16 results about "Amidase activity" patented technology

This invention relates to compounds of formula (I) and methods of treatment using the compounds. The compounds of the invention can be used in combination with antibacterial agents to treat bacterial infections. More specifically, the compounds of formula (I) can be used in combination with a class of antibacterial agents known as carbapenems. The novel compounds of the present invention are enzyme inhibitors and more particularly are metallo-β-lactamase inhibitors.

The invention discloses a beta-lactamase inhibitor intermediate eutectic crystal or salt and a preparation method and application thereof, and belongs to the technical field of pharmaceutical chemicals. The structural formula is shown in the specification, wherein R2 represents benzyl or allyl; and R3 represents alkyl amido with a protecting group, naphthenic amido, aromatic amido and derivative amido thereof. The preparation method comprises the following steps: dissolving a compound I in a solvent A, adding an alkali solution at the temperature of lower than 0 DEG C for reaction, then adding acid to adjust the pH to be acidic, adding a solvent B to extract a product, layering, and leaving an organic phase; and then adding a beta-lactamase inhibitor side chain R3H for reaction. The purity of the beta-lactamase inhibitor prepared from the intermediate eutectic or new salt is greater than 99.90%, the pharmaceutical quality standard of bulk pharmaceutical chemicals is met, and the technological process is safe, simple, convenient, green and environment-friendly to operate; the reaction in each step is high in atom economy, high in selectivity, high in purity and high in yield, and is suitable for large-scale production.

The present invention relates to a process for the preparation of glufosinate comprising the steps of hydrolyzing an N-carbamoyl glufosinate amide with an amidase to form an N-carbamoyl amino acid compound followed by cleavage of the carbamoyl moiety of the N-carbamoyl amino acid compound.

This invention relates to an oxobenzohexacyclic borate ester compound, its preparation method, and its uses, belonging to the pharmaceutical field. The derivatives of this invention are compounds represented by Formula I, or their salts, conformational isomers, or optical isomers. The oxobenzohexacyclic borate ester derivatives provided by this invention exhibit good, broad-spectrum inhibitory activity against clinically common metallo-β-lactamases (MBL) and serine β-lactamases (SBL), and show good antibacterial activity against various drug-resistant bacteria when used in combination with the β-lactam antibiotic meropenem. Therefore, the series of derivatives provided by this invention have great potential in the preparation of dual broad-spectrum inhibitors of MBL and SBL and in drugs to overcome β-lactam antibiotic-resistant bacteria. Formula I.

The invention provides an amidase mutant and application thereof in preparation of (S)-penthiopyrad, and belongs to the technical field of gene engineering and enzyme catalysis. Compared with amidase with an amino acid sequence as shown in SEQ ID No.1, the amidase mutant disclosed by the invention comprises one or more site mutations as follows: alanine at the 132 site is mutated into leucine; serine at the 205th site is mutated into glycine; the alanine at the 211 site is mutated into glycine. Compared with wild amidase, the amidase mutant disclosed by the invention has the advantages that the enzyme activity and stereoselectivity are obviously improved; the preparation method based on the mutant is mild in process and simple and convenient to operate, and the obtained (S)-penthiopyrad has excellent chiral selectivity and product optical purity, conforms to the development trend of green pesticide creation and has important industrial application value.

The present disclosure relates to an engineered microorganism having an exogenous gene encoding an amidase, where the microorganism is capable of catabolizing acetamide to produce a carboxylic acid without the use of an additional substrate.

The present invention relates to a process for recovering a polyamide, the process comprising: (i) subjecting the polyamide to acid hydrolysis in an aqueous liquid to produce polyamide oligomers soluble in the aqueous liquid; and (ii) converting the oligomer into its monomer component using an amidase.

The invention belongs to the technical field of fine chemical engineering, and discloses a directional synthesis process of high-decontamination N-lauroyl alanine. The process is characterized by comprising the following steps: constructing a lipase and amidase concerted catalysis system, coupling an electron transfer mechanism driven by visible light, generating acyl free radicals through mediation of a photosensitizer by taking lauric acid and L-alanine as raw materials in an aprotic solvent, and realizing alpha-amino high-selectivity N-acylation under the catalysis of a composite immobilized enzyme. According to the method disclosed by the invention, high-selectivity, high-efficiency and green oriented synthesis of N-lauroyl alanine is successfully realized through a synergistic reaction system of visible light catalysis, lipase and amidase, so that the long-standing fundamental contradiction in the prior art is solved; and a universal technical normal form is provided for clean manufacturing of other N-acylamino acid surfactants.

This invention provides an amidase mutant and its application in the preparation of ( S The application of pyrimethanil belongs to the fields of genetic engineering and enzyme catalysis technology. Compared with the amidase shown in SEQ ID No. 1, the amidase mutant of this invention contains one or more mutations at the following sites: alanine at position 132 is mutated to leucine; serine at position 205 is mutated to glycine; alanine at position 211 is mutated to glycine. Compared with wild-type amidase, the enzyme activity and stereoselectivity of the amidase mutant of this invention are significantly improved; based on the mild and simple preparation method of this mutant, the obtained ( S )-Pyrimethanil possesses excellent chiral selectivity and product optical purity, which aligns with the development trend of green pesticide creation and has significant industrial application value.

The invention belongs to the technical field of green chemistry, and particularly relates to a method for bi-directionally synthesizing chiral lactam through bi-enzyme cascade-chemical catalysis. According to a methylpiperidone synthesis route taking 2-methyl glutaronitrile as a raw material, nitrile hydratase is subjected to iterative saturated mutation, substrate channel residues and active site residues are subjected to semi-rational engineering transformation, and 4-cyano valeramide and 4-cyano-2-methyl butyramide are generated with high selectivity. And carrying out cascade reaction on the modified nitrile hydratase and amidase, so as to directionally generate the corresponding mono-cyano carboxylic acid. Then, a Raney nickel catalyst hydrogenation reaction is adopted to treat the whole-cell catalytic solution, and two regioselectivity products can be obtained, namely 5-methyl-2-piperidone (the yield is 96.9%, and the regioselectivity is 98.3%) and 3-methyl-2-piperidone (the yield is 67.9%, and the regioselectivity is 70.4%).

The application provides a method for synthesizing dextroketoprofen. The method comprises the following steps: S1: taking ketoprofen amide as a raw material, performing a hydrolysis reaction in a reaction medium, a cosolvent, a phase transfer catalyst and an amidase system, and performing separation and purification to obtain dextroketoprofen and levo-ketoprofen amide; S2: performing a chemical racemization reaction on the levo-ketoprofen amide in the presence of a solvent and a base to obtain ketoprofen amide; and repeating step S1 by taking the ketoprofen amide as a raw material. The method has high substrate concentration, low enzyme substrate ratio, high selectivity, high conversion rate and high product purity, higher efficiency, low solvent consumption, lower cost, fully utilized raw materials, less solid waste discharge, can meet the requirements of industrialized production of enzyme catalysis, and has good industrial application potential.

According to the 6-diazo-5-oxo-n-leucine derivative, the preparation method and the application, DON is released through a breakable amido bond, immunoregulation of sepsis-related macrophages can be achieved, the safety is high, immune response of sepsis mice can be effectively inhibited through polarization of M2 type macrophages, and the 6-diazo-5-oxo-n-leucine derivative has a good application prospect. Finally, the inflammation treatment of sepsis is realized. The derivative is a metabolic drug formed by connecting DON and leucine-PEG, the drug can be self-assembled into nano-particles, release DON to play an anti-inflammatory role and reduce systemic toxicity at inflammation parts with high esterase and amidase, and the derivative has good chemical stability and drug development potential, is suitable for further pharmacological research, and can be used for preparing a drug for treating inflammation. And the compound has good synthesizability and pharmaceutical properties.

The invention provides methods for stabilizing liquid enzyme compositions by incubating the liquid compositions at a temperature of at least 40°C for at least 24 hours, and subsequently removing precipitated solids.

This invention belongs to the fields of enzyme engineering and genetic engineering, specifically relating to nicotinamide enzyme mutants and their application in a method for producing nicotinic acid based on a nitrile hydratase-nicotinamide enzyme cascade catalytic system. The invention first identifies nicotinamide enzyme as the rate-limiting enzyme in the reaction pathway. Through directed evolution, a saturated mutant library is created, yielding a series of nicotinamide enzyme mutants with high catalytic efficiency. Among them, the A79S mutant shows the most significant increase in enzyme activity, reaching 759.2 U / mg, a 4.74-fold increase compared to the wild type. Subsequently, using a cascade reactor model, resting *E. coli* cells containing nitrile hydratase and nicotinamide enzyme mutant genes are connected in series. By controlling the optimal conditions for both strains, highly efficient continuous synthesis of NA is achieved, with a nicotinic acid yield of 298.4 g / L. Both nitrile hydratase and nicotinamide enzyme exhibit maximum catalytic efficiency, and both catalytic reactions are complete, while substrate inhibition is avoided.

Provided are a β-lactamase inhibitor and the use thereof. The β-lactamase inhibitor has a structure as represented by the below formula (I), or a pharmaceutically acceptable salt thereof, or an isomer thereof or a deuterated substance thereof. A group of the β-lactamase inhibitor capable of enhancing the lipid solubility of the compound binds to the amide and sulfonic acid groups in an avibactam structure, thereby increasing the lipid solubility of the structure. Under the action of biological enzymes, the β-lactamase inhibitor can rapidly and completely release an active metabolite, i.e. avibactam, and enabling the rapid onset of action thereof, which effectively improves the oral bioavailability of avibactam, and enables oral administration of avibactam, thereby solving the problem whereby avibactam cannot be be administered orally.

The present invention relates to a method for preparing glufosinate, comprising the steps of first hydrolyzing N-carbamoyl glufosinate amide with an amidase enzyme to form an N-carbamoyl amino acid compound, and then cleaving the carbamoyl portion of the N-carbamoyl amino acid compound.