The invention relates to a genetically modified prokaryotic cell capable of improved iron-sulfur cluster delivery, characterized by a modified gene encoding a mutant Iron Sulfur Cluster Regulator (IscR) and one or more transgenes or upregulated endogenous genes encoding iron-sulfur (Fe—S) cluster polypeptides or proteins that catalyze complex radical-mediated molecular rearrangements, electron transfer, radical or non-redox reactions, sulfur donation or perform regulatory functions. The prokaryotic cells are characterized by enhanced activity of these iron-sulfur (Fe—S) cluster polypeptides, enhancing their respective functional capacity, and facilitating enhanced yields of compounds in free and protein-bound forms, including heme, hemoproteins, tetrapyrroles, B vitamins, amino acids, δ-aminolevulinic acid, biofuels, isoprenoids, pyrroloquinoline quinone, ammonia, indigo, or their precursors, whose biosynthesis depends on their activity. The invention further relates to a method for producing said compounds or their precursors using the genetically modified prokaryotic cell of the invention, and the use of the genetically modified prokaryotic cell.

The present disclosure relates to a novel method, expression vectors, and host cells for producing nicotinamide riboside by regulating the pathways that lead to the production of nicotinamide riboside.

The present invention is directed to microbial production of nicotinamide riboside and/or nicotinamide mononucleotide using a genetically modified fungus.

The present disclosure relates to a novel method, expression vectors, and host cells for producing nicotinamide riboside by regulating the pathways that lead to the production of nicotinamide riboside.

A cofactor self-sufficient Escherichia coli and its construction method and application in the synthesis of L-glufosinate are provided. The present invention expresses a NADH kinase and key enzymes of the cofactor synthesis pathway in E. coli, and knocks out the genes of enzymes that catabolizes cofactor, and with the addition of co-metabolic intermediates during cell incubation, the intracellular NADP(H) concentration is increased by at least 50% and the catalytic activity of glufosinate dehydrogenase by 2-fold, resulting in a significant increase in the spatiotemporal yield of the glufosinate synthesis reaction.