Isolated oxidases, isolated polynucleotides encoding the oxidases, and methods of using the oxidases to produce -oxocarboxylic acid compounds or L--amino acid compounds are described.

The present disclosure provides recombinant bacteria with elevated production of ethanol and/or n-butanol from ethylene. Methods for the production of the recombinant bacteria, as well as for use thereof for production of ethanol and/or n-butanol are also provided.

The disclosure provides polypeptides and encoding nucleic acids of engineered formate dehydrogenases. The disclosure also provides cells expressing an engineered formate dehydrogenase. The disclosure further provides methods for producing a bioderived compound comprising culturing cells expressing an engineered formate dehydrogenase. Where the engineered formate dehydrogenase is capable of catalyzing a conversion.

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals.

The present invention relates to an FeS fusion protein acting as an electron transport chain, a novel carbon monoxide:formate oxidoreductase (CFOR) including the FeS fusion protein, novel Thermococcus strain BCF12 transformed with CFOR, and the use thereof. According to the present invention, two different enzymes may be physically linked directly to each other through the FeS fusion protein of the present invention, and thus electrons generated from any one enzyme may be transported directly to another enzyme through the FeS cluster of the FeS fusion protein. Accordingly, a reaction that produces a target substance with high efficiency by directly supplying electrons necessary for the production of the target substance is possible without leakage of electrons generated in any one enzyme. In addition, the present invention has an advantage in that the overall enzyme reaction rate and yield can be dramatically improved using a new electron transport reaction. Furthermore, it is possible to ensure the stability of each enzyme by allowing the enzymes to exist in a physically fixed state in cells.

The present invention relates to enzymatic reactor cells and related methods of use, e.g., to produce formic acid and/or formate by using an enzymatic reactor cell, wherein the enzymatic reactor cell includes a surface, a linker, and one or more enzymes.

The present invention discloses a method for preparing L-glufosinate ammonium by biological enzymatic de-racemization, a glufosinate ammonium dehydrogenase mutant and a use thereof. The method for preparing L-glufosinate ammonium by biological enzymatic de-racemization includes catalyzing D,L-glufosinate ammonium as a raw material by a multi-enzyme catalysis system to obtain L-glufosinate ammonium. The enzyme catalysis system includes D-amino acid oxidase for catalyzing D-glufosinate ammonium in the D,L-glufosinate ammonium to 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid, and a glufosinate ammonium dehydrogenase mutant for catalytically reducing 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid to L-glufosinate ammonium. The glufosinate ammonium dehydrogenase mutant is obtained by mutation of glufosinate-ammonium dehydrogenase in wild fungi Thiopseudomonas denitrificans at a mutation site of V377S. The glufosinate ammonium dehydrogenase mutant in the present invention has better catalytic efficiency. When racemic D, L-glufosinate ammonium is used as a substrate for a catalytic reaction, the conversion rate is much higher than the conversion rate of a wild-type enzyme, and the yield of 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid (PPO for short) is also greatly improved.

The present invention provides a method for efficiently producing L-homophenylalanine and a strain producing L-homophenylalanine. In the present invention, a new route for the synthesis of L-homophenylalanine by a cascade enzymatic method using cheap benzaldehyde and pyruvic acid as raw materials is designed. By constructing the pathway-related enzymes into the same E. coli strain, a recombinant E. coli is obtained, with which L-homophenylalanine is catalytically produced through reaction in a 5 L reactor, with a yield of 100.9 g/L, a conversion rate of 94%, and ee>99%. Compared with the existing main methods for producing L-HPA, the production cost of L-homophenylalanine is greatly reduced. Thus, the present invention has good application prospects.

The present invention relates to a genetically engineered microorganism expressing (i) formate tetrahydrofolate (THF) ligase, methenyi-THF cyclohydrolase and methylene-THF dehydrogenase, (ii) the enzymes of the glycine cleavage system (GCS), (iii) serine deaminase and serine hydroxymethyltransferase (SHMT), (iv) an enzyme increasing the availability of NADPH, and (v) optionally formate dehydrogenase (FDH), and wherein the genetically engineered microorganism has been genetically engineered to express at least one of the enzymes of (i) to (v), wheren said enzyme is not expressed by the corresponding microorganism that has been used to prepare the genetically engineered microorganism, and wherein the enzymes of (i) to (v) are genomically expressed.