Abstract: A mutant glutathione synthetase (GSHB) suitable for generating ?-Glu-Val-Gly, and a method for producing ?-Glu-Val-Gly using the same are provided. ?-Glu-Val-Gly is produced by using a mutant GSHB having a mutation at such a position as V7, N13, I14, N15, K17, F22, F95, M165, N199, Y200, P202, I274, T285, and P287.

Abstract: A method for producing ?-Glu-Val-Gly is described, wherein the method includes the steps of cultivating a ?-Glu-Val-Gly-producing bacterium belonging to the family Enterobacteriaceae in a culture medium so that the ?-Glu-Val-Gly accumulates in the culture medium or the cells of the bacterium, or both, and collecting the ?-Glu-Val-Gly from the culture medium or the cells of the bacterium, or both. The bacterium 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.

Abstract: A mutant glutathione synthetase (GSHB) suitable for generating ?-Glu-Val-Gly, and a method for producing ?-Glu-Val-Gly using the same are provided. ?-Glu-Val-Gly is produced by using a mutant GSHB having a mutation at such a position as V7, N13, I14, N15, K17, F22, F95, M165, N199, Y200, P202, I274, T285, and P287.

Abstract: A mutant glutamate-cysteine ligase (GSHA) suitable for generating ?-Glu-Val, and a method for producing ?-Glu-Val-Gly using the same are provided. ?-Glu-Val is produced by using a mutant GSHA having a specific mutation with Glu and Val as raw materials, and ?-Glu-Val-Gly is further produced by using ?-Glu-Val and Gly as raw materials. ?-Glu-Val-Gly is produced by using a mutant GSHA having a specific mutation with Glu, Val, and Gly as raw materials.

Abstract: A mutant glutamate-cysteine ligase (GSHA) suitable for generating ?-Glu-Val, and a method for producing ?-Glu-Val-Gly using the same are provided. ?-Glu-Val is produced by using a mutant GSHA having a specific mutation with Glu and Val as raw materials, and ?-Glu-Val-Gly is further produced by using ?-Glu-Val and Gly as raw materials. ?-Glu-Val-Gly is produced by using a mutant GSHA having a specific mutation with Glu, Val, and Gly as raw materials.

Abstract: A transglutaminase protein which is mutated to have improved heat resistance and/or pH stability. A mutation is introduced into WT transglutaminase at a cysteine residue capable of forming a disulfide bond (SS bond).

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R,4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by mutating the amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:4.

Abstract: The present invention describes a method for generating a serine derivative and an optically active isomer thereof by a convenient technique, and an enzyme and the like useful in the method. In the presence of the following protein (A) and/or (B) having an enzymatic activity, an ?-amino acid is reacted with an aldehyde to form a serine derivative: (A) a protein comprising the amino acid sequence of SEQ ID NO:5, and (B) a protein comprising an amino acid sequence of SEQ ID NO: 5, but which includes substitution, deletion, insertion and addition of one or more amino acids and is able to catalyze the reaction to form the serine derivative.

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R,4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by substituting an amino acid at least at one of positions (positions 100, 180 to 183, 243 and 244) involved in efficiently producing the (2R,4R)-monatin in an amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:2.

Abstract: The present invention describes a method for generating a serine derivative and an optically active isomer thereof by a convenient technique, and an enzyme and the like useful in the method. In the presence of the following protein (A) and/or (B) having an enzymatic activity, an ?-amino acid is reacted with an aldehyde to form a serine derivative: (A) a protein comprising the amino acid sequence of SEQ ID NO:5, and (B) a protein comprising an amino acid sequence of SEQ ID NO: 5, but which includes substitution, deletion, insertion and addition of one or more amino acids and is able to catalyze the reaction to form the serine derivative.

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R,4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by substituting an amino acid at least at one of positions (positions 100, 180 to 183, 243 and 244) involved in efficiently producing the (2R,4R)-monatin in an amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:2.

Abstract: A transglutaminase protein which is mutated to have improved heat resistance and/or pH stability. A mutation is introduced into WT transglutaminase at a cysteine residue capable of forming a disulfide bond (SS bond).

Abstract: The present invention relates to a method for designing and preparing mutant transglutaminases on the basis of the three-dimensional structure of MTG derived from Streptoverticillium mobaraense (MTG), and the mutant MTG thus prepared. The present invention provides a method for modifying MTG on the basis of the three-dimensional structure, and transglutaminase having reactivity on the substrate improved by the method. In the present invention, the binding site of MTG for the substrate is extrapolated based on the three-dimensional structure obtained by X-ray crystal structure analysis of MTG crystals, and the mutant transglutaminases are designed and produced by replacing, inserting or deleting amino acid residues positioned at the substrate-binding site of the transglutaminase.

Abstract: The present invention relates to variant aldolase enzymes that are modified so as to produce IHOG (4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid: IHOG), a process for producing an optically active IHOG using the same, and a process for producing an optically active monatin.

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R, 4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by substituting an amino acid at least at one of positions (positions 100, 180 to 183, 243 and 244) involved in efficiently producing the (2R, 4R)-monatin in an amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:2.

Abstract: O-acetylserine, L-cysteine and sulphurous compounds derived therefrom may be produced using a bacterium belonging to the genus Escherichia which harbors a mutant feedback-resistant serine acetyltransferases in which the amino acid sequence corresponding to positions from 89 to 96 in a wild-type serine acetyltransferase is replaced with any one of the amino acid sequences shown in SEQ ID NOS: 4 to 9, and feedback inhibition by L-cysteine in the bacterium is desensitized.

Abstract: The present invention aims at providing an excellent peptide-synthesizing protein and a method for efficiently producing a peptide. The peptide is synthesized by reacting an amine component and a carboxy component in the presence of at least one of proteins shown in the following (I) and (II). (I) The mutant protein having an amino acid sequence comprising one or more mutations from any of the mutations 1 to 68, and the mutations 239 to 290 and 324 to 377 in an amino acid sequence of SEQ ID NO:2.

Abstract: The present invention aims at providing an excellent peptide-synthesizing protein and a method for efficiently producing a peptide. The peptide is synthesized by reacting an amine component and a carboxy component in the presence of at least one of proteins shown in the following (I) and (II). (I) The mutant protein having an amino acid sequence comprising one or more mutations from any of the mutations 1 to 68, and the mutations 239 to 290 and 324 to 377 in an amino acid sequence of SEQ ID NO:2.

Abstract: The present invention relates to a method for designing and preparing mutant transglutaminases on the basis of the three-dimensional structure of MTG derived from Streptoverticillium mobaraense (MTG), and the mutant MTG thus prepared. The present invention provides a method for modifying MTG on the basis of the three-dimensional structure, and transglutaminase having reactivity on the substrate improved by the method. In the present invention, the binding site of MTG for the substrate is extrapolated based on the three-dimensional structure obtained by X-ray crystal structure analysis of MTG crystals, and the mutant transglutaminases are designed and produced by replacing, inserting or deleting amino acid residues positioned at the substrate-binding site of the transglutaminase.

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R, 4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by substituting an amino acid at least at one of positions (positions 100, 180 to 183,243 and 244) involved in efficiently producing the (2R, 4R)-monatin in an amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:2.