Abstract: The present invention provides a method for producing glycine or a salt thereof by fermentation of a bacterium which has been modified to overexpress a gene encoding a protein having L-threonine 3-dehydrogenase activity and a gene encoding a protein having 2-amino-3-oxobutanoate coenzyme A ligase activity. The bacterium can be, for example, a coryneform bacterium or a bacterium belonging to the family Enterobacteriaceae.

Abstract: The present invention provides a method for producing glycine or a salt thereof by fermentation of a bacterium which has been modified to overexpress a gene encoding a protein having L-threonine 3-dehydrogenase activity and a gene encoding a protein having 2-amino-3-oxobutanoate coenzyme A ligase activity. The bacterium can be, for example, a coryneform bacterium or a bacterium belonging to the family Enterobacteriaceae.

Abstract: The present invention provides a coryneform bacterium having an ability to produce a heterologous fusion protein by secretory production, which has been modified to express a genetic construct for secretory production of the heterologous fusion protein encoding at least a heterologous fusion protein comprising an extein and an intein having an activity of acyl rearrangement. The method for producing proteins modified at the C-terminus is also provided.

Abstract: The present invention provides a coryneform bacterium having an ability to produce a heterologous fusion protein by secretory production, which has been modified to express a genetic construct for secretory production of the heterologous fusion protein encoding at least a heterologous fusion protein comprising an extein and an intein having an activity of acyl rearrangement. The method for producing proteins modified at the C-terminus is also provided.

Abstract: A method for producing an L-amino acid is described, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan, or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of a wild-type alcohol dehydrogenase encoded by the adhE gene or a mutant alcohol dehydrogenase which is resistant to aerobic inactivation.

Abstract: A method for manufacturing a product of a reaction catalyzed by a protein having 2-oxoglutarate-dependent enzyme activity such as (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof using a bacterium transformed with a DNA fragment containing a gene coding for a protein having 2-oxoglutarate-dependent enzyme activity such as L-isoleucine dioxygenase activity; and wherein said bacterium has the ability to produce a product such as (2S,3R,4S)-4-hydroxy-L-isoleucine.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A method for manufacturing a product of a reaction catalyzed by a protein having 2-oxoglutarate-dependent enzyme activity such as (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof using a bacterium transformed with a DNA fragment containing a gene coding for a protein having 2-oxoglutarate-dependent enzyme activity such as L-isoleucine dioxygenase activity; and wherein said bacterium has the ability to produce a product such as (2S,3R,4S)-4-hydroxy-L-isoleucine.

Abstract: A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof using an L-isoleucine-producing bacterium transformed with a DNA fragment containing a gene coding for a protein having L-isoleucine dioxygenase activity; and having the ability to produce (2S,3R,4S)-4-hydroxy-L-isoleucine.

Abstract: A highly active L-isoleucine dioxygenase from Bacillus thuringiensis is provided. A method for manufacturing (2S,3R,4S)-4-hydroxy-L-isoleucine or a salt thereof by reacting L-isoleucine in an aqueous solvent in the presence of L-isoleucine dioxygenase and isolating (2S,3R,4S)-4-hydroxy-L-isoleucine is also provided.

Abstract: A method for producing an L-amino acid is described, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan, or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of a wild-type alcohol dehydrogenase encoded by the adhE gene or a mutant alcohol dehydrogenase which is resistant to aerobic inactivation.

Abstract: L-arginine, citrulline and pyrimidine derivatives including orotic acid, uridine, uridine 5?-monophosphate (UMP), cytidine and cytidine 5?-monophosphate (CMP) are produced using a bacterium belonging to the genus Escherichia harboring a mutant carbamoylphosphate synthetase in which the amino acid sequence corresponding to positions from 947 to 951 in a wild type carbamoylphosphate synthetase is replaced with any one of amino acid sequences of SEQ ID NOS: 1 to 9, and feedback inhibition by uridine 5?-monophosphate in the bacterium is desensitized.

Abstract: L-arginine, citrulline and pyrimidine derivatives including orotic acid, uridine, uridine 5?-monophosphate (UMP), cytidine and cytidine 5?-monophosphate (CMP) are produced using a bacterium belonging to the genus Escherichia harboring a mutant carbamoylphosphate synthetase in which the amino acid sequence corresponding to positions from 947 to 951 in a wild type carbamoylphosphate synthetase is replaced with any one of amino acid sequences of SEQ ID NOS: 1 to 9, and feedback inhibition by uridine 5?-monophosphate in the bacterium is desensitized.

Abstract: L-arginine, citrulline and pyrimidine derivatives including orotic acid, uridine, uridine 5′-monophosphate (UMP), cytidine and cytidine 5′-monophosphate (CMP) are produced using a bacterium belonging to the genus Escherichia harboring a mutant carbamoylphosphate synthetase in which the amino acid sequence corresponding to positions from 947 to 951 in a wild type carbamoylphosphate synthetase is replaced with any one of amino acid sequences of SEQ ID NOS: 1 to 9, and feedback inhibition by uridine 5′-monophosphate in the bacterium is desensitized.