Provided is an enzyme useful for prenylation and recombinant pathways for the production of cannabinoids, cannabinoid precursors and other prenylated chemicals in a cell free system as well and recombinant microorganisms that catalyze the reactions.

This invention provides recombinant cells and methods for producing terpenes and terpenoids by increasing production or accumulation or both of isoprenoid precursors thereof.

This invention provides recombinant cells and methods for producing terpenes and terpenoids by increasing production or accumulation or both of isoprenoid precursors thereof.

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.

The invention provides non-naturally occurring microbial organisms having a toluene, benzene, p-toluate, terephthalate, (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate, (2-hydroxy-4-oxobutoxy)phosphonate, benzoate, styrene, 2,4-pentadienoate, 3-butene-1ol or 1,3-butadiene pathway. The invention additionally provides methods of using such organisms to produce toluene, benzene, p-toluate, terephthalate, (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate, (2-hydroxy-4-oxobutoxy)phosphonate, benzoate, styrene, 2,4-pentadienoate, 3-butene-1ol or 1,3-butadiene.

The invention provides non-naturally occurring microbial organisms having a toluene, benzene, p-toluate, terephthalate, (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate, (2-hydroxy-4-oxobutoxy)phosphonate, benzoate, styrene, 2,4-pentadienoate, 3-butene-1ol or 1,3-butadiene pathway. The invention additionally provides methods of using such organisms to produce toluene, benzene, p-toluate, terephthalate, (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate, (2-hydroxy-4-oxobutoxy)phosphonate, benzoate, styrene, 2,4-pentadienoate, 3-butene-1ol or 1,3-butadiene.

The present invention relates to enzymes capable of hydrolysing organophosphate (OP) molecules. In particular, the invention relates to variants of the OpdA enzyme from Agrobacterium that display improved activity when compared to the naturally occurring OpdA. The invention is also towards polypeptides that have organophosphate hydrolysing activity for the organophosphates chlorpyrifos methyl, diazinon and parathion ethyl.

The present invention relates to enzymes capable of hydrolysing organophosphate (OP) molecules. In particular, the invention relates to variants of the OpdA enzyme from Agrobacterium that display improved activity when compared to the naturally occurring OpdA. The invention is also towards polypeptides that have organophosphate hydrolysing activity for the organophosphates chlorpyrifos methyl, diazinon and parathion ethyl.

Provided is a D-amino acid oxidative enzyme mutant. The sequence of the mutant comprises a sequence by mutating the 54.sup.th amino acid residue N, the 58.sup.th amino acid residue F, the 211.sup.th amino acid residue C, and the 213.sup.th amino acid residue M of the sequence shown in SEQ ID NO:1 or the sequence having at least 76% identity with SEQ ID NO:1. The D-amino acid oxidative enzyme mutant has a higher enzyme activity, enzyme activity stability and/or ammonium resistance than a mild D-amino acid oxidative enzyme mutant. Also provided is an application of the D-amino acid oxidative enzyme mutant in preparing 2-oxo-4-(hydroxymethylphosphinyl)butyric acid.

Provided is a D-amino acid oxidative enzyme mutant. The sequence of the mutant comprises a sequence by mutating the 54.sup.th amino acid residue N, the 58.sup.th amino acid residue F, the 211.sup.th amino acid residue C, and the 213.sup.th amino acid residue M of the sequence shown in SEQ ID NO:1 or the sequence having at least 76% identity with SEQ ID NO:1. The D-amino acid oxidative enzyme mutant has a higher enzyme activity, enzyme activity stability and/or ammonium resistance than a mild D-amino acid oxidative enzyme mutant. Also provided is an application of the D-amino acid oxidative enzyme mutant in preparing 2-oxo-4-(hydroxymethylphosphinyl)butyric acid.