The present disclosure relates to an ATP phosphoribosyltransferase (HisG) protein and a method for producing histidine using the same.

The present disclosure relates to an ATP phosphoribosyltransferase (HisG) protein and a method for producing histidine using the same.

A method for producing ergothioneine at a low cost in large quantities and a bacterium for use in said method are provided. A method for producing ergothioneine or a related substance thereof, or a mixture thereof, comprising culturing a bacterium belonging to the family Enterobacteriaceae having the ergothioneine-producing ability in a culture medium, and collecting ergothioneine or a related substance thereof, or a mixture thereof, from the culture medium or from the cells obtained by culture, wherein said bacterium is the one which is modified so as to have a reduced activity of a protein comprising a core sequence region comprising 5 amino acid residues: Ser-Arg-Gly-Arg-Thr (SEQ ID NO:7) as a part thereof; and a bacterium belonging to the family Enterobacteriaceae having the ergothioneine-producing ability modified so as to have a reduced activity of a protein comprising a core sequence region comprising 5 amino acid residues: Ser-Arg-Gly-Arg-Thr (SEQ ID NO:7) as a part thereof.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

A method for producing an L-amino acid such as L-glutamic acid is provided. An L-amino acid is produced by culturing a bacterium having an ability to produce an L-amino acid, which has been modified so that the activity of a non-PTS fructose-uptake carrier and the activity of fructokinase are both increased, in a medium containing fructose, and collecting the L-amino acid from the medium or cells of the bacterium.

A method for producing an L-amino acid such as L-glutamic acid is provided. An L-amino acid is produced by culturing a bacterium having an ability to produce an L-amino acid, which has been modified so that the activity of a non-PTS fructose-uptake carrier and the activity of fructokinase are both increased, in a medium containing fructose, and collecting the L-amino acid from the medium or cells of the bacterium.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises (a) a protein having the amino acid sequence as shown in SEQ ID NO: 2; (b) a protein having an amino acid sequence of SEQ HD NO: 2 with a mutation of one or more amino acids and having a proline hydroxylase activity; or (c) a protein retaining the mutation of one or more amino acids as in (b), and having the proline hydroxylase activity and having at least 78% homology with the amino acid sequence of the protein in (b). Protein having the amino acid sequence as shown in SEQ HD NO: 2 and mutants obtained by genetically engineering have higher catalytic specificity or significantly increased catalytic activity when compared to proline hydroxylases in prior art.