17 results about "Acetolactate synthase" patented technology

This invention belongs to the field of agricultural herbicides and provides a photosynthetic inhibitor herbicidal composition comprising 5-aminolevulinic acid, malondialdehyde, and a herbicidal active ingredient. The herbicidal active ingredient is selected from one or a combination of several herbicides selected from acetolactate synthase inhibitors, photosynthetic system II inhibitors, or protoporphyrinogen oxidase (PPO) inhibitors. This invention utilizes the synergistic effect of 5-aminolevulinic acid, malondialdehyde, and a specific type of herbicidal active ingredient to effectively enhance the efficacy of the herbicidal active ingredient, enabling rapid and thorough weed control.

This invention belongs to the fields of applied environmental microbiology and agricultural biotechnology, and discloses ImALS, an acetyllactone synthase resistant to high concentrations of methoxylamine, its encoding gene, and its applications. Its nucleotide sequence is SEQ ID NO.1, with a full length of 1785 bp, encoding 594 amino acids, and its amino acid sequence is SEQ ID NO.2. ImALS shares less than 58.3% homology with previously reported acetyllactone synthases, thus representing a novel ALS gene. The acetyllactone synthase ImALS provided by this invention exhibits a specific activity of 0.52 mM / mg against sodium pyruvate. ImALS demonstrates strong resistance to the ALS inhibitor methoxylamine herbicide, with a half-maximal inhibitory concentration (IC50) of 1500 μM, indicating that the ImALS gene has significant application potential in methoxylamine-resistant transgenic engineering.

The invention provides a lactic acid bacteria genetic engineering strain for producing acetic acid as well as a construction method and application thereof, and belongs to the technical field of genetic engineering and microbial fermentation. The lactic acid bacterium gene engineering strain is a lactic acid bacterium gene engineering strain in which two lactic dehydrogenase and one acetolactate synthase are knocked out. According to the lactic acid bacteria gene engineering strain for producing the acetic acid, the lactic acid bacteria gene engineering strain for producing the acetic acid is obtained by taking Lacticaseibacillus casei Zhang as an original strain and sequentially knocking out key lactic acid metabolic enzyme genes including lactic dehydrogenase LCAZH0554, lactic dehydrogenase LCAZH2512 and acetolactate synthase LCAZH1837 by utilizing a gene knockout means to enhance an acetic acid generation pathway, and the lactic acid bacteria gene engineering strain for producing the acetic acid can stably produce the acetic acid under a fermentation system or a biological reaction condition. The yield of acetic acid after static fermentation of the lactic acid bacterium genetically engineered bacterium is remarkably improved compared with that of an original lactic acid bacterium strain.

The invention belongs to the technical field of gene engineering and crop breeding, and particularly relates to a brassica campestris ALS natural variant gene, a mutant protein and application thereof. The Brassica campestris ALS mutant gene BrALS3R is found in rapes for the first time, consists of 1959 bases, is naturally mutated and encodes rape acetolactate synthetase III (ALS3), and compared with a wild ALS3 gene, the 1074th base of the Brassica campestris ALS mutant gene BrALS3R mutates from C to A, so that the 358th amino acid of mutant protein encoded by the Brassica campestris ALS mutant gene BrALS3R mutates from aspartic acid to glutamic acid (D358E). A plant containing the BrALS3R gene has ALS herbicide resistance, so that the gene is introduced into a plant without ALS herbicide resistance by utilizing a crossbreeding or transgenosis method, and the resistance of a receptor plant to the ALS herbicide can be improved.

Provided are a genetically engineered bacterium for high-yield production of D-pantothenic acid (D-PA), and a preparation method therefor and a use thereof. The D-PA production yield of the engineered bacterium is significantly improved by means of the following actions: overexpressing acetolactate synthases IlvB and IlvN for pyruvate diversion while deleting a transcription attenuation region and mutating a valine feedback inhibition site; overexpressing ketol-acid reductoisomerase IlvC and dihydroxy acid dehydratase IlvD, and altering the coenzyme preference of IlvC from NADPH to NADH to unlock the upstream pathway for D-PA synthesis; overexpressing PanB and overexpressing a serine-glycine transport system to promote the synthesis of 5,10-methylenetetrahydrofolate; at the same time, enhancing the expression of ketopantoic acid reductase PanE; and finally overexpressing pantothenate synthetase PanC and increasing the content of cofactor ATP required by PanC. By means of the integrated enhancement of the above multiple modules, the provided engineered bacterium achieves improved cell growth due to balanced cofactors and increased D-PA.

This application provides herbicidal compositions containing (a) fluroxypyr or an agriculturally acceptable ester or salt thereof and (b) an acetolactate synthase (ALS) inhibitor herbicide, wherein the ALS inhibitor herbicide is diclosulam, chloransulam, chlorimuron, or tifensulfuron, or an agriculturally acceptable ester or salt thereof. The compositions provide synergistic weed control of undesirable vegetation in areas including, but not limited to, soybean, cotton, corn, sorghum, sunflower, sugarcane, sugar beet, alfalfa, cereals (including but not limited to wheat, barley, rice, and oats), uncultivated areas, fallow areas, perennial crop areas, fruit orchards, or plantation crops.

The application discloses an acetyl lactic acid synthase mutant and application thereof, and belongs to the technical field of bioactive enzymes. The acetyl lactic acid synthase mutant is acetyl lactic acid synthase-PCC6803-L255I, acetyl lactic acid synthase-PCC6803-V398I or acetyl lactic acid synthase-PCC6803-T488V. The application of the acetyl lactic acid synthase mutant in catalyzing preparation of acetyl lactic acid. The acetyl lactic acid synthase derived from PCC6803 is reformed by a site-directed mutation method, and mutant enzymes, acetyl lactic acid synthase-PCC6803-L255I, acetyl lactic acid synthase-PCC6803-V398I and acetyl lactic acid synthase-PCC6803-T488V, are screened, and the catalytic efficiency of the mutant enzymes is 120%, 130% and 110% of that of the wild enzyme respectively. The application lays a technical foundation for metabolic engineering of a blue-green algae photosynthetic cell factory.

The invention discloses a breeding method for creating acetolactate synthase herbicide-resistant brassica napus through sweet and white interspecific hybridization. The breeding method comprises the following steps: performing acetolactate synthase ALS herbicide tolerance screening on the brassica napus; the method comprises the following steps: carrying out BnALS3 gene sequence identification on fresh and tender leaves of a tolerant Brassica campestris L. resource material MYC-1 in a seedling stage; the tolerance characteristic of acetolactate synthase ALSALS herbicides of a brassica napus resource material MYC-1 is introduced into brassica napus, and a brassica napus parent material resistant to ALS herbicides is obtained. By utilizing the method disclosed by the invention, the tolerance of the brassica napus to acetolactate synthase ALS herbicides can be improved.

Provided are a herbicidal composition and a method for controlling weeds that have a superior weed controlling effect. The present herbicidal composition comprises one or more uracil compounds selected from the group consisting of a compound represented by formula (I) and a compound represented by formula (II), and one or more compounds selected from the group consisting of the herbicide compound group B and the safener group C, wherein a weight ratio of the uracil compounds to one or more compounds selected from the group consisting of the herbicide compound group B and the safener group C is 1:0.02 to 1:50, and the herbicide compound group B is the group consisting of the following B-1 to B-12 below: B-1, acetolactate synthase inhibitors; B-2, acetyl CoA carboxylase inhibitors; B-3, protoporphyrinogen IX oxidase inhibitors; B-4, 4-hydrophenylpyrubic acid dioxygenase inhibitors; B-5, phytoene desaturase inhibitors; B-6, photosystem II inhibitors; B-7, very-long-chain fatty acid synthesis inhibitors; B-8, microtubule formation inhibitors; B-9, auxin-type herbicides; B-10, enolpyruvylshikimate-3-phosphate synthase inhibitors; B-11, glutamine synthase inhibitors; and B-12, other herbicides; (including agriculturally acceptable salts or derivatives thereof).

A herbicidal composition and a method for controlling weeds, including one or more uracil compounds of formula (I) and a compound of formula (II), and a herbicide compound of group B and a safener of group C. A weight ratio of the uracil compounds to the herbicide compound group B and the safener group C is 1:0.02 to 1:50, and the herbicide compound of group B is one or more of compounds B-1 to B-12: B-1, acetolactate synthase inhibitors; B-2, acetyl CoA carboxylase inhibitors; B-3, protoporphyrinogen IX oxidase inhibitors; B-4, 4-hydrophenylpyrubic acid dioxygenase inhibitors; B-5, phytoene desaturase inhibitors; B-6, photosystem II inhibitors; B-7, very-long-chain fatty acid synthesis inhibitors; B-8, microtubule formation inhibitors; B-9, auxin-type herbicides; B-10, enolpyruvylshikimate-3-phosphate synthase inhibitors; B-11, glutamine synthase inhibitors; and B-12, other herbicides; or agriculturally acceptable salts or derivatives thereof

The application discloses a new sulfonylurea herbicide-resistant mutation gene of Brassica napus and application thereof, and relates to the field of plant molecular breeding. The application provides a breeding method for creating sulfonylurea (SU) herbicide-resistant rapeseed through interspecific distant cross of Brassica napus and self-crossing for 6 generations, and specifically comprises the following steps: creating a new sulfonylurea herbicide-resistant Brassica napus NR9 through interspecific distant cross of Brassica napus and self-crossing for 6 generations; performing PCR amplification on the NR9 by using specific primers of an acetolactate synthase gene (ALS3) to obtain three new nucleotide mutation site sequences of the NR9 on the ALS3, and the three new nucleotide mutation site sequences are respectively a 312th nucleotide, a 535th nucleotide and an 816th nucleotide; and introducing the gene containing the mutation site into other rapeseed germplasm which is not resistant to sulfonylurea herbicide by using plant conventional breeding methods such as hybridization and backcrossing to improve the tolerance of the target variety or strain of the ALS3 gene mutation nucleic acid sequence to the sulfonylurea herbicide.

The invention provides an engineering bacterium for producing D-pantothenic acid as well as a construction method and application of the engineering bacterium. The engineering bacterium expresses an acetolactate synthase large subunit gene ilv2, an acetolactate synthase small subunit gene ilv6, a keto acid reductoisomerase gene ilvC, a dihydroxy acid dehydratase gene ilvD, a hydroxymethyltransferase gene ecm31, a keto pantoic acid reductase gene panE, an L-aspartic acid decarboxylase gene panD and a pantothenic acid synthase gene panC. According to the method, mitochondria is selected as a targeting compartment, and modular combination optimization approach positioning is adopted, so that the yield of D-pantothenic acid is greatly increased, compared with the yield of an original strain without spatial tissue optimization, the yield is increased by more than one time, the metabolic flux bottleneck in a traditional cytoplasm synthesis mode is broken through, and efficient synthesis of D-pantothenic acid is realized.

This invention provides an acetolactate synthase mutant, a valine-producing strain, its construction method, and its application. The acetolactate synthase mutant is obtained by mutating acetolactate synthase, specifically by mutating isoleucine at position 325 to threonine, serine at position 330 to arginine, and asparagine at position 477 to aspartic acid. The valine-producing strain constructed from the acetolactate synthase mutant is plasmid-free, has no growth defects, requires no induction, and possesses advantages such as good genetic stability and high fermentation yield. It is an excellent strain for stable valine production. This strain efficiently synthesizes valine de novo using glucose as a substrate, significantly increasing valine yield.

The invention relates to a recombinant halomonas. The recombinant halomonas comprises an alsS (acetolactate synthase) gene, an ilvC (acetohydroxyacid isoreductase) gene, an ilvD (dihydroxy acid dehydratase) gene and an ilvE (transaminase) gene which are externally introduced. According to the recombinant halomonas disclosed by the invention, the L-valine can be efficiently produced without sterilization, in an energy-saving and water-saving manner through open fermentation, and the industrial production of the L-valine is facilitated.

The invention belongs to the technical field of agricultural chemicals, and relates to a single-channel double-target weeding method for targeting branched chain amino acid biosynthesis, in particular to a single-channel double-target weeding method realized by combined use of an acetolactate synthase inhibitor and a keto-alcohol acid reductoisomerase inhibitor. According to the weeding method, an AHAS herbicide and a KARI inhibitor are compounded to serve as active ingredients to achieve the purpose of synergistic interaction, and the mass percent of the AHAS herbicide and the mass percent of the KARI inhibitor in the active ingredients are 1%: 99%-99%: 1% respectively. When weeding is carried out according to a specific proportion, the inhibition rate of the rape root length is measured on a plate model, the synergistic multiple can reach 10.43, and when weeding activity evaluation is carried out on a potted model, the synergistic multiple can reach 6.79. AHAS herbicides, including all commercial herbicides targeting AHAS, especially mesosulfuron, nicosulfuron, penoxsulam, bispyribac-sodium, imazapyr and triafamone, and KARI inhibitors, including all possible KARI inhibitors, especially the following three compounds

The application belongs to the technical field of synthetic biology, and a bacillus subtilis engineering bacterium is preserved in the China General Microbiological Culture Collection Center on March 11, 2026, with a preservation number of CGMCC No. 37899. The chassis strain bacillus subtilis is preserved in the China General Microbiological Culture Collection Center on March 3, 2026, with a preservation number of CGMCC No. 37834. The modification strategy is to knock out the alpha subunit gene of acetoin dehydrogenase and the phosphotransferase gene from the genome of bacillus subtilis CGMCC No. 37834, and express the acetolactate synthase gene and the alpha-acetolactate decarboxylase gene. The engineering bacterium can be used to prepare fermentation products containing the microbial-crop interaction signal substances acetoin and 2,3-butanediol, and can be used to promote the growth of crop roots, improve the growth and yield of crops.

The invention relates to acetolactate synthase and application thereof, and belongs to the technical field of enzyme engineering and metabolic engineering. Wild acetolactate synthase from Corynebacterium glutamicum ATCC13032 is taken as a basis, error-prone PCR is performed on a coding gene ilvBN of the wild acetolactate synthase, acetolactate synthase mutants IlvBNM1 and IlvBNM2 are obtained through screening, the feedback inhibition effects of L-valine, L-leucine and L-isoleucine on the mutants are relieved, and the activity of the mutants is improved. Under the condition that the concentrations of the L-valine, the L-leucine and the L-isoleucine are respectively 0-30 mmol / L, the enzyme activity is not obviously changed, and the method can be widely applied to synthesis of the L-valine, the L-leucine and the L-isoleucine.