The present disclosure provides methods for making glycosylated cannabinoids including methods using recombinant host cells comprising a pathway capable of producing a cannabinoid and a heterologous nucleic acid that encodes a UDP-glycosyl transferase. The disclosure also provides compositions of recombinant host cells capable of producing glycosylated cannabinoids, and compositions and uses of the glycosylated cannabinoids.

The present disclosure provides methods for making glycosylated cannabinoids including methods using recombinant host cells comprising a pathway capable of producing a cannabinoid and a heterologous nucleic acid that encodes a UDP-glycosyl transferase. The disclosure also provides compositions of recombinant host cells capable of producing glycosylated cannabinoids, and compositions and uses of the glycosylated cannabinoids.

Provided herein are genetically modified host cells, compositions, and methods for improved production of vanillin and/or glucovanillin. The host cells, compositions, and methods described herein provide an efficient route for the heterologous production of vanillin and/or glucovanillin and any compound that can be synthesized or biosynthesized from either or both.

The present disclosure provides engineered bacteria for producing vanillin.

The present invention relates generally to the use of novel UDP-glucosyltransferases enzymes having specific activity towards cannabinoid compounds. The present invention further relates generally to the use of novel UGT enzymes having specific activity towards cannabinoid compounds to generate water-soluble cannabinoid glycoside compounds.

The present invention relates generally to the use of novel UDP-glucosyltransferases enzymes having specific activity towards cannabinoid compounds. The present invention further relates generally to the use of novel UGT enzymes having specific activity towards cannabinoid compounds to generate water-soluble cannabinoid glycoside compounds.

A heparin skeleton synthase originates from Neisseria animaloris, with an amino acid sequence as shown in SEQ ID NO.2 and a nucleotide sequence of the coding gene as shown in SEQ ID NO.1. Its recombinant expression level is 6.8 times that of the existing heparin skeleton synthase KfiA from Escherichia coli K5, and total enzyme activity per fermentation liquor is 5.22 times that of the heparin skeleton synthase KfiA. The heparin skeleton synthase mutants obtained through site-directed mutagenesis of the sites No. 16, No. 25, No. 30, No. 111, No. 165, and No. 172 in the amino acid sequence of the said heparin skeleton synthase all have high expression levels.

Recombinant microorganisms, plants, and plant cells are disclosed that have been engineered to express a mutant AROM polypeptide and/or mutant catechol-O-methyltransferase polypeptide alone or in combination with one or more vanillin biosynthetic enzymes or UDP-glycosyltransferases (UGTs). Such microorganisms, plants, or plant cells can produce vanillin or vanillin beta-D-glucoside.

Recombinant microorganisms, plants, and plant cells are disclosed that have been engineered to express a mutant AROM polypeptide and/or mutant catechol-O-methyltransferase polypeptide alone or in combination with one or more vanillin biosynthetic enzymes or UDP-glycosyltransferases (UGTs). Such microorganisms, plants, or plant cells can produce vanillin or vanillin beta-D-glucoside.

Recombinant microorganisms, plants, and plant cells are disclosed that have been engineered to express a mutant AROM polypeptide and/or mutant catechol-O-methyltransferase polypeptide alone or in combination with one or more vanillin biosynthetic enzymes or UDP-glycosyltransferases (UGTs). Such microorganisms, plants, or plant cells can produce vanillin or vanillin beta-D-glucoside.