The present invention relates to non-naturally occurring polypeptides useful for preparing armodafinil, polynucleotides encoding the polypeptides, and methods of using the polypeptides. The non-naturally occurring polypeptides of the present invention are effective in carrying out biocatalytic conversion of the (i) 2-(benzhydrylsulfinyl)acetamide to (−)-2-[(R)-(diphenylmethyl)sulfinyl]acetamide (armodafinil), or (ii) benzhydryl-thioacetic acid to (R)-2-(benzhydrylsulfinyl)acetic acid, which is a pivotal intermediate in the synthesis of armodafinil, in enantiomeric excess.

The present invention generally relates to the field of biotechnology as it applies to the production of aryl sulfates using recombinant host cells. More particularly, the present invention pertains to recombinant host cells comprising (e.g., expressing) a polypeptide having aryl sulfotransferase activity, wherein said recombinant host cells have been modified to have an increased uptake of sulfate compared to identical host cells that does not carry said modification. Further provided are processes for the production of aryl sulfates, such as zosteric acid, employing such recombinant host cells.

The present invention generally relates to the field of biotechnology as it applies to the production of aryl sulfates using recombinant host cells. More particularly, the present invention pertains to recombinant host cells comprising (e.g., expressing) a polypeptide having aryl sulfotransferase activity, wherein said recombinant host cells have been modified to have an increased uptake of sulfate compared to identical host cells that does not carry said modification. Further provided are processes for the production of aryl sulfates, such as zosteric acid, employing such recombinant host cells.

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a β-ketoacyl synthase or a β-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a β-ketoacyl synthase or a β-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

A strain of Burkholderia is Burkholderia glathei ECU0712, with an accession number of CGMCC NO. 14464. With the strain or its extract as the biocatalyst, thioether is catalyzed to be oxidized asymmetrically to chiral sulfoxide, with significant advantages that the obtained product has a high optical purity, and benefits of a simple reaction system, short preparation time of the catalyst and a high yield of the product.

A method for enzymatic sulfurylation of a substrate is provided which includes the steps of reacting the substrate with 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in a medium containing a bacterium belonging to the family Enterobacteriaceae to produce a sulfated derivative of the substrate, and collecting the sulfated derivative from the medium, wherein the bacterium has been modified to produce, at least, a protein having sulfotransferase activity, and to attenuate expression of an aphA gene, a cysQ gene, or a cpdB gene, or a combination of these.

The present disclosure relates to synthesis of enantiomerically rich key drug intermediates as a means for manufacturing of thiocarbamate derivatives as A2A adenosine receptor (A2AR) inhibitors. More particularly, the present disclosure provides a viable efficient technology using enzymatic biotransformation process which utilizes cheaper substrate for production of high value key intermediates for A2AR inhibitors.

A process for the enzymatic oxidation of sulfinic acids includes sulfinic acids of formula H.sub.2NCH(R)CH.sub.2SO.sub.2H to sulfonic acids of formula H.sub.2NCH(R)CH.sub.2SO.sub.3H and an enzyme selected from the class of H.sub.2O.sub.2-generating oxidases in the presence of the substrate of said enzyme.

The present invention relates to non-naturally occurring polypeptides useful for preparing armodafinil, polynucleotides encoding the polypeptides, and methods of using the polypeptides. The non-naturally occurring polypeptides of the present invention are effective in carrying out biocatalytic conversion of the (i) 2-(benzhydrylsulfinyl)acetamide to ()-2-[(R)-(diphenylmethyl)sulfinyl]acetamide (armodafinil), or (ii) benzhydryl-thioacetic acid to (R)-2-(benzhydrylsulfinyl)acetic acid, which is a pivotal intermediate in the synthesis of armodafinil, in enantiomeric excess.