The present invention relates to a secretagogue compound derived from oxalate degrading bacteria, for use in the treatment of an oxalate related disease and/or oxalate related imbalance in a subject, wherein the administration of the secretagogue results in a reduction of urinary oxalate and/or plasma oxalate in the subject. The invention further relates to a pharmaceutical composition comprising such a secretagogue compound, a method for treating a subject suffering from an oxalate related disease, and to a method for preparing a secretagogue.

Disclosed is an NADH-dependent amino acid dehydrogenase and an application thereof in increasing lysine yield. The amino acid dehydrogenases are aspartate dehydrogenase derived from Pseudomonas aeruginos, aspartate semialdehyde dehydrogenase derived from Tistrella mobilis, dihydropyridine dicarboxylic acid reductase derived from Mycobacterium tuberculosis, and diaminopimelate dehydrogenase derived from Tepidanaerobacter acetatoxydans. The amino acid sequences thereof are as shown in SEQ ID NOs: 1, 3, 5, and 7, respectively. NADH or both NADH and NADPH can be used as co-factors of the amino acid dehydrogenase to synthesize lysine, thereby reducing the demand for NADPH in the cell, and significantly increasing the production of lysine or pentanediamine.

The present invention provides a glufosinate-ammonium dehydrogenase mutant and application in synthesis of L-glufosinate-ammonium thereof, the method uses 2-carbonyl-4-[(hydroxy)(methyl)phosphinoyl]-butyric acid or its salts as a substrate and the glufosinate-ammonium dehydrogenase or cells containing the glufosinate-ammonium dehydrogenase as a biocatalyst to carry out reductive amination, thereby obtaining L-glufosinate-ammonium. The method has features of high conversion rate of raw materials, high yield, easy separation and purification of the product, and high chiral purity; compared with other catalytic processes, the method in the present invention has features of relatively simple process and a conversion rate of raw materials up to 100%.

The present disclosure provides compositions and methods for rapid production of chemicals in genetically engineered microorganisms in a large scale. Also provided herein is a high-throughput metabolic engineering platform enabling the rapid optimization of microbial production strains. The platform, which bridges a gap between current in vivo and in vitro bio-production approaches, relies on dynamic minimization of the active metabolic network.

The present disclosure provides compositions and methods for rapid production of chemicals in genetically engineered microorganisms in a large scale. Also provided herein is a high-throughput metabolic engineering platform enabling the rapid optimization of microbial production strains. The platform, which bridges a gap between current in vivo and in vitro bio-production approaches, relies on dynamic minimization of the active metabolic network.

Disclosed herein are genetically engineered hematopoietic cells, which express one or more Krebs cycle modulating polypeptides, and optionally a chimeric receptor polypeptide (e.g., an antibody-coupled T cell receptor (ACTR) polypeptide or a chimeric antigen receptor (CAR) polypeptide) capable of binding to a target antigen of interest. Also disclosed herein are uses of the engineered hematopoietic cells for inhibiting cells expressing a target antigen in a subject in need thereof.

The present disclosure belongs to the technical field of biocatalysis and biotransformation, and particularly relates to whole-cell biocatalysis method for producing α, ω-dicarboxylic acids and use thereof. The biosynthetic pathway designed in the present disclosure is divided into three modules to co-express several different enzymes in host cells respectively, and then the whole-cells are used to catalyze the production of α, ω-dicarboxylic acid from cycloalkanes, cycloalkanol and lactones in a cascade reaction. Compared with the chemical method, this process does not produce any harmful gases during the production process, does not require high temperature, high pressure, and complex metal catalysts, and is a green and environmental protection production method.

Provided is an amino acid dehydrogenase mutant. The amino acid sequence of the mutant is obtained by mutating the amino acid sequence shown in SEQ ID NO:1. The mutation includes at least one of the following mutation sites: 64th, 94th, 133rd, 137th, 148th, 168th, 173rd, 183 rd, 191st, 207th, 229th, 248th, 255th and 282nd sites; or the amino acid sequence of the amino acid dehydrogenase mutant is an amino acid sequence having the mutation sites in the mutated amino acid sequence and having a 80% or more homology with the mutated amino acid sequence. The mutant enzyme activity is more than 50 times higher than that of wild amino acid dehydrogenase, and the enzyme specificity is also correspondingly improved.

The invention provides methods for improving efficiency of fermentation by arginine supplementation, and genetically modified bacterium for use therefor. More particularly the invention provides methods for (i) increasing the production ATP intensive products with arginine supplementation, (ii) increasing utilization of arginine by a C1-fixing bacterium; and (iii) providing C1-fixing bacterium with optimized arginine de-aminase pathways.

An enzyme having the following characteristics (a) and (b): (a) the enzyme has an activity of reversible dehydrogenation of D-amino acids; (b) the enzyme is a hexamer of polypeptides having an amino acid sequence having 80% or greater identity to the amino acid sequence of SEQ ID NO: 2.