A technique relating to a method for enzymatically producing maytansinol from an ansamitocin species, such as AP3, is provided. The method for producing maytansinol includes enzymatically producing maytansinol from an ansamitocin species with any one of various proteins.

A recombinant microorganism includes a transgene encoding a polypeptide of a Type II biotin synthase, wherein a holo-protein of the Type II biotin synthase comprises per polypeptide chain a first [4Fe—4S] cluster (radical SAM (RS) cluster) coordinated to a CxxxCxxC motif in the polypeptide chain and a second [4Fe—4S] cluster. The Type II biotin synthase contains a serine to cysteine swap in its holo-protein amino acid sequence, that is the amino acid at the position corresponding to Ser-43 in the E. coli K12 Type I biotin synthase holo-protein is a Cysteine and the amino acid corresponding to Cys-97 in the E. coli K12 Type I biotin synthase holo-protein is a Serine. A method for producing biotin includes cultivating the recombinant microorganism in a growth medium to produce a culture; and recovering biotin from the culture.

Polynucleotides and polypeptides useful in the manufacture of a class of chemical compounds known as alkaloids are provided. The polynucleotides and polypeptides may be used to synthesize alkaloids, including reticuline, thebaine and morphine, in vivo and in vitro. The polynucleotides further may be used to examine the presence of the polynucleotides in a cell or a cell extract, and to modulate expression thereof in living cells.

Polynucleotides and polypeptides useful in the manufacture of a class of chemical compounds known as alkaloids are provided. The polynucleotides and polypeptides may be used to synthesize alkaloids, including reticuline, thebaine and morphine, in vivo and in vitro. The polynucleotides further may be used to examine the presence of the polynucleotides in a cell or a cell extract, and to modulate expression thereof in living cells.

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

The present invention discloses processes for obtaining a color from an algal biomass. The process includes subjecting an algal biomass to cavitation, thus at least partially disrupting cells of the algal biomass and extracting color from the disrupted, algal biomass.

A method of demethylizing an opioid to a nor-opioid is provided. The method comprises contacting an opioid with at least one enzyme. Contacting the opioid with the at least one enzyme converts the opioid to a nor-opioid. A method of converting a nor-opioid to a nal-opioid is provided. The method comprises contacting a nor-opioid with at least one enzyme. Contacting the nor-opioid with the at least one enzyme converts the nor-opioid to a nal-opioid.

A method of demethylizing an opioid to a nor-opioid is provided. The method comprises contacting an opioid with at least one enzyme. Contacting the opioid with the at least one enzyme converts the opioid to a nor-opioid. A method of converting a nor-opioid to a nal-opioid is provided. The method comprises contacting a nor-opioid with at least one enzyme. Contacting the nor-opioid with the at least one enzyme converts the nor-opioid to a nal-opioid.

An isolated or engineered polypeptide, a microorganism comprising a nucleic acid sequence encoded by the polypeptide, and a method for synthesizing a polyphenolic phytochemicals phosphate derivative using the polypeptide or the microorganism are provided. The polypeptide having a homologous protein sequence that is more than 70% identical to the polyphenol phosphorylation synthetase (SEQ ID NO: 13) comprises a conserved domain which sequentially comprises: an ATP-binding domain, which includes active catalytic sites of Lys27, Arg102, and Glu282; a substrate-binding domain, which includes a conserved motif of DDHHFYIDAMLDAKAR (SEQ ID NO: 14), and includes active catalytic sites ofAsp627, His629, and His630; and a phosphorylated histidine catalytic domain, which includes His795 based on SEQ ID NO: 13.