CD8. + T-cell anti-tumor response. By combining vancomycin with immune checkpoint inhibitors, the antigen-presenting capacity of dendritic cells is enhanced, thereby increasing the sensitivity of MSS CRC to anti-PD-1 or anti-PD-L1 immunotherapy. This application focuses on the upstream initiation link of gut microbiota-metabolites-dendritic cells-immune activation, relieving the inhibition of dendritic cell antigen presentation by L-asparagine and enhancing CD8+. + T cell activation and tumor immune response enhance the sensitivity of MSS-type colorectal cancer to anti-PD-1 / PD-L1 therapy.

The application belongs to the technical field of molecular biology, and particularly relates to metabolic markers for evaluating the prognosis of patients with hypertrophic cardiomyopathy and application thereof. The application determines that one or more of 3-hydroxyrilotene, asparagine-lysine, cyclohexylamine, arachidonic acid, aconitic acid, propionyl carnitine, ceramide, tryptophan, 3-hydroxysebacic acid, traumatic acid, phosphatidylcholine, alanine-proline, lysophosphatidylcholine, taurine and S-garlicin cysteine are related to the prognosis of hypertrophic cardiomyopathy, can evaluate the prognosis of patients with hypertrophic cardiomyopathy after undergoing muscle resection of interventricular septum, and shows accurate judgment on all-cause death or rehospitalization, cardiovascular events and postoperative new-onset arrhythmia. Finally, all the prognostic biomarkers are reproduced in an independent cohort, which is helpful for postoperative risk evaluation of patients with hypertrophic cardiomyopathy, has high specificity and high sensitivity.

Provided is a cyclic peptide, which has a sequence of cyclo(X1X2X3X4X5X6), wherein X1 is asparagine; X2 is glycine or sarcosine; X3 is arginine; X4 is selected from a group consisting of threonine, tyrosine, and phenylalanine; X5 is lysine; and X6 is selected from a group consisting of tyrosine, valine, and glutamic acid. Provided is a preparation method for the cyclic peptide. Provided is a complex, comprising the cyclic peptide, a linker, and a chelating agent. Provided is a use of the complex as a radionuclide-labeled targeting molecule. Provided is a radionuclide labeling method, comprising bringing a complex that chelates a radionuclide into contact with an object to be labeled by the radionuclide.

A recombinant adeno-associated virus (rAAV) vector comprising an AAVhu68 capsid produced in a production system comprising a nucleotide sequence of SEQ ID NO: 1, or a sequence at least 75% identical thereto which encodes SEQ ID NO:2. The AAVhu68 capsid comprises subpopulations of highly deamidated asparagine residues in asparagine-glycine pairs in the amino acid sequence of SEQ ID NO: 2. Also provided are compositions containing the rAAV and uses thereof. Additionally, rAAV having an engineered AAV capsid comprising at least one subpopulation of vp1 or vp2 proteins having a Val at amino acid position 157 with reference to the AAVhu68 vp1 numbering are provided.

This invention discloses a mutant, gene, and recombinant bacteria of a highly thermostable single-chain sweet protein. The mutant is characterized by the following amino acid sequences shown in SEQ ID NO.1: isoleucine (I) at position 5 is mutated to glutamic acid (E), glutamic acid (E) at position 23 is mutated to alanine (A), isoleucine (I) at position 26 is mutated to arginine (R), cysteine ​​(C) at position 41 is mutated to alanine (A), tyrosine (Y) at position 65 is mutated to isoleucine (I), glycine (G) at position 83 is mutated to arginine (R), and asparagine (N) at position 90 is mutated to glutamic acid (E). Based on structural analysis and computationally assisted design for protein stability, this invention achieves site-directed mutagenesis of the single-chain sweet protein, resulting in a highly thermostable mutant. Compared to the original single-chain sweet protein, the thermostable mutant of this invention exhibits higher T... m It was heated by more than 20.4°C while maintaining its sweetness.

The application discloses a mutant and gene of single-chain sweet protein with high thermal stability, wherein the mutant is obtained by mutating isoleucine (I) at the 5th position, glutamic acid (E) at the 23rd position, isoleucine (I) at the 26th position, tyrosine (Y) at the 65th position, glycine (G) at the 83rd position and asparagine (N) at the 90th position in the amino acid sequence shown in SEQ ID NO. 1 to alanine (A), arginine (R), isoleucine (I), glutamic acid (E) and aspartic acid (D) respectively; the application is based on structural analysis and protein stability calculation aided design, and the single-chain sweet protein is subjected to site-directed mutagenesis, so that the mutant of single-chain sweet protein with high thermal stability is obtained; compared with the single-chain sweet protein, the mutant of single-chain sweet protein with high thermal stability has a T m increase of 18.4 DEG C or more and maintains sweetness.

The application provides a pyroglutamic acid transaminase mutant and application thereof, the mutant is obtained by mutation on the basis of wild-type pyroglutamic acid transaminase, and specific mutation includes at least one of the following sites: (1) the 13th isoleucine is mutated into arginine; (2) the 35th valine is mutated into arginine; (3) the 183rd asparagine is mutated into aspartic acid; and the mutant is suitable for industrial enzymatic production of L-aspartic acid and the process of amino acids taking L-aspartic acid as a precursor; especially, the I13R / V35R / N183D mutant obtained by modification has high positive catalytic activity and strict direction selectivity, and completely loses the reverse reaction activity of decomposing L-aspartic acid; the mutant is overexpressed with phosphoenolpyruvate carboxylase in L-threonine production strain THRS-6, and a high-efficiency L-threonine synthesis metabolic pathway is constructed, and the yield of L-threonine is significantly improved when glucose is used as a substrate.

This invention relates to a formate dehydrogenase mutant and its applications, belonging to the field of enzyme engineering. The formate dehydrogenase mutant is derived by mutating one or more of the following positions in the amino acid sequence shown in SEQ ID NO.1: tryptophan at position 128 is mutated to lysine, alanine at position 225 is mutated to valine, tryptophan at position 595 is mutated to cysteine, asparagine at position 750 is mutated to cysteine, aspartic acid at position 759 is mutated to valine, and serine at position 888 is mutated to glutamic acid. The formate dehydrogenase mutant provided by this invention has significant advantages in substrate affinity, catalytic activity, and enzyme stability, thereby increasing its value in industrial applications.

The invention relates to methods of inhibiting hair growth in a subject, the method comprises administering an inhibitor of lactic acid fermentation to the subject, wherein the inhibitor is selected from the group consisting of pyruvate dehydrogenase kinase inhibitor, desoxyrhapontigenin, a phosphofructokinases inhibitor, a thioredoxin-1 inhibitor, L- Asparaginase, a GLUT1 inhibitor, a glutaminase C inhibitor, a hexokinase inhibitor and an mTORCI and mTORC2 inhibitor. Also provided herein are compositions for inhibiting hair growth and methods of screening for inhibitors of hair growth.

This invention discloses a cyclic nonapeptide with both anti-photoaging and antioxidant effects. The amino acid sequence of the cyclic nonapeptide is: cyclic (arginine-glycine-aspartic acid-serine-asparagine-lysine-valine-lysine-phenylalanine). The cyclic nonapeptide of this invention can effectively reduce deep photoaging caused by UVA and surface oxidative damage induced by UVB, thereby achieving comprehensive skin protection.

2 Methods of Treatment with Asparaginase Abstract The invention relates to methods of treating diseases with L-asparaginase. Methods of Treatment with Asparaginase Abstract The invention relates to methods of treating diseases with L-asparaginase. 2 20 24 27 82 86 11 D ec 2 02 4 2 0 2 4 A b s t r a c t 2 0 2 4 2 7 8 2 8 6 1 1 D e c 2

This invention discloses a mutant of cellobiose 2-epimerase and a method for improving the production efficiency of ipilactose, belonging to the fields of enzyme engineering and biocatalysis. This invention aims to overcome the bottlenecks of CsCE in terms of catalytic activity, thermal stability, and application cost. This invention provides a mutant of cellobiose 2-epimerase, with the mutant starting from SEQ ID NO.1, where the valine position at position 52 is mutated to asparagine. This provides a practical solution for the green, efficient, and large-scale production of ipilactose.

This invention relates to: a method for preparing a galactosylation-controlled target recombinant protein or a method for controlling the galactosylation of a target recombinant protein, comprising the step of increasing the osmotic pressure of the culture solution of animal cells expressing the target recombinant protein during animal cell culture; a method for preparing a galactosylation-controlled target recombinant protein or a method for controlling the galactosylation of a target recombinant protein, comprising the step of supplementing the culture solution of animal cells expressing the target recombinant protein with asparagine during animal cell culture; a method for preparing a galactosylation-controlled target recombinant protein or a method for controlling the galactosylation of a target recombinant protein, comprising the step of increasing the osmotic pressure of the culture solution of animal cells expressing the target recombinant protein and supplementing it with asparagine during animal cell culture; and a galactosylation-controlled target recombinant protein prepared by said method.

This invention discloses a method for preparing a xylitol dehydrogenase mutant, relating to the field of industrial biotechnology. The method involves obtaining an amino acid sequence for the xylitol dehydrogenase mutant by substituting serine at position 77 with cysteine, serine at position 106 with asparagine, and alanine at position 110 with asparagine, based on the amino acid sequence shown in SEQ ID NO. 1. A recombinant vector containing a nucleic acid molecule encoding the xylitol dehydrogenase mutant is constructed. The recombinant vector is introduced into host cells, the host cells are cultured and the xylitol dehydrogenase mutant is expressed, and cells containing the xylitol dehydrogenase mutant are collected or isolated from cells. This invention reduces intermediate accumulation and improves xylitol conversion rate.

This invention provides a 3-sterone-Δ 1 -Dehydrogenase mutants and their application in the preparation of steroidal drug intermediates. 3-Sterone-Δ 1 -Dehydrogenase mutants are based on the wild-type 3-sterone-Δ amino acid sequence as shown in SEQ ID NO:1. 1 The enzyme was obtained by mutating amino acid position 425 of the β-dehydrogenase to glutamine, glycine, aspartic acid, or asparagine. This invention utilizes molecular docking combined with computer-aided mutation site prediction and single-point mutation verification of the amino acid at the catalytic center of the PrKstD enzyme to obtain a series of enzymes capable of enhancing 3-sterone-Δ... 1 A mutant with the activity of dehydrogenase catalyzing the synthesis of steroidal drug intermediates. The 3-sterone-Δ 1 The dehydrogenase mutant exhibits higher activity towards the substrate, effectively improving catalytic activity and reaction stability, and realizing a low-cost, green and efficient catalytic mode.

This invention relates to the use of a class of deaminases or transaminases and their cofactors or metabolic substrates as drugs for the treatment of polyglutamine diseases. Specifically, this invention discovers that a series of transaminases and deaminases (such as asparagine synthase ASNS) can degrade polyglutamine aggregates by deaminating polyglutamine (polyQ) proteins, thereby treating polyglutamine diseases.

The application relates to the technical field of microbial culture medium, and discloses a chemical component limited culture medium for supporting growth of bifidobacterium and application thereof. The CDM comprises a carbon source, salts, amino acids, vitamins and water; the carbon source is selected from at least one of glucose, fructose, lactose, maltose and galactooligosaccharide, the salts comprise sodium acetate, potassium hydrogen phosphate, ammonium acetate, magnesium sulfate heptahydrate, ferrous sulfate heptahydrate, sodium chloride and manganese sulfate monohydrate, the amino acids comprise alanine, cystine, cysteine, tryptophan and asparagine, and the vitamins comprise pyridoxine hydrochloride, nicotinic acid, calcium pantothenate, thiamine hydrochloride, riboflavin, p-aminobenzoic acid, folic acid and biotin. The CDM of the application is a liquid culture medium, only comprises 21 definite components, is simple in components, convenient in preparation, and is high in universality, and can effectively support growth of bifidobacterium.

A composition for preventing, ameliorating, or treating mitochondrial disorders according to the present invention comprises a peptide consisting of the amino acid sequence of general formula 1: K-Y-R1-R2-R3-R4-R5-R6-R7-R8 (general formula 1), wherein, in general formula 1, R1 is arginine (R), lysine (K), or glutamine (Q); R2 is arginine (R) or glutamine (Q); R3, R4, and R5 are each arginine (R) or lysine (K); R6 is asparagine (N) or serine (S); and R7 and R8 are lysine (K) or tyrosine (Y). The composition according to the present invention can prevent, ameliorate, or treat mitochondrial disorders by reducing oxidative stress caused by increased reactive oxygen species in cells.

The present invention provides a tobacco filler that allows flexibility in the ratio of saccharides to amino acids in tobacco sheet form. The tobacco filler comprises a first tobacco sheet, a second tobacco sheet, or a combination thereof. Each of the first and second tobacco sheets contains three saccharides selected from glucose, fructose, sucrose, and mixtures thereof, and three amino acids selected from aspartic acid, glutamic acid, asparagine, and mixtures thereof. The first tobacco sheet has a saccharide-to-amino acid mass ratio of 50 or more, while the second tobacco sheet has a saccharide-to-amino acid mass ratio of 20 or less.

The present application relates to a kind of specific synthesis plant inulin of inulin sucrose enzyme mutant and its application, the mutant is the 300th aspartic acid of wild type inulin sucrose enzyme from Lactobacillus reuteri (Lactobacillus reuteri) Limosilactobacillus reuteri ) Mutated into alanine.It precisely cuts off the ability of wild type enzyme to synthesize million Dalton high molecular weight microbial inulin at molecular level, while perfectly retaining the synthesis ability of medium-low degree of polymerization inulin.This mutant fundamentally solves the problem of wild type enzyme product molecular weight distribution extremely wide, component complex, realizes the efficient biosynthesis of specific inulin.At the same time, it can greatly reduce the difficulty and energy consumption of downstream separation and purification process, significantly reduce production cost.In the high-quality inulin large-scale green manufacturing of food and health product industry, it has great application value.

An Fc-binding polypeptide with improved alkaline stability comprising a mutant of the Fc-binding domain of Staphylococcus protein A (SpA), said mutant being defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO 51 or EQ ID NO 52, wherein at least the asparagine or serine residue at a position corresponding to position 11 in SEQ ID NO: 4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

This invention relates to an endonuclease β-agarase, its mutants, mutation methods, and applications, belonging to the field of biotechnology. This invention discloses for the first time a mutant of *Pseudomonas alterniflora* (…). Pseudoalteromonas An endonuclease β-agarase, ORF2093, was obtained from strain A601. This endonuclease β-agarase ORF2093 exhibits certain thermal stability, wide pH tolerance, and stable physicochemical properties, thus possessing potential for industrial application. This invention employs rational design and site-directed mutagenesis technology to mutate the serine residue at position 373 in the non-catalytic region of the endonuclease β-agarase ORF2093 to asparagine. The resulting mutant showed significantly enhanced relative activity compared to the wild type, and it was found that the mutant enzyme possesses the ability to degrade novel agaroctaose substrates.

Provided in the present invention are a lipid nanoparticle conjugate, and a preparation method therefor and the use thereof. In particular, an antibody is conjugated to the surface of an LNP via the N-glycosylation site of an Fc heavy chain by using a copper-free click chemistry reaction, thereby obtaining an LNP with specific cell or tissue targeting properties. Preferably, the N-glycosylation site is located on the asparagine residue at position 297 of the Fc heavy chain.

This invention relates to an asparagine peptide mixture, its preparation method, and its application in the preparation of products that delay skin aging, belonging to the field of cosmetic technology. The asparagine peptide mixture provided by this invention is an active peptide mixture with a molecular weight <5 kDa, prepared from asparagus root tubers via enzymatic hydrolysis. This asparagine peptide mixture can significantly enhance the vitality of human skin fibroblasts (HSF), promote cell proliferation, and enhance the tissue repair capacity of HSF cells; it can effectively inhibit β-galactosidase activity while increasing the expression level of pre-type I collagen. Furthermore, this invention identifies the top ten most active short peptides in the asparagine peptide mixture through structural identification and activity screening, and demonstrates through molecular docking that the asparagine peptide mixture intervenes in the skin aging process through multiple pathways, providing solid in vitro scientific evidence for the development of natural peptide cosmetics with multiple anti-aging effects from the traditional medicinal plant asparagus.

This invention discloses a phase-separated polypeptide based on LARKS encoding and its antibacterial application. The polypeptide has the structural formula A-B-(G). m -X1GGGS-X2G; where A is the phase separation driving unit, selected from π-electron-rich aromatic hydrophobic segments; B is a cationic amino acid, selected from lysine, arginine, and histidine; (G) m The linker is a flexible linker, m=0,1,2 or3, and G is glycine; X1GGGS is the LARKS core sequence, X1 is selected from phenylalanine, tyrosine, tryptophan, and serine; X2G is the C-terminal flexible tail, and X2 is selected from glycine, serine, threonine, asparagine, glutamine, and glutamic acid; the phase separation driving unit induces liquid-liquid phase separation of the polypeptide through π-π interaction and forms cation-π interaction with its adjacent cationic amino acid B.

This application relates to the field of bioengineering technology, specifically to a cyanide dihydrate mutant. The amino acid sequence of the cyanide dihydrate mutant, compared to the wild-type cyanide dihydrate enzyme sequence, involves mutations at one or more amino acids at positions 34, 97, 225, 301, and 307. The mutated amino acid is selected from arginine, aspartic acid, asparagine, or lysine. Compared to the wild-type cyanide dihydrate mutant, the cyanide dihydrate mutant of this invention exhibits significantly improved cyanide dihydrate enzyme activity, as well as strong catalytic activity, alkali resistance, and high-temperature resistance. It retains high enzyme activity in alkaline solvent reaction systems and can degrade cyanide under high-temperature conditions, demonstrating excellent prospects for industrial application.

The present invention relates to a detoxifying peptide, characterized in that its sequence comprises the following general amino acid sequence: N-(Val-Gly-X1-X2-Pro-Gly)n-OH, in which: N and OH correspond respectively to the N-terminal and C-terminal end of the peptide; X1 and X2 are chosen from valine (Val), glycine (Gly), threonine (Thr), asparagine (Asn), glutamine (Gln), alanine (Ala), leucine (Leu) and isoleucine (Ile); n is an integer between 1 and 3; for use in the treatment and / or prevention of a disorder associated with glycation and / or glycoxidation of proteins and / or lipids.

This invention discloses a modified American cockroach polypeptide derivative, its preparation method, polypeptide composition, and applications. The amino acid sequence of the polypeptide derivative is shown in SEQ ID NO: 1 (PA1702); it is modified by replacing the asparagine at position 13 of the natural polypeptide PA1701 with glutamine, and can be prepared by Fmoc solid-phase polypeptide synthesis. Network pharmacology predicts that it acts on 59 core anti-inflammatory targets, enriched in pathways such as PI3K-Akt and MAPK. Molecular docking shows that PA1702 has a strong binding affinity for TNF-α and AKT1. In vitro experiments confirm that PA1702 is non-cytotoxic, can inhibit LPS-induced release of NO, TNF-α, IL-6, and IL-1β, and promote cell migration. The above-mentioned polypeptide derivative can be used as an active ingredient in cosmetics or pharmaceutical compositions; it has anti-inflammatory, skin barrier repair, and wound healing promotion effects, and can be used to prepare anti-inflammatory, skin barrier repair, and wound healing-promoting cosmetics or drugs.