Anti-sense-oriented RNA gene suppression agents in the form of a loop of anti-sense-oriented RNA is produced in cells of transgenic organisms, e.g. plants, by transcription from a recombinant DNA construct that comprises in 5′ to 3′ order a promoter element operably linked to more than one anti-sense-oriented DNA element and one or more complementary DNA elements.

The present disclosure provides a genetically modified mouse comprising a genomic nucleic acid encoding human APOE4, a genomic nucleic acid encoding mouse TREM2 modified to include a R47H substitution, and at least one genomic modification selected from the group consisting of: (a) a genomic nucleic acid encoding mouse ABCA7 modified to include an A 1541 G substitution; (b) a genomic nucleic acid encoding mouse APP modified to include G60IR, F606Y, and R609H substitutions; (c) a genomic nucleic acid encoding mouse PLCG2 modified to include a M28L substitution; (d) a genomic nucleic acid encoding mouse MTHFR modified to include a A262V substitution; (e) an inactivated Ceacaml allele; and (f) an inactivated II1rap allele. Methods of producing the genetically modified mouse and methods of using the genetically modified mouse are also provided.

Provided herein is a non-naturally occurring microbial organism (NNOMO) having a methanol metabolic pathway (MMP) that can enhance the availability of reducing equivalents in the presence of methanol. Such reducing equivalents can be used to increase the product yield of organic compounds produced by the microbial organism, such as succinate. Also provided herein are methods for using such an organism to produce succinate.

A minimally invasive device and method for suturing papillary muscles includes drawing a suture through a first papillary muscle using a needle, drawing the suture through a second papillary muscle, and tightening the suture to move at least one of the first papillary muscle and the second papillary muscle towards the other of the first papillary muscle and the second papillary muscle.

Provided are an L-glutamate dehydrogenase mutant and an application thereof, the mutant mutating the amino acid residue A at position 166 and/or the amino acid residue V at position 376 shown in SEQ ID NO. 1 into a hydrophilic or small sterically hindered amino acid residue, the application performing an amination reaction of 2-oxo-4-(hydroxymethylphosphinyl)butyrate in the presence of an L-amino acid dehydrogenase mutant, an inorganic amino donor, and a reduced coenzyme NADPH, and performing an acidification reaction on the obtained L-glufosinate salt to obtain L-glufosinate. Compared to wild L-glutamate dehydrogenase, the present L-glutamate dehydrogenase mutant has a higher concentration of substrates that can be catalysed when preparing L-glufosinate, thereby increasing the efficiency of the action of the enzyme and reducing reaction costs.

The present invention relates to methods and transformed host cells for the production of eriodictyol from naringenin via bioconversion.

Provided herein is a non-naturally occurring microbial organism having a methanol metabolic pathway that can enhance the availability of reducing equivalents in the presence of methanol. Such reducing equivalents can be used to increase the product yield of organic compounds produced by the microbial organism, such as 1,2-propanediol, n-propanol, 1,3-propanediol or glycerol. Also provided herein are methods for using such an organism to produce 1,2-propanediol, n-propanol, 1,3-propanediol or glycerol.

A method of demethylizing an opioid to a nor-opioid is provided. The method comprises contacting an opioid with at least one enzyme. Contacting the opioid with the at least one enzyme converts the opioid to a nor-opioid. A method of converting a nor-opioid to a nal-opioid is provided. The method comprises contacting a nor-opioid with at least one enzyme. Contacting the nor-opioid with the at least one enzyme converts the nor-opioid to a nal-opioid.

Disclosed in the present disclosure is a method for preparing (S)-1,2,3,4-tetrahydroisoquinoline-1-carboxylic acid and derivatives thereof, comprising: taking a racemate of a compound represented by Formula (I) or a racemate of a salt of the compound represented by Formula (I) as a substrate, and making a R-isomer of the compound represented by Formula (I) in the substrate react under the catalysis of oxidative dehydrogenase to generate imino acid represented by formula (II); and converting the imino acid represented by Formula (II) into an S-isomer of the compound represented by Formula (I) in the presence of pipecolic acid reductase and a coenzyme capable of supplying hydrogen anions. The present disclosure is featured by mild reaction condition, strong stereoselectivity, high reaction efficiency, high conversion rate, etc.

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Described herein are an immobilized enzyme, and a preparation method therefor and a use thereof. The immobilized enzyme includes activated PEI and an enzyme covalently bonded to the activated PEI, where the enzyme is selected from any one of a transaminase, a ketoreductase, a monooxygenase, an ammonia lyase, an ene-reductase, an imine reductase, an amino acid dehydrogenase and a nitrilase.