The disclosure relates to recombinant microorganisms for the production of fatty amines and derivatives thereof. Further contemplated are cultured recombinant host cells as well as methods of producing fatty amines by employing these host cells.

A method for asymmetrically preparing L-phosphinothricin by oxidation-reduction reaction through biological multienzyme coupling, where D,L-phosphinothricin as a raw material is catalyzed by an enzyme catalysis system to obtain L-phosphinothricin, wherein the enzyme catalysis system comprises a D-amino acid oxidase mutant for catalyzing D-phosphinothricin in D,L-phosphinothricin into 2-carbonyl-4-[hydroxy(methyl)phosphono]butyric acid and a transaminase for catalytic reduction of the 2-carbonyl-4-[hydroxy(methyl) phosphono]butyric acid into L-phosphinothricin; the D-amino acid oxidase mutant is obtained by mutation of D-amino acid oxidase in wild strain Rhodotorula taiwanensis at one of the following four sites: (1) M213S; (2) M213S-N54V-F58E; (3) M213S-N54V-F58E-D207A; (4) M213S-N54V-F58E-D207A-S60T. According to the present invention, the D-amino acid oxidase mutant provides better catalytic efficiency, and when racemic D,L-phosphinothricin is used as a substrate for catalytic reaction, the conversion rate is much higher than that of the wild type enzyme, and the PPO yield is also greatly improved.

Microorganisms are genetically engineered to produce 3-hydroxypropionate (3-HP). The microorganisms are carboxydotrophic acetogens. The microorganisms produce acetyl-coA using the Wood-Ljungdahl pathway for fixing CO/CO.sub.2. A β-alanine pyruvate aminotransferase from a microorganism that contains such an enzyme is introduced. Additionally, an acetyl-coA carboxylase may also be introduced. The production of 3-HP can be improved. This can be effected by improved promoters or higher copy number or enzymes that are catalytically more efficient.

Methods for the production of L-glufosinate (also known as phosphinothricin or (S)-2 -amino-4-(hydroxy(methyl)phosphonoyl)butanoic acid) are provided. The methods comprise a two-step process. The first step involves the oxidative deamination of D-glufosinate to PPO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid). The second step involves the specific amination of PPO to L-glufosinate, using an amine group from one or more amine donors. By combining these two reactions, the proportion of L-glufosinate in a mixture of L-glufosinate and D-glufosinate can be substantially increased.

The present application discloses genetically modified yeast cells comprising an active 3-HP fermentation pathway, and the use of these cells to produce 3-HP.

The present application discloses genetically modified yeast cells comprising an active 3-HP fermentation pathway, and the use of these cells to produce 3-HP.

The present disclosure describes the engineering of microbial cells for fermentative production of histamine and provides novel engineered microbial cells and cultures, as well as related histamine production methods.

The disclosure relates to recombinant microorganisms for the production of fatty amines and derivatives thereof. Further contemplated are cultured recombinant host cells as well as methods of producing fatty amines by employing these host cells.

Compositions and methods for the production of L-glufosinate are provided. The method involves converting racemic glufosinate to the L-glufosinate enantiomer or converting PPO to L-glufosinate in an efficient manner. In particular, the method involves the specific amination of PPO to L-glufosinate, using L-glutamate, racemic glutamate, or another amine source as an amine donor. PPO can be obtained by the oxidative deamination of D-glufosinate to PRO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid) or generated via chemical synthesis. PPO is then converted to L-glufosinate using a transaminase in the presence of an amine donor. When the amine donor donates an amine to PPO, L-glufosinate and a reaction by product are formed. Because the PPO remaining represents a yield loss of L-glufosinate, it is desirable to minimize the amount of PPO remaining in the reaction mixture. Degradation, other chemical modification, extraction, sequestration, binding, or other methods to reduce the effective concentration of the by-product, i.e., the corresponding alpha ketoacid or ketone to the chosen amine donor will shift the reaction equilibrium toward L-glufosinate, thereby reducing the amount of PPO and increasing the yield of L-glufosinate. Therefore, the methods described herein involve the conversion or elimination of the alpha ketoacid or ketone by-product to another product to shift the equilibrium towards L-glufosinate.

The disclosure relates to recombinant microorganisms for the production of fatty amines and derivatives thereof. Further contemplated are cultured recombinant host cells as well as methods of producing fatty amines by employing these host cells.