The present disclosure describes the engineering of microbial cells for fermentative production of deoxyhydrochorismic acid and provides novel engineered microbial cells and cultures, as well as related deoxyhydrochorismic acid production methods.

The present disclosure provides metabolic signatures and genetic markers for tracking enhanced nitrogen utilization efficiency phenotypes in tobacco plants and for introgressing enhanced nitrogen utilization efficiency phenotypes into tobacco plants. The disclosure also provides tobacco plants comprising enhanced nitrogen utilization efficiency and methods to the creation of tobacco plants comprising enhanced nitrogen utilization efficiency. The disclosure also provides recombinant polynucleotides and polypeptides for enhancing nitrogen utilization efficiency in modified tobacco plants and tobacco plants comprising the provided recombinant polynucleotides and polypeptides.

The present invention discloses a genetically engineered bacterium using glucose as a substrate for de novo synthesis of vanillin and an application thereof, which belongs to the technical field of gene recombination and metabolic engineering. The genetically engineered bacterium using the glucose as the substrate for de novo synthesis of vanillin disclosed by the present invention is recombinant Corynebacterium glutamicum modified by chassis microorganisms and including a vanillin synthesis module and a methyl cyclic regeneration module. The genetically engineered bacteria constructed by the present invention are safe and non-toxic, can use the glucose for de novo synthesis of natural vanillin, and is low in production cost, high in yield, and promising in application prospect.

The present invention provides engineered phenylalanine ammonia-lyase (PAL) enzymes comprising one or more mutations that increase the enzymes' tyrosine ammonia-lyase (TAL) activity. Also provided are plants comprising the engineered PAL enzymes and methods of using these plants to sequester CO.sub.2 or produce phenylpropanoid-derived products.

The present disclosure provides a recombinant Escherichia coli for producing chlorogenic acid and application thereof. In the present disclosure, tyrosine ammonia-lyase FjTAL derived from Flavobacterium johnsoniae, hpaBC derived from E. coli, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase mutant aroG.sup.fbr, chorismate mutase tyrC derived from Zymomonas mobilis, quinic acid/shikimate-5 dehydrogenase ydiB derived from E. coli, hydroxycinnamoyl CoA:quinic acid transferase NtHQT derived from Nicotiana tabacum, and 4-coumarate:CoA ligase At4CL1 derived from Arabidopsis thaliana are expressed in the recombinant E. coli, thereby constructing a chlorogenic acid biosynthesis pathway in E. coli. Then, the aroB gene and gldA gene derived from E. coli are overexpressed, and an endogenous gene menI is knocked out from the recombinant E. coli. The recombinant strain produced chlorogenic acid by fermentation at a titer of up to 638.2 mg/L in a shake flask or at a titer of 2.8 g/L in a 5-L fermenter.

Recombinant hosts and methods for producing resveratrol in recombinant hosts are disclosed herein.

The present invention provides transgenic plants comprising 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate (DAHP) Synthase that is insensitive to feedback inhibition, particularly to feedback inhibition by phenylalanine, producing increased amounts of the Shikimate pathway primary and secondary metabolites, including aromatic amino acids compared to corresponding non-transgenic plants.

The invention pertains to a method for preparing cells that can be used as biocatalysts by inducing in them a growth-decoupled state, in which interferase inhibits the expression of genes except the ones that code for the pathway enzymes of interest. mRNAs that code for interferase-resistant products are overexpressed in the background of a metabolically-frozen cell. Enzymes that compete for a substrate or product of the pathway of interest may be altered such that the enzyme is sensitive to a site-specific protease, which protease is inducible in the host cell.

The present invention relates to the use of specific variants of 3-deoxyarabinoheptulosanate 7-phosphate synthase for producing ortho-aminobenzoic acid by means of microbial fermentation and microorganisms suitable for this purpose.

The present invention provides engineered 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DHS) polypeptides comprising mutations that deregulate the shikimate pathway, resulting in increased production of aromatic amino acids and enhanced carbon assimilation in plants. Also provided are polynucleotides, constructs, and vectors that encode the engineered polypeptides; cells, seeds, and plants that express the engineered polypeptides; and methods for generating and using plants that express the engineered polypeptides.