Transgenic plants and methods for terpenoid production leveraging such transgenic plants are provided. Such transgenic plants may comprise a first heterologous nucleic acid encoding a polypeptide having 3-hydroxy-3-methylglutarylCoA reductase activity and a second heterologous nucleic acid encoding a polypeptide that introduces de novo formation of isopentenyl phosphate in the plant. Such de novo IP production may be achieved through the overexpression of phosphomevalonate decarboxylase in conjunction with 3-hydroxy-3-methylglutarylCoA reductase, which can result in up to a 130-fold increase of terpenoid production as compared to a wild-type plant.

The present application discloses a method of testing for efficacy of a potential drug agent against cancerous cells in a mammal, including generating the cancer cells in a mammal; contacting the cancer cells with a potential drug agent by administering the potential drug agent to the mammal; and measuring effect of the potential drug agent on the cancer cells, wherein reduction of number of cancer cells in the mammal is indicative of efficaciousness of the potential drug agent against cancerous cells.

This invention relates to in vitro production of nucleic acids, particularly RNAs and specifically messenger RNAs (mRNA).

Provided herein are production systems and methods to produce a plurality of organic carbon-containing compounds from carbon dioxide, including glyceraldehyde 3-phosphate, glucose, cellulose, and starch, using stabilized enzymes in aqueous media.

The present application relates, in some aspects, to the development of an assay that uses cell survival and/or cell viability as a phenotypic identifier to positively select for agents that destabilize a protein of interest.

The present invention relates to an enzyme-catalyzed process for producing UDP-galactose from low-cost substrates uridine monophosphate and D-galactose in a single reaction mixture. The process can be operated (semi)continuously or in batch mode. The process can be extended to uridine as starting material instead of uridine monophosphate. Further, the process can be adapted to produce galactosylated molecules and biomolecules including saccharides, proteins, peptides, glycoproteins or glycopeptides, particularly human milk oligosaccharides (HMO) and (monoclonal) antibodies.

The present disclosure discloses a method for efficient catalytic synthesis of PAPS based on constructing an ATP regeneration system, and belongs to the technical field of bioengineering. Efficient production of PAPS is realized through microbial recombination expression and artificial construction of PAPS bifunctional synthetase. On the basis, an ATP regeneration system coupling with polyphosphate kinase from Corynebacterium glutamicum and Mycobacterium tuberculosis can be used for recovering two byproducts: pyrophosphoric acid and ADP at the same time, the equivalent conversion of a substrate and a product is realized, the PAPS generated in a catalysis system has high purity, and the sulfonic acid group donation in most sulfonic acid transfer reactions can be realized.

The present invention discloses a polyphosphate kinase mutant, engineered strain and application thereof, wherein the polyphosphate kinase mutant is obtained by single- or multi-site mutations of the amino acid at position 79, 106, 108, 111 or 285 of the amino acid sequence shown in SEQ ID No. 2. The present invention provides a variety of polyphosphate kinase mutants derived from Cytophaga hutchinsonii, and the specific enzyme activity of these mutants is 2.7-17.9 times higher than that of the parent polyphosphate kinase, more than 70% of the amount of adenosine triphosphate (ATP) consumption in ATP-dependent biocatalytic synthesis reactions may be reduced by the ATP regeneration system constituted by the mutants, which has broad industrial application prospects.

The present invention relates to an expression system for the heterologous expression of a nucleic acid sequence of interest in a mammalian cell, the system comprising: (i) a first genetic entity, comprising: a nucleic acid sequence encoding a functional Epstein Barr virus nuclear antigen 1 (EBNA-1), the nucleic acid sequence being operably linked to regulatory elements that allow for expression of the nucleic acid sequence encoding a functional EBNA-1; (ii) a second genetic entity, comprising: a nucleic acid sequence encoding a functional nucleoside diphosphate kinase A (NDPK-A), the nucleic acid sequence being operably linked to regulatory elements that allow for expression of the nucleic acid sequence encoding a functional NDPK-A; (iii) a third genetic entity, comprising: the nucleic acid sequence of interest being operably linked to regulatory elements that allow for expression of the nucleic acid sequence of interest; and (iv) a four genetic entity, comprising: the Epstein Barr virus OriP sequence or one or more subsequences thereof, wherein the one or more subsequences comprise at least the ‘Family of Repeats’ DNA-binding site for EBNA-1 and the ‘Dyad Symmetry’ DNA-binding site for EBNA-1. The present invention also relates to corresponding mammalian host cells and methods for expressing a nucleic acid sequence of interest by means of such expression system.

The present invention relates to an enzyme-catalyzed process for producing UDP-N-acetyl-α-D-glucosamine (UDP-GlcNAc) from low-cost substrates uridine monophosphate and N-acetyl-D glucosamine in a single reaction mixture with immobilized or preferably co-immobilized enzymes. Uridine may be used as starting material instead of uridine monophosphate as well. Further, the process may be adapted to produce GlcNAcylated molecules and biomolecules including saccharides, particularly human milk oligosaccharides (HMO), proteins, peptides, glycoproteins, particularly antibodies, or glycopeptides, and bioconjugates, particularly carbohydrate conjugate vaccines and antibody-drug conjugates.