A non-naturally occurring microbial organism includes a microbial organism having a 1,3-butanediol (1,3-BDO) pathway having at least one exogenous nucleic acid encoding a 1,3-BDO pathway enzyme expressed in a sufficient amount to produce 1,3-BDO. The pathway includes an enzyme selected from a 2-amino-4-ketopentanoate (AKP) thiolase, an AKP dehydrogenase, a 2-amino-4-hydroxypentanoate aminotransferase, a 2-amino-4-hydroxypentanoate oxidoreductase (deaminating), a 2-oxo-4-hydroxypentanoate decarboxylase, a 3-hydroxybutyraldehyde reductase, an AKP aminotransferase, an AKP oxidoreductase (deaminating), a 2,4-dioxopentanoate decarboxylase, a 3-oxobutyraldehyde reductase (ketone reducing), a 3-oxobutyraldehyde reductase (aldehyde reducing), a 4-hydroxy-2-butanone reductase, an AKP decarboxylase, a 4-aminobutan-2-one aminotransferase, a 4-aminobutan-2-one oxidoreductase (deaminating), a 4-aminobutan-2-one ammonia-lyase, a butenone hydratase, an AKP ammonia-lyase, an acetylacrylate decarboxylase, an acetoacetyl-CoA reductase (CoA-dependent, aldehyde forming), an acetoacetyl-CoA reductase (CoA-dependent, alcohol forming), an acetoacetyl-CoA reductase (ketone reducing), a 3-hydroxybutyryl-CoA reductase (aldehyde forming), a 3-hydroxybutyryl-CoA reductase (alcohol forming), a 4-hydroxybutyryl-CoA dehydratase, and a crotonase. A method for producing 1,3-BDO, includes culturing such microbial organisms under conditions and for a sufficient period of time to produce 1,3-BDO.

Transgenic host cells, vectors useful for making transgenic host cells, and kits useful for making transgenic host cells are described. Also described are transgenic plants. In some embodiments, transgenic host cells express a 4-hydroxyphenylacetaldehyde synthase (4HPAAS). In some embodiments, transgenic host cells express a tyrosol:UDP-glucose 8-O-glucosyltransferase (T8GT). The transgenic host cells are useful for biosynthesis of one or more of salidroside, icariside D2, tyrosol, and 4-hydroxypenylacetaldehyde.

Some embodiments relate to genetically engineered bacterial strains for modulation of levels of the bacterial metabolite 4-ethylphenol (4EP) and its sulfated form, 4-ethylphenyl sulfate (4EPS). In some embodiments, the bacteria reduce or inhibit production of 4EP or 4EPS in the gut of a subject. The bacteria can ameliorate, delay the onset, or reduce the likelihood of one or more symptoms associated with anxiety and/or autism spectrum disorder (ASD) in the subject.

Described are 3-methylcrotonic acid decarboxylase (MDC) variants showing an improved activity in converting 3-methylcrotonic acid into isobutene as well as methods for the production of isobutene using such enzyme variants.

The present disclosure describes the engineering of microbial cells for fermentative production of 4-APEA and related products and provides novel engineered microbial cells and cultures, as well as related 4-APEA production methods.

With the aim of providing a method allowing production of an unsaturated hydrocarbon compound such as butadiene with high productivity and an enzyme used in the method, the present inventors introduced mutations involving amino acid replacement into various positions of a ferulic acid decarboxylase, and prepared multiple modified forms of the enzyme. Then, the present inventors evaluated those modified forms in terms of the catalytic activity for the production of butadiene, and found as a result that the catalytic activity was improved in the case where, for example, the amino acid at position 395 was glutamine, histidine, asparagine, leucine, isoleucine, methionine, lysine, serine, arginine, tyrosine, or phenylalanine.

Disclosed herein are prokaryotic and eukaryotic microbes, including E. coli and S. cerevisiae, genetically altered to biosynthesize tryptamine and tryptamine derivatives. The microbes of the disclosure may be engineered to contain plasmids and stable gene integrations containing sufficient genetic information for conversion of an anthranilate or an indole to a tryptamine. The fermentative production of substituted tryptamines in a whole-cell biocatalyst may be useful for cost effective production of these compounds for therapeutic use.

Described are methods for the production of isobutene comprising the enzymatic conversion of 3-methylcrotonic acid into isobutene wherein the enzymatic conversion of 3-methylcrotonic acid into isobutene is achieved by making use of an FMN-dependent decarboxylase associated with an FMN prenyl transferase, wherein said FMN prenyl transferase catalyzes the prenylation of a flavin cofactor (FMN or FAD) utilizing dimethylallyl phosphate (DMAP) into a flavin-derived cofactor, wherein said method further comprises providing said DMAP enzymatically by: (i) the enzymatic conversion of dimethylallyl pyrophosphate (DMAPP) into said DMAP; or (ii) a single enzymatic step in which prenol is directly enzymatically converted into said DMAP; or (iii) two enzymatic steps comprising: first enzymatically converting DMAPP into prenol; and then enzymatically converting the thus obtained prenol into said DMAP; or (iv) the enzymatic conversion of isopentenyl monophosphate (IMP) into said DMAP, or by a combination of any one of (i) to (iv). Moreover, described are methods for the production of isobutene comprising the enzymatic conversion of 3-methylcrotonic acid into isobutene wherein the enzymatic conversion of 3-methylcrotonic acid into isobutene is achieved by making use of an FMN-dependent decarboxylase associated with an FMN prenyl transferase, wherein said FMN prenyl transferase catalyzes the prenylation of a flavin cofactor (FMN or FAD) utilizing dimethylallyl pyrophosphate (DMAPP), wherein said method further comprises providing said DMAPP enzymatically by: (v) the enzymatic conversion of isopentenyl pyrophosphate (IPP) into said DMAPP; or (vi) the enzymatic conversion of dimethylallyl phosphate (DMAP) into said DMAPP; or (vii) the enzymatic conversion of prenol into said DMAPP; (viii) or by a combination of any one of (v) to (vii). Moreover, described are methods for providing said flavin cofactor enzymatically by the enzymatic conversion of riboflavin into flavin mononucleotide (FMN).

Disclosed herein are prokaryotic and eukaryotic microbes, including E. coli and S. cerevisiae, genetically altered to biosynthesize tryptamine and tryptamine derivatives. The microbes of the disclosure may be engineered to contain plasmids and stable gene integrations containing sufficient genetic information for conversion of an anthranilate or an indole to a tryptamine. The fermentative production of substituted tryptamines in a whole-cell biocatalyst may be useful for cost effective production of these compounds for therapeutic use.

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.