C12N9/0006

PTERIN-DEPENDENT BIOCATALYSTS AND USES THEREOF
20170362617 · 2017-12-21 ·

Provided herein are biocatalysts and systems thereof for pterin-dependent enzymes and pathways and methods of making and using the same. Provided herein in some embodiments are biocatalysts having a pterin source and a pterin-dependent enzymatic pathway biologically coupled to the pterin source. Tetrahydrobiopterin (referred to herein as BH4 or BH 4) can be the pterin source. The BH4 can be synthesized by a tetrahydrobiopterin synthesis pathway. The tetrahydrobiopterin synthesis pathway can include a GTP cyclohydrase; a pyruvoyl tetrahydropterin synthase; a sepiapterin reductase, and/or any combination thereof. The biocatalyst can further contain a pterin-dependent enzymatic pathway. The pterin-dependent enzymatic pathway can be amino acid mono-oxygenase, phenylalanine hydroxylase, tryptophan hydroxylase, tyrosine hydroxylase, nitric oxide synthase, alkylglycerol monooxygenase, and/or any combination thereof.

COMPOSITIONS AND METHODS FOR SUCCINATE PRODUCTION

The present application provides genetically modified yeast cell comprising an active succinate fermentation pathway, as well as methods of using these cells to produce succinate.

METHODS AND COMPOSITIONS FOR REDUCING CLOSTRIDIUM DIFFICILE INFECTION

The present invention relates to methods and compositions for reducing the risk and severity of C. difficile infection. It is based, at least in part, on the discovery that a restricted fraction of the gut microbiota, including the bacterium Clostridium scindens, contributes substantially to resistance against C. difficile infection. Without being bound by any particular theory, it is believed that this is achieved through the biosynthesis of secondary bile acids.

METHODS AND COMPOSITIONS FOR EFFICIENT GENETIC MODIFICATIONS OF BACILLUS LICHENIFORMIS STRAINS

The instant disclosure is generally related to compositions and methods for obtaining and constructing Bacillus licheniformis host cells (e.g., protein production host cells, cell factories) having increased protein production capabilities. Certain embodiments of the disclosure are directed to efficient genetic modifications of B. licheniformis cells and the subsequent selection of such B. licheniformis cells having increased protein production capabilities. Certain other embodiments of the disclosure are generally related to methods and compositions for producing/obtaining auxotrophic B. licheniformis cells, wherein certain other embodiments of the disclosure are directed to methods and compositions for restoring prototrophy in auxotrophic B. licheniformis cells, and expressing genes of interest (GOIs) in such restored prototrophy B. licheniformis cells.

COMPOSITIONS AND METHODS FOR ADOPTIVE CELL THERAPY

Provided herein are compositions and methods for adoptive cell therapy comprising engineered immune cells that express an antigen-targeted chimeric antigen receptor and a prodrug converting enzyme for the treatment of inflammation, inflammatory diseases, or pathogenic infections.

METHOD FOR CONVERTING NON-ETHANOL PRODUCING, ACETOGENIC STRAIN TO ETHANOL-PRODUCING STRAIN AND METHOD FOR PRODUCING ETHANOL FROM SAME ETHANOL-PRODUCING STRAIN BY USING CARBON MONOXIDE

The present invention relates to a transformed strain having ethanol production potential, constructed by introducing a foreign gene for ethanol production into a non-ethanol producing acetogen Eubacterium limosum and a method for producing ethanol, using the strain. According to the present invention, Eubacterium limosum which is a conventional acetogen lacking ethanol production potential is used to produce ethanol, which is a high value-added product, as a single product from carbon monoxide contained in waste gas.

Anaerobic Cell-Free Systems and Environments and Methods for Making and Using Same

The present disclosure relates to cell-free compositions and methods for making and using the same. In one aspect, the composition includes: an extract derived from one or more organisms; one or more proteins of interest, wherein the one or more proteins are expressed from one or more nucleic acids exogenous to the extract and/or by the one or more organisms, wherein preferably the one or more proteins react with a substrate to produce a product; and one or more O2, O—, or H.sub.2O.sub.2 scavengers. The composition may be oxygen-deprived. The composition may also include an energy recycling system.

Engineering of multi-carbon substrate utilization pathways in methanotrophic bacteria

The present disclosure relates to genetically engineered methanotrophic bacteria with the capability of growing on a multi-carbon substrate as a primary or sole carbon source and methods for growing methanotrophic bacteria on a multi-carbon substrate.

MUTANT GLUCOSE OXIDASE (GOD) HAVING IMPROVED THERMAL STABILITY AND GENE AND APPLICATION THEREOF

The present invention relates to the field of genetic engineering, particularly to a glucose oxidase mutant having improved thermal stability, gene and application thereof. The present invention provides several glucose oxidase GOD mutants with high catalytic efficiency and improved thermal stability, which breaks the barrier of low enzyme activity and poor stability and is suited well to meet the requirements of application to the fields of food, medicine, feed and textile industry, and has a very broad application prospect.

ENASIDENIB GLYCOSIDES AND METHODS OF TREATING DISEASES ASSOCIATED WITH ISOCITRATE DEHYDROGENASE (IDH) DYSFUNCTION

Enasidenib glycosides and methods of making enasidenib glycosides are disclosed. Glycosyl transferases catalyze addition of one or more monosaccharides to enasidenib to yield enasidenib glycosides. Suitable monosaccharides can be in the L- or D-configuration and typically have 5, 6, or 7 carbons. Suitable monosaccharides include allose, apiose, arabinose, fructose, fucitol, fucose, galactose, galacturonate, glucose, glucuronic acid, mannose, N-acetylglucosamine, rhamnose, or xylose. Uridine diphosphate glycosyl transferases can catalyze formation of either an alpha or beta glycosidic bond.