An object of the invention is to provide a peptide having a stabilized secondary structure. The present invention provides a peptide having a secondary structure stabilized by a crosslinked structure and containing at least one combination of a special amino acid of the formula (I): ##STR00001##
(wherein, (A) represents a single bond or a linking group having, in the main chain thereof, from 1 to 10 atoms;
(B) represents a group containing at least one bond;
(C) represents a hydrogen atom or an alkyl group which may be substituted with a substituent; and X represents a group substitutable by a substitution reaction with a sulfanyl group) and an amino acid having, in the side chain thereof, a sulfanyl group; and having the crosslinked structure formed through a thioether bond between the side chain of the special amino acid residue and the sulfanyl group.

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 application describes methods, including non-naturally occurring methods, for biosynthesizing 3-hydroxy-3-methylglutaryl-coA and intermediates thereof, as well as non-naturally occurring hosts for producing 3-hydroxy-3-methylglutaryl-coA. This application also describes methods, including non-naturally occurring methods, for biosynthesizing isoprene and intermediates thereof, as well as non-naturally occurring hosts for producing isoprene.

This application describes methods, including non-naturally occurring methods, for biosynthesizing 3-hydroxy-3-methylglutaryl-coA and intermediates thereof, as well as non-naturally occurring hosts for producing 3-hydroxy-3-methylglutaryl-coA. This application also describes methods, including non-naturally occurring methods, for biosynthesizing isoprene and intermediates thereof, as well as non-naturally occurring hosts for producing isoprene.

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 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 specification discloses a kit and a method that can mildly generate a lachrymatory factor. The present disclosure relates to a lachrymatory factor generating kit 1 comprising (1) a dry PRENCSO composition 2 comprising PRENCSO and a porous carrier carrying it and being dried, and (2) a dry enzyme composition 3 comprising alliinase, a lachrymatory factor synthase (LFS) and a porous carrier carrying them and being dried. The present disclosure also relates to a method for generating a lachrymatory factor, the method comprising contacting water with the dry PRENCSO composition 2 and the dry enzyme composition 3.

The present specification discloses a kit and a method that can mildly generate a lachrymatory factor. The present disclosure relates to a lachrymatory factor generating kit 1 comprising (1) a dry PRENCSO composition 2 comprising PRENCSO and a porous carrier carrying it and being dried, and (2) a dry enzyme composition 3 comprising alliinase, a lachrymatory factor synthase (LFS) and a porous carrier carrying them and being dried. The present disclosure also relates to a method for generating a lachrymatory factor, the method comprising contacting water with the dry PRENCSO composition 2 and the dry enzyme composition 3.

Provided herein are genetically modified yeast cells that recombinantly expresses a gene encoding a mutant beta-lyase. Also provided are methods of producing fermented products and methods of producing ethanol.