Genetically programmed microorganisms, such as bacteria, pharmaceutical compositions thereof, and methods of modulating and treating a disease and/or disorder are disclosed.

The present invention is directed to cyclopropylamine derivatives which are LSD1 inhibitors useful in the treatment of diseases such as cancer.

The invention provides a genetically modified bacterium for production of thiamine; where the bacterium is characterized by a transgene encoding a thiamine monophosphate phosphatase (TMP phosphatase having EC 3.1.3.-) as well as transgenes encoding polypeptides that catalyze steps in the thiamine pathway. The genetically modified bacterium is characterized by enhanced synthesis and release of thiamine into the extracellular environment. The invention further provides a method for producing thiamine using the genetically modified bacterium of the invention; as well as the use of the genetically modified bacterium for extracellular thiamine production.

The present invention relates to autotrophic microorganisms with altered photorespiration and improved CO.sub.2 fixation as well as a method of producing said autotrophic microorganisms. Particularly, the autotrophic microorganisms show an improved growth rate, productivity and energy conversion efficiency.

The present invention relates to a method of providing thermal and/or acoustic insulation to a structure, comprising the steps of: providing a substrate which comprises fibres; applying the substrate to the structure; blending the substrate with a binder composition before, during or after application of the substrate to the structure; allowing curing of the binder composition after the substrate and the binder composition have been applied to the structure; wherein the binder composition comprises at least one hydrocolloid. The present invention also relates to an insulated structure obtainable by said method.

The present invention provides recombinant Escherichia coli for producing glutarate, a construction method and use thereof. A double-plasmid recombinant bacterium is constructed through molecular biological means for co-expressing an aldehyde synthase (AAS) gene, an amine oxidase Mao (gene) and an aldehyde dehydrogenase (Glox) gene. The constructed expression plasmids are introduced into the Escherichia coli to reconstruct to obtain recombinant cells. A recombination strain for efficiently producing glutarate is obtained through amicillin resistance and kanamycin resistance combined plate screening. Efficient production of the glutarate is achieved by optimizing concentration of a substrate, cell concentration and a transformation temperature. L-lysine with a concentration of 30 g/L may be transformed into 19.65 g of glutarate through reactions for 30 h under transformation conditions that the cell concentration is 30 g/L, the pH value is 8 and 6 mM of NAD.sup.+ is additionally added, wherein a transformation rate may be 65.3%.

The present disclosure discloses a production method of Danshensu, belonging to the technical field of bioengineering. The present disclosure constructs a novel genetic engineering strain co-expressed by three enzymes, which can be applied to the production of optically pure 3-(3,4-dihydroxyphenyl)-2-hydroxypropionic acid. All of the (D/L)--hydroxycarboxylic acid dehydrogenase selected by the present disclosure have the characteristics of poor substrate specificity and strong optical specificity, and can produce optically pure D-danshensu and L-danshensu. Further, the production efficiency of the recombinant strain is improved by knocking out or enhancing the expression of a related gene on the E. coli genome to promote substrate transport and reduce product decomposition. The method for producing Danshensu and -ketoglutaric acid by using the transformation of the recombinant strain according to the present disclosure is simple, has easily available raw materials, few impurities, and has good industrial application prospects.

Provided are methods and compositions for activating oligonucleotide aptamer-deactivated DNA polymerases, comprising cleaving the aptamer by endonuclease V enzymatic activity to reduce or eliminate binding of the oligonucleotide aptamer to the DNA polymerase, thereby activating DNA synthesis activity of the DNA polymerase in a reaction mixture. Mixtures for use in methods of the invention are also provided. The oligonucleotide aptamers of the present invention are circular and comprise one or more deoxyinosine nucleotides providing for aptamer-specific recognition and cleavage of the circular aptamer by the endonuclease V enzymatic activity. Exemplary oligonucleotide aptamers, mixtures and methods employing endonuclease V enzymatic activity are provided. The methods can be practiced using kits comprising a DNA polymerase-binding oligonucleotide aptamer and at least one endonuclease V enzymatic activity having oligonucleotide aptamer-specific recognition to provide for specific cleavage of the aptamer by the endonuclease V enzymatic activity.

A method is provided for measuring glycated hemoglobin in a hemoglobin-containing sample which comprises reacting glycated hemoglobin in the hemoglobin-containing sample with an enzyme that catalyzes a reaction of oxidizing the glycated hemoglobin to generate hydrogen peroxide, in the presence of at least one anionic surfactant selected from the group consisting of N-acyl taurine in which a hydrogen atom of the amino group may be substituted with a substituent, alkyl sulfoacetic acid, polyoxyethylene alkyl ether acetic acid, N-acyl amino acid in which a hydrogen atom of the amino group may be substituted with a substituent, polyoxyethylene alkyl ether phosphoric acid, polyoxyethylene polycyclic phenyl ether phosphoric acid, alkyl phosphoric acid, and salts thereof, to generate hydrogen peroxide, and measuring the generated hydrogen peroxide.

The present invention relates to a kit for quantitative analysis of glycated hemoglobin (HbA1c), and the kit for quantitative analysis of HbA1c according to the present invention has excellent long-term stability of an enzyme reagent and thus has an effect of easily overcoming the disadvantages of the conventional reagents used in enzyme assays (e.g., storage, accuracy, portability, convenience of use, etc.).