The present invention relates to a method of producing glutathione, wherein photosynthetic membrane vesicles and enzymes catalyzing glutathione synthesis are combined and glutamate, cysteine and glycine are used as reaction substrates. As enzymes catalyzing glutathione synthesis, γ-glutamylcysteine synthetase and glutathione synthetase may be used together, or bifunctional glutathione synthetase may be used alone. According to the conventional methods, there is a problem in that expensive adenosine triphosphate should be continuously supplied when glutathione is produced. However, according to the present invention, since photosynthetic membrane vesicles are used as a source to regenerate adenosine triphosphate, it is possible to continuously produce glutathione without additionally adding adenosine triphosphate, thereby reducing production costs of glutathione.

This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.

Provided are a novel promoter, a vector including the same, a microorganism including the same, and a method of producing glutathione using the same.

The present invention relates to a method of producing glutathione, wherein photosynthetic membrane vesicles and enzymes catalyzing glutathione synthesis are combined and glutamate, cysteine and glycine are used as reaction substrates. As enzymes catalyzing glutathione synthesis, γ-glutamylcysteine synthetase and glutathione synthetase may be used together, or bifunctional glutathione synthetase may be used alone. According to the conventional methods, there is a problem in that expensive adenosine triphosphate should be continuously supplied when glutathione is produced. However, according to the present invention, since photosynthetic membrane vesicles are used as a source to regenerate adenosine triphosphate, it is possible to continuously produce glutathione without additionally adding adenosine triphosphate, thereby reducing production costs of glutathione.

This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.

A microorganism useful as an expression host for γ-Glu-Val synthetase and a method for producing γ-Glu-Val-Gly using γ-Glu-Val synthetase expressed in the microorganism are provided. By using γ-Glu-Val synthetase expressed in a bacterium, such as Escherichia bacteria, modified so that the activity of a protein encoded by a ybdK gene (YBDIQ is reduced as an expression host, γ-Glu-Val-Gly is produced (Yom Glu, Val, and Gly as raw materials.

The present invention provides a method for producing an L-amino acid such as a branched-chain L-amino acid by fermentation using a bacterium of the family Enterobacteriaceae, particularly a bacterium belonging to the genus Escherichia, which has been modified to attenuate expression of the gshA gene.

The present disclosure concerns a method for producing peptides such as glutathione and a microorganism that can be used for such method. One or more embodiments of the first aspect of the present disclosure concern a method for producing peptides such as glutathione comprising culturing a prokaryotic microbial strain in which the expression levels of one or more genes selected from among the gshA gene, the gshB gene, and the gshF gene are enhanced, compared with the expression levels thereof in the wild-type strain thereof in a medium in which the total concentration of cysteine and cystine is 0.5 g/l or lower. The second aspect of the present disclosure concerns a microorganism comprising disruptions of the γ-glutamyltransferase gene and the glutathione reductase gene and exhibiting the enhanced expression levels of the gshA gene and the gshB or gshF gene.

The invention provides an improved host strain for production of desired protein.

This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.