Described herein are devices and methods for increasing the production of steviol glycosides, which have industrial and economic value. The steviol glycosides produced by the devices and methods disclosed herein do not require the ultra purification that is common in conventional or commercial methods and do not have a bitter aftertaste, making them better suited as flavor-enhancing additives to food, pharmaceutical, and nutritional supplement products.

The present disclosure provides genetically modified host cells that produce a cannabinoid, a cannabinoid derivative, a cannabinoid precursor, or a cannabinoid precursor derivative. The present disclosure provides methods of synthesizing a cannabinoid, a cannabinoid derivative, a cannabinoid precursor, or a cannabinoid precursor derivative.

This document relates to using bidirectional, multi-enzymatic scaffolds to biosynthesize cannabinoids in recombinant hosts.

Genetically engineered hosts and methods for their production and use in synthesizing hydrocarbons are provided.

This invention relates to the field of genetic engineering. Specifically, the invention relates to the construction of operons to produce biologically active agents. For example, operons may be constructed to produce agents that control the function of biochemical pathway proteins (e.g., protein phosphatases, kinases and/or proteases). Such agents may include inhibitors and modulators that may be used in studying or controlling phosphatase function associated with abnormalities in a phosphatase pathway or expression level. Fusion proteins, such as light activated protein phosphatases, may be genetically encoded and expressed as photoswitchable phosphatases. Systems are provided for use in controlling phosphatase function within living cells or in identifying small molecule inhibitors/activator/modulator molecules of protein phosphatases associated with cell signaling.

The present invention provides for a genetically modified host cell capable of producing isopentenol and/or 3-methyl-3-butenol, comprising (a) an increased expression of phosphomevalonate decarboxylase (PMD) (b) an increased expression of a phosphatase capable of converting isopentenol into 3-methyl-3-butenol, (c) optionally the genetically modified host cell does not express, or has a decreased expression of one or more of NudB, phosphomevalonate kinase (PMK), and/or PMD, and (d) optionally one or more further enzymes capable of converting isopentenol and/or 3-methyl-3-butenol into a third compound, such as isoprene.

The present invention provides for a genetically modified yeast host cell capable of producing elevated levels of 3-methyl-3-butene-1-ol or isoprenol.

Described are mevalonate diphosphate decarboxylase variants having improved activity in converting 3-phosphonoxyisovalerate into isobutene. Such variants can be employed in processes for biologically producing isobutene from 3-hydroxyisovalerate or from 3-hydroxy-3-methylbutyrate into isobutene, for biologically producing isoprenol from mevalonate or from mevalonate-3-phosphate or for biologically producing 1,3-butadiene from 3-hydroxypent-4-enoate or from 3-phosphonoxypent-4-enoate. Also described is an enzyme which is characterized in that it is capable of converting 3-phosphonoxyisovalerate into isobutene with a kcat of more than 0.1 s.sup.−1.

Disclosed are nucleic acid sequences comprising a first E. coli homology region, wherein the first E. coli homology region comprises a protospacer adjacent motif (PAM) mutation; a constitutive promoter; a mevalonate-3-kinase (M3K) gene; a mevalonate diphosphate decarboxylase (MVD) gene; and a second E. coli homology region. Disclosed are vectors comprising one or more of the disclosed nucleic acid sequences. Disclosed are recombinant cells comprising a nucleic acid sequence, wherein the nucleic acid sequence comprises a first E. coli homology region, wherein the first E. coli homology region comprises a PAM mutation; a constitutive promoter; a M3K gene; a MVD gene; and a second E. coli homology region.

Described herein are devices and methods for increasing the production of steviol glycosides, which have industrial and economic value. The steviol glycosides produced by the devices and methods disclosed herein do not require the ultra purification that is common in conventional or commercial methods and do not have a bitter aftertaste, making them better suited as flavor-enhancing additives to food, pharmaceutical, and nutritional supplement products.