Provided herein are biocatalysts and systems thereof for pterin-dependent enzymes and pathways and methods of making and using the same.

A method is described for producing an L-amino acid including the steps of cultivating in a culture medium an L-amino acid-producing bacterium belonging to the family Enterobacteriaceae to produce and accumulate the L-amino acid in the culture medium, cells of the bacterium, or both, and collecting the L-amino acid from the culture medium, the cells, or both, wherein said bacterium has been modified to overexpress a gene encoding a periplasmic adaptor protein.

This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.

The disclosure relates, in some aspects, to compositions and methods useful for production of nitrated aromatic molecules. The disclosure is based, in pan, on whole cell systems expressing artificial fusion proteins comprising cytochrome P450 enzymes linked to reductase enzymes. In some aspects, the disclosure relates to methods of producing nitrated aromatic molecules in whole cell systems having artificial fusion proteins comprising cytochrome P450 enzymes linked to reductase enzymes.

The present application relates to a novel promoter and a method for producing target materials using the same. More specifically, the present application relates to a novel polynucleotide having promoter activity, a gene expression cassette, and a host cell comprising the same, and a method for producing target materials using the microorganism.

This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.

This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.

The present disclosure relates to a microorganism of the genus Corynebacterium producing L-amino acid, a method for producing L-amino acid using the same, use of L-amino acid production, and a composition for producing L-amino acid.

Disclosed are processes and methods for production of pigment compounds, such as melanin, using engineered microbial systems and chemical modifications to intermediate compounds. One process involves producing a first intermediate (e.g., an amino acid like tyrosine) and a second intermediate (e.g., an enzyme like tyrosinase) within a microbial cell, exporting the intermediates to an extracellular medium, and enabling their reaction outside the cell to form the pigment compound. The microbial cell is genetically engineered to enhance production and export of intermediates, prevent reuptake, and optimize enzyme activity post-export. Additional intermediates or capping agents are introduced to modulate pigment properties, such as color, molecular weight, and solubility. The process may be applied to produce various pigments, including pheomelanin and violacein, and is scalable for industrial applications in textiles, cosmetics, and carbon sequestration. The system minimizes cellular toxicity, simplifies purification, and allows for tailored pigment production.

An engineered strain for improving tryptophan production and a construction method and use thereof are provided. By screening out a strain capable of tolerating high-concentration tryptophan and performing genomic sequencing and protein sequence analysis on the strain, it is found that certain proteins in the strain undergo point mutations and these mutations are capable of enhancing tryptophan production. To increase tryptophan production, protein sequences encoded by fadR or pepD genes in a parent strain are modified. These modifications result in an engineered strain with significantly higher tryptophan production compared to the parent strain. Under scaled-up production conditions, the tryptophan production reaches 62.385.80 g/L in a 5 L fermenter, with a glucose-to-tryptophan yield of 24.1%. Compared to an original strain, tryptophan production increases by 1.48-fold, and the glucose-to-tryptophan yield improves by 1.26-fold. The biological materials and its use belong to the technical field of molecular biology and possess broad practical application value.