The present invention relates generally to production methods, enzymes and recombinant yeast strains for the biosynthesis of clinically important cannabinoid compounds.

Disclosed are a nucleic acid molecule, a polypeptide having epoxy group-removing catalytic activity and use thereof. According to the invention, by means of genetic engineering, the nucleic acid molecule encoding a de-epoxidation protein is expressed in a plant, so that an epoxy group of a trichothecene mycotoxin is removed, and the toxin amount in the plant is reduced. The polypeptide of the invention is capable of catalyzing a reaction between vomitoxin and glutathione under mild conditions to remove epoxy groups to produce a glutathionylated derivative.

Synthetic cannabinoid compounds for treatment of epilepsy, substance addiction, and Alzheimer's disease by administering to an individual in need thereof a pharmaceutical composition including a compound having the structure: ##STR00001##
or a pharmaceutically acceptable salt thereof, and a pharmaceutically acceptable vehicle therefor.

An isolated polynucleotide encoding a modified luciferase polypeptide and substrates. The OgLuc variant polypeptide has at least 60% amino acid sequence identity to SEQ ID NO: 1 and at least one amino acid substitution at a position corresponding to an amino acid in SEQ ID NO: 1. The OgLuc variant polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the corresponding polypeptide of the wild-type Oplophorus luciferase.

A method of producing electrical power includes: a cathode having a porphyrin precursor attached to a substrate, and having a first enzyme, wherein the first enzyme reduces oxygen; an anode having a first region of an anode substrate and having a gold nanoparticle composition located thereon, and having a second region of the anode substrate having an enzyme composition located thereon, wherein the enzyme composition includes a second enzyme, wherein the first region and second region are separate regions; and a neutral fuel liquid in contact with the anode and cathode, the neutral fuel liquid having a neutral pH and a fuel reagent; and operating the fuel cell to produce electrical power with the neutral fuel liquid having the neutral pH and the fuel reagent.

A production method for a crystal of a crystalline protein, the method including a step of inducing expression of a crystalline protein in Escherichia coli into which an expression construct of the crystalline protein has been introduced, and incubating the Escherichia coli for a predetermined time until a crystal of the crystalline protein is formed inside the Escherichia coli, and a crystal structure analysis method including a step of subjecting a crystal produced by the above-described production method to an X-ray crystal structure analysis together with the Escherichia coli, are useful as technologies for conveniently producing and analyzing a crystal of a protein.

The present invention provides for a mechanism to completely replace the electron accepting function of glycerol formation with an alternative pathway to ethanol formation, thereby reducing glycerol production and increasing ethanol production. In some embodiments, the invention provides for a recombinant microorganism comprising a down-regulation in one or more native enzymes in the glycerol-production pathway. In some embodiments, the invention provides for a recombinant microorganism comprising an up-regulation in one or more enzymes in the ethanol-production pathway.

Phosphite dehydrogenase (ptxD) expression was established as a selectable marker for nuclear and chloroplast genetic selection in Picochlorum renovo and Picochlorum celeri Phosphite was used as a sole phosphorus source in P. renovo and P. celeri. Growth on phosphite led to comparable growth and composition relative to phosphate.

The present invention refers to a modified D-amino acid oxidase (DAAO). In particular, the modified DAAO of the present invention has the activity of catalyzing the oxidation of D-glufosinate into PPO. Further, the modified DAAO of the present invention has increased activity of catalyzing the oxidation of D-glufosinate into PPO and/or increased stability as compared to SEQ ID NO: 4. The present invention also refers to the polynucleotide encoding the modified DAAO of the present invention, the vector and host cell expressing the modified DAAO of the present invention, and the method of producing L-glufosinate with the modified DAAO and host cell of the present invention.

A genetically engineered strain having high-yield of L-valine is disclosed. Starting from Escherichia coli W3110, an acetolactate synthase gene alsS of Bacillus subtilis is inserted into a genome thereof and overexpressed; a ppGpp 3′-pyrophosphate hydrolase mutant R290E/K292D gene spoTM of Escherichia coli is inserted into the genome and overexpressed; a lactate dehydrogenase gene ldhA, a pyruvate formate lyase I gene pflB, and genes frdA, frdB, frdC, frdD of four subunits of fumaric acid reductase are deleted from the genome; a leucine dehydrogenase gene bcd of Bacillus subtilis replaces a branched chain amino acid transaminase gene ilvE of Escherichia coli; and an acetohydroxy acid isomeroreductase mutant L67E/R68F/K75E gene ilvCM replaces the native acetohydroxy acid isomeroreductase gene ilvC of Escherichia coli. Furthermore, the L-valine fermentation method is improved by using a two-stage dissolved oxygen control. The L-valine titer and the sugar-acid conversion rate are increased.