8 results about "Amidase activity" patented technology

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 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 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 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.