Disclosed in the present invention is an L-glutamate dehydrogenase mutant, the sequence of the L-glutamate dehydrogenase mutant being a sequence in which amino acid residue A at position 175 in SEQ ID NO: 1 is mutated to be G, and amino acid residue V at position 386 is mutated to be an amino acid residue having less steric hindrance. Further disclosed in the present invention is an application of the described L-amino acid dehydrogenase mutant in the preparation of L-glufosinate-ammonium or a salt thereof. When the L-glutamate dehydrogenase mutant of the present invention is used to prepare L-glufosinate-ammonium or a salt thereof, compared to an L-glutamate dehydrogenase mutant in which only position 175 or 386 is mutated, the specific enzyme activity is higher. Therefore, the action efficiency of the enzyme is improved, reaction costs are reduced, and industrial production is facilitated.

A recombinant microorganism including a genetic modification that increases expression of a gene encoding a ferric enterobactin transporter-associated protein or a gene encoding a TonB-dependent transporter-associated protein, or a genetic modification that decreases expression of a fur gene encoding a ferric uptake regulator (Fur) protein, wherein the recombinant microorganism removes greater amounts of nitric oxide from a sample comprising nitric oxide than a same microorganism without the genetic modification

The present disclosure provides recombinant bacteria for production of indole-3-acetic acid (IAA). Pharmaceutical compositions and methods of treating diseases are also included.

The present application provides engineered polypeptides having imine reductase activity, polynucleotides encoding the engineered imine reductases, host cells capable of expressing the engineered imine reductases, and methods of using these engineered polypeptides with a range of ketone and amine substrate compounds to prepare secondary and tertiary amine product compounds.

A process comprising (i) providing a gaseous stream including greater than 1% by volume carbon dioxide; (ii) providing water; (iii) converting the carbon dioxide and the water to an organic intermediate and oxygen gas in the presence of light; (iv) separating the oxygen gas from the organic intermediate; and (v) converting the organic intermediate to ethylene and carbon dioxide after said step of separating the oxygen gas from the organic intermediate.

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.).

Provided herein are CasX:gNA systems comprising CasX polypeptides, guide nucleic acids (gNA), and optionally donor template nucleic acids useful in the modification of a SOD1 gene. The systems are also useful for introduction into cells, for example eukaryotic cells having mutations in the SOD1 protein or the SOD1 regulatory element. Also provided are methods of using such CasX:gNA systems to modify cells having such mutations and utility in methods of treatment of a subject with a SOD1-related disease.

Provided are modified tobacco plants having reduced nitrate levels and tobacco products generated from the modified tobacco plants having reduced tobacco specific nitrosamines (TSNAs). Also provided are methods of reducing TSNAs in tobacco products by altering the gene expression of the nitrate assimilation pathway

The present disclosure provides a polyethylene glycol-modified urate oxidase. At least 11 of the following amino acid sites in the urate oxidase have a PEG modification: T.sup.1, K.sup.3, K.sup.4, K.sup.30, K.sup.35, K.sup.76, K.sup.79, K.sup.97, K.sup.112, K.sup.116, K.sup.120, K.sup.152, K.sup.179, K.sup.222, K.sup.231, K.sup.266, K.sup.272, K.sup.285, K.sup.291, and K.sup.293.

The disclosure includes non-naturally occurring or engineered CRISPR Cas9, each associated with at least one destabilization domain (DD), along with compositions, systems and complexes involving the DD-CRISPR Cas9, nucleic acid molecules and vectors encoding the same, delivery systems involving the same, uses therefor.