Patent classifications
C12Y202/01001
Method for producing L-lysine using microorganisms having ability to produce L-lysine
The present invention relates to a modified polynucleotide encoding aspartate kinase (EC:2.7.2.4; hereinafter, referred to as LysC), transketolase (EC:2.2.1.1; hereinafter, referred to as Tkt) or pyruvate carboxylase (EC:6.4.1.1; hereinafter, referred to as Pyc), in which the initiation codon is substituted with ATG, a vector including the same, a microorganism transformed with the vector, and a method for producing L-lysine using the same.
Compositions and methods for increased ethanol production from biomass
The present application discloses the identification of the novel K. marxianus xylose transporter genes KHT105 and RAG4, as well as the identification of a novel set of I. orientalis pentose phosphate pathway genes The present application further discloses a series of genetically modified yeast cells comprising various combinations of arabinose fermentation pathways, xylose fermentation pathways, pentose phosphate pathways, and/or xylose transporter genes, and methods of culturing these cells to produce ethanol in fermentation media containing xylose.
GENETIC ENGINEERING BACTERIUM FOR DE NOVO SYNTHESIS OF CIS,CIS-MUCONIC ACID BY TAKING GLUCOSE AS SUBSTRATE AND APPLICATIONS THEREOF
The present invention discloses a genetic engineering bacterium for de novo synthesis of cis,cis-muconic acid by taking glucose as a substrate and applications thereof, and belongs to the technical field of genetic recombination and metabolic engineering. The genetic engineering bacterium for de novo synthesis of cis,cis-muconic acid (MA) by taking glucose as the substrate disclosed in the present invention is modified with chassis microbes, and includes recombinant Corynebacterium glutamicum for a cis,cis-muconic acid pathway construction module and an intermediate high-yield module. Production capacity of strains is greatly improved; MA of 90.2 g/L is finally obtained in fermentation liquor; and possibilities are provided for green and low-cost production of numerous chemicals such as adipic acid and nylon-66.
METHOD FOR PRODUCING AROMATIC COMPOUND
Provided are a method for producing an aromatic compound or a salt thereof using a transformed cell capable of producing the aromatic compound or the salt thereof, and this transformed cell. The present invention provides a method for producing an aromatic compound or a salt thereof, comprising the step of culturing a transformed cell with enhanced expression of a multi-pass transmembrane polypeptide represented by the following (A) or (B): (A) a polypeptide consisting of the amino acid sequence represented by SEQ ID NO: 2, and (B) a polypeptide consisting of an amino acid sequence having at least 76% identity to the amino acid sequence represented by SEQ ID NO: 2.
RECOMBINANT YEAST CELL
A recombinant yeast cell functionally expressing: a) a nucleic acid sequence encoding a protein having NAD+-dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10); and b) a nucleic acid sequence encoding a protein having transketolase activity (EC 2.2.1.1), wherein the expression of the nucleic acid sequence encoding the protein having transketolase activity is under control of a promoter (the TKL promoter), which TKL promoter has an anaerobic/aerobic expression ratio for the transketolase of 2 or more.
ENGINEERED PROTEINS WITH A PROTEASE CLEAVAGE SITE
Various aspects and embodiments herein relate to recombinant proteins with at least one protease recognition sequence that can be inactivated by a cognate protease and methods of preparing such proteins. In some embodiments, recombinant phosphoglucose isomerase (Pgi) proteins are provided. In other embodiments, recombinant phosphotransacetylase (Pta) proteins are provided. In yet other embodiments, recombinant transketolase A (TktA) proteins are provided.
METHODS FOR CONTROL OF FLUX IN METABOLIC PATHWAYS
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.
Engineered phosphoglucose isomerase proteins with a protease cleavage site
Various aspects and embodiments herein relate to recombinant proteins with at least one protease recognition sequence that can be inactivated by a cognate protease and methods of preparing such proteins. In some embodiments, recombinant phosphoglucose isomerase (Pgi) proteins are provided. In other embodiments, recombinant phosphotransacetylase (Pta) proteins are provided. In yet other embodiments, recombinant transketolase A (TktA) proteins are provided.
CELL-FREE SYSTEM FOR CONVERTING METHANE INTO FUEL AND CHEMICAL COMPOUNDS
The present disclosure relates, in some aspects, to cell-free methods and systems for large-scale conversion of methane to isobutanol, comprising combining, in a bioreactor at elevated pressure, methane, oxygen, and cell lysates containing methane monooxygenase, methanol dehydrogenase, and enzymes that catalyze the conversion of formaldehyde to isobutanol, to form a cell-free reaction mixture, and incubating under suitable conditions the cell-free reaction to convert methane to isobutanol.
METHOD FOR PRODUCING L-LYSINE USING MICROORGANISMS HAVING ABILITY TO PRODUCE L-LYSINE
The present invention relates to a modified polynucleotide encoding aspartate kinase (EC:2.7.2.4; hereinafter, referred to as LysC), transketolase (EC:2.2.1.1; hereinafter, referred to as Tkt) or pyruvate carboxylase (EC:6.4.1.1; hereinafter, referred to as Pyc), in which the initiation codon is substituted with ATG, a vector including the same, a microorganism transformed with the vector, and a method for producing L-lysine using the same.