Abstract: A method of denaturing a protein by treating the protein with a protein glutaminase and a transglutaminase, a food containing a protein having been denatured with these enzymes, and an enzyme preparation for denaturing a protein which contains these enzymes. A protein is denatured by adding protein glutaminase and transglutaminase to the protein substantially at the same timing, or adding protein glutaminase to the protein before the transglutaminase acts on the protein, or controlling the quantitative ratio of protein glutaminase to transglutaminase, by which a protein is treated, to a definite level.

Abstract: An insulin preparation having an ultra-rapid onset of action is provided by adding a substance that interacts with the insulin dimer formation surface or the hexamer formation surface to an insulin solution. The substance exerts its effect by inhibiting insulin dimer formation and/or hexamer formation.

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 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 method for producing a protein having an antithrombotic activity, which comprises replacing, in a protein that has an amino acid sequence having a homology of not less than 30% to the amino acid sequence of SEQ ID NO: 1 and forms a higher order structure composed of a first ? strand (?1), a first a helix (?1), a second ? helix (?2), a second ? strand (?2), a loop, a third ? strand (?3), a fourth ? strand (?4) and a fifth ? strand (?5) in this order from the amino terminus, at least one amino acid residue in a region from ?2 to ?2 and/or a region from ?3 to ?4 so that electric charge of the amino acid residue is changed towards positive direction.

Abstract: There is provided a mutant nucleoside-5?-phosphate producing enzyme with improved nucleoside-5?-phosphate producing ability of a nucleoside-5?-phosphate producing enzyme that has transphosphorylation activity and/or phosphatase activity and has one Lys residue, two Arg residues and two His residues with distances between their C?'s within a particular ranges and a space around them allowing a binding of a nucleoside, of which mutation is designed by using the crystal structure of EB-AP.

Abstract: A method for producing a protein having an antithrombotic activity, which comprises replacing, in a protein that has an amino acid sequence having a homology of not.less than 30% to the amino acid sequence of SEQ ID NO: 1 and forms a higher order structure composed of a first &bgr; strand (&bgr;1), a first a helix (&agr;1), a second &agr; helix (&agr;2), a second &bgr; strand (&bgr;2), a loop, a third &bgr; strand (&bgr;3), a fourth &bgr; strand (&bgr;4) and a fifth &bgr; strand (&bgr;5) in this order from the amino terminus, at least one amino acid residue in a region from &agr;2 to &bgr;2 and/or a region from &bgr;3 to &bgr;4 so that electric charge of the amino acid residue is changed towards positive direction.

Abstract: The present invention provides a method for isotopically labeling a functional group possessed by an amino acid residue of a protein. The present invention also provides a protein whose functional group in an amino acid residue is isotopically labeled. A functional group in an amino acid residue of a protein is substituted with an isotope-labeling group derived from an isotope-labeling compound by making use of the action of an enzyme. In particular, the carboxyamide nitrogen atom in a glutamine residue of a protein is replaced with an isotopically labeled atom by acting a transglutaminase on the glutamine residue.

Abstract: A method for producing a protein having an antithrombotic activity, which comprises replacing, in a protein that has an amino acid sequence having a homology of not less than 30% to the amino acid sequence of SEQ ID NO: 1 and forms a higher order structure composed of a first &bgr; strand (&bgr;1), a first &agr; helix (&agr;1), a second &agr; helix (&agr;2), a second &bgr; strand (&bgr;2), a loop, a third &bgr; strand (&bgr;3), a fourth &bgr; strand (&bgr;4) and a fifth &bgr; strand (&bgr;5) in this order from the amino terminus, at least one amino acid residue in a region from &agr;2 to &bgr;2 and/or a region from &bgr;3 to &bgr;4 so that electric charge of the amino acid residue is changed towards positive direction.

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 method for producing a protein having an antithrombotic activity, which comprises replacing, in a protein that has an amino acid sequence having a homology of not less than 30% to the amino acid sequence of SEQ ID NO: 1 and forms a higher order structure composed of a first &bgr; strand (&bgr;1), a first &agr; helix (&agr;1), a second &agr; helix (&agr;2), a second &bgr; strand (&bgr;2), a loop, a third &bgr; strand (&bgr;3), a fourth &bgr; strand (&bgr;4) and a fifth &bgr; strand (&bgr;5) in this order from the amino terminus, at least one amino acid residue in a region from &agr;2 to &bgr;2 and/or a region from &bgr;3 to &bgr;4 so that electric charge of the amino acid residue is changed towards positive direction.

Abstract: The present invention provides a method for isotopically labeling a functional group possessed by an amino acid residue of a protein. The present invention also provides a protein whose functional group in an amino acid residue is isotopically labeled.