Abstract: The present invention provides a 2-OST mutant exhibiting a high activity.

Abstract: Described herein is an enzyme useful for producing a target peptide, capable of producing the target peptide without requiring ATP. More specifically, provided herein is a modified enzyme includes an amino acid sequence such as a modified amino acid sequence including a mutation of one or more of the following amino acid residues: E81, I127, I136, T139, F140, G142, W143, I147, I181, I201, Q219, T229, M244, A249, P255, E256, I260, S293, N294, Y295, and I299 in an amino acid sequence of SEQ ID NO: 1, and having the following property (a) or (b) enhanced relative to an enzyme of the amino acid sequence of SEQ ID NO: 1: (a) imidazole dipeptide production activity; or (b) thermal stability.

Abstract: The present invention provides a 2-OST mutant exhibiting a high activity.

Abstract: The present invention provides an alternative L-glutamate oxidase that allows for measurement of L-glutamate. More specifically, the present invention provides the following L-glutamate oxidase mutant (a) or (b) and the like: (a) an L-glutamate oxidase mutant including an amino acid sequence that has 90% or more identity to an amino acid sequence of SEQ ID NO: 3 and exhibits an activity of oxidizing L-glutamate, except an L-glutamate oxidase including an amino acid sequence of SEQ ID NO: 1; or (b) an L-glutamate oxidase mutant comprising a peptide linker consisting of 1 to 20 amino acid residues which is inserted into one or more sites selected from the group consisting of (1) a site in a region proximity to a boundary between ?1 and ?2 regions, (2) a site in a region proximity to a boundary between ?2 and ? regions and (3) a site in a region proximity to a boundary between ? and ? regions in the L-glutamate oxidase mutant (a), and having the activity of oxidizing L-glutamate.

Abstract: The present invention provides a 2-OST mutant exhibiting a high activity.

Abstract: The present invention provides a unit and a method useful for more precise phenylalanine measurement. More specifically, the present invention provides a modified phenylalanine dehydrogenase that includes a mutation of at least one amino acid residue so as to improve the characteristics (for example, substrate specificity, solubility, and phenylalanine dehydrogenase activity) of a phenylalanine dehydrogenase related to measurement of phenylalanine, a method for analyzing phenylalanine by measuring phenylalanine contained in a test sample using the modified phenylalanine dehydrogenase, and others.

Abstract: A method for producing an objective protein and a method for producing a disaccharide are provided. An objective protein is produced by culturing Talaromyces cellulolyticus in a culture medium containing an expression inducer such as gentiobiose. A disaccharide is produced from a saccharide raw material by enzymatic conversion using a disaccharide synthesizing enzyme.

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 method for producing an objective protein and a method for producing a disaccharide are provided. An objective protein is produced by culturing Talaromyces cellulolyticus in a culture medium containing an expression inducer such as gentiobiose. A disaccharide is produced from a saccharide raw material by enzymatic conversion using a disaccharide synthesizing enzyme.

Abstract: The present invention provides a 2-OST mutant exhibiting a high 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 technique for efficiently culturing cells such as stem cells is provided. Cells such as stem cells are cultured using a cell culture vessel coated with a fibroin-like protein into which a cell adhesion sequence containing RGD (Arg-Gly-Asp) is inserted.

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: The present application relates to a modified isoprene synthase that has an isoprene synthetic activity and has at least one mutation of an amino acid residue in the amino acid sequence of SEQ ID NO: 4, an amino acid sequence having one or several amino acid substitutions, deletions, insertions or additions in the amino acid sequence of SEQ ID NO: 4, or an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO: 4. The modified isoprene synthase is useful for preparing isoprene monomers in improved yields.

Abstract: The present invention provides a means and method useful for measurement of a total branched-chain amino acid concentration. Specifically, the present invention provides a modified enzyme in which at least one amino acid residue is mutated so as to improve a property of a leucine dehydrogenase which is associated with the measurement of the total branched-chain amino acids, such as, for example, substrate specificities of leucine dehydrogenase for total branched-chain amino acids, activity of leucine dehydrogenase for any branched-chain amino acids, and thermal stability of leucine dehydrogenase; and a method of analyzing the total branched-chain amino acids, comprising measuring the total branched-chain amino acids contained in a test sample using the modified enzyme.

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: The present invention provides a means and method useful for measurement of a total branched-chain amino acid concentration. Specifically, the present invention provides a modified enzyme in which at least one amino acid residue is mutated so as to improve a property of a leucine dehydrogenase which is associated with the measurement of the total branched-chain amino acids, such as, for example, substrate specificities of leucine dehydrogenase for total branched-chain amino acids, activity of leucine dehydrogenase for any branched-chain amino acids, and thermal stability of leucine dehydrogenase; and a method of analyzing the total branched-chain amino acids, comprising measuring the total branched-chain amino acids contained in a test sample using the modified enzyme.

Abstract: Modified isoprene synthases that have one or more mutations of a given amino acid residue(s) in any amino acid sequence of (a) the amino acid sequence of SEQ ID NO:4, (b) an amino acid sequence having one or several amino acid substitutions, deletions, insertions or additions in the amino acid sequence of SEQ ID NO:4, or (c) an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO:4, and has an isoprene synthetic activity are useful for preparing isoprene monomer in improved yields.

Abstract: The present invention provides a means and method useful for measurement of a total branched-chain amino acid concentration. Specifically, the present invention provides a modified enzyme in which at least one amino acid residue is mutated so as to improve a property of a leucine dehydrogenase which is associated with the measurement of the total branched-chain amino acids, such as, for example, substrate specificities of leucine dehydrogenase for total branched-chain amino acids, activity of leucine dehydrogenase for any branched-chain amino acids, and thermal stability of leucine dehydrogenase; and a method of analyzing the total branched-chain amino acids, comprising measuring the total branched-chain amino acids contained in a test sample using the modified enzyme.