Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-??-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-??-diester through a peptide bond.

Abstract: The present invention provides a method for efficiently producing a ?-alanyl-amino acid (e.g., carnosine) or derivative thereof. Specifically, it provides a method for producing a ?-alanyl-amino acid (e.g., ?-alanyl-histidine) or derivative thereof, by reacting a ?-alanyl ester or a ?-alanyl amide and an amino acid or derivative thereof in the presence of an enzyme or an enzyme-containing product that has an ability to form the ?-alanyl-amino acid (e.g., ?-alanyl-histidine) or derivative thereof from the ?-alanyl ester or the ?-alanyl amide and the amino acid (e.g., histidine) or derivative thereof. The present invention also provides a protein which is able to catalyze production of a ?-alanyl-amino acid or derivative thereof from a ?-alanyl ester or a ?-alanyl amide and an amino acid or derivative thereof, and a polynucleotide encoding said protein.

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: The present invention provides a new method for producing serine derivatives and their optically-activated derivatives in a convenient manner. In the presence of an enzyme, an L-?-amino acid of formula (I): (in the formula (I), R1 is a hydrocarbon group) is reacted with an aldehyde of formula (II): (in the formula (II), R2 is a hydrocarbon) to produce an L-serine derivative of formula (III). .

Abstract: A novel protein which has an activity to transport hydantoin compounds is described, as well as a recombinant expressing this transporter protein. From Microbacterium liquefaciens strain AJ3912, a novel gene was discovered to encode a protein which is able to transport hydantoin compounds. A recombinant with an excellent ability to uptake hydantoin compounds is obtained by introducing and expressing the novel gene, called mhp, using gene recombination techniques.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-??-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-??-diester through a peptide bond.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: It is an object of the present invention to provide a procedure for realizing inexpensive and simple production of 3-indole-pyruvic acid. A transformant is made using a polynucleotide having a specific nucleotide sequence encoding a protein having an oxidase activity, and oxidase is generated by culturing the transformant in a medium to accumulate the oxidase in the medium and/or the transformant. Further, tryptophan is converted into 3-indole-pyruvic acid in the presence of the transformant and/or a culture thereof to produce 3-indole-pyruvic acid.

Abstract: The present invention provides a method of producing a dipeptide from starting materials that are available at low costs through a route industrially advantageous and simple. Dipeptides are produced from amino acid esters and amino acids by using a culture of a microbe having an ability to produce a dipeptide from an amino acid ester and an amino acid, microbial cells separated from the culture, or treated microbial cell product.

Abstract: A method is disclosed that allows the production of peptides having three or more amino acid residues easily, inexpensively and at high yield without going through a complex synthesis method. A novel enzyme that efficiently produces a peptide from bacteria belonging to the genus Empedobacter or the genus Sphingobacterium is provided. The enzyme acts on a carboxy component and an amine component to form peptides having three or more amino acid residues by acting on a carboxy component and an amine component.

Abstract: A method for producing ?-hydroxy amino acid and its optically-active isomer is provided. The ?-hydroxy amino acid is produced by reacting a predetermined D-?-amino acid and 5,10-methylene tetrahydrofolic acid in the presence of an enzyme derived from a microorganism belonging to the genera Paracoccus, Aminobacter, or Ensifer.

Abstract: A method for producing an ?-L-aspartyl-L-phenylalanine-?-ester (also named ?-L-(?-o-substituted aspartyl)-L-phenylalanine), which is an intermediate of an ?-L-aspartyl-L-phenylalanine-?-methyl ester (also named ?-L-aspartyl-L-phenylalanine methyl ester; product name: aspartame), easily, at high yield and inexpensively without going through a complex synthesis method is provided. Further, an easy, inexpensive and high-yield production method for an ?-L-aspartyl-L-phenylalanine-?-methyl ester is provided. ?-L-aspartyl-L-phenylalanine-?-methyl ester is produced from a L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to catalyze a reaction in which L-phenylalanine performs no nucleophilic attack on a ?-ester site of L-aspartic acid-?,?-diester but performs a nucleophilic attack on an ?-ester site thereof.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: The present invention provides a method for producing dipeptide using inexpensively acquirable starting materials by an industrially advantageous and simple pathway. Dipeptide is produced from L-amino acid ester and L-amino acid using a culture of microbes having the ability to produce a dipeptide from an L-amino acid ester and an L-amino acid, using microbial cells isolated from the culture, or a treated microbial cell product of the microbe.

Abstract: A novel protein which has an activity to transport hydantoin compounds is described, as well as a recombinant expressing this transporter protein. From Microbacterium liquefaciens strain AJ3912, a novel gene was discovered to encode a protein which is able to transport hydantoin compounds. A recombinant with an excellent ability to uptake hydantoin compounds is obtained by introducing and expressing the novel gene, called mhp, using gene recombination techniques.

Abstract: The present invention relates to a 5-substituted hydantoin racemase, which efficiently catalyzes racemization reactions at a high optimum temperature for racemization reactions, DNA coding for the racemase, and processes for producing optically active amino acids.

Abstract: A method for producing an ?-L-aspartyl-L-phenylalanine-?-ester (also named ?-L-(?-o-substituted aspartyl)-L-phenylalanine), which is an intermediate of an ?-L-aspartyl-L-phenylalanine-?-methyl ester (also named ?-L-aspartyl-L-phenylalanine methyl ester; product name: aspartame), easily, at high yield and inexpensively without going through a complex synthesis method is provided. Further, an easy, inexpensive and high-yield production method for an ?-L-aspartyl-L-phenylalanine-?-methyl ester is provided. ?-L-aspartyl-L-phenylalanine-?-methyl ester is produced from a L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to catalyze a reaction in which L-phenylalanine performs no nucleophilic attack on a ?-ester site of L-aspartic acid-?,?-diester but performs a nucleophilic attack on an ?-ester site thereof.

Abstract: A method for producing ?-hydroxy amino acid and its optically-active isomer is provided. The ?-hydroxy amino acid is produced by reacting a predetermined D-?-amino acid and 5,10-methylene tetrahydrofolic acid in the presence of an enzyme derived from a microorganism belonging to the genera Paracoccus, Aminobacter, or Ensifer.

Abstract: The present invention provides a new method for producing serine derivatives and their optically-activated derivatives in a convenient manner. In the presence of an enzyme, an L-?-amino acid of formula (I): (in the formula (I), R1 is a hydrocarbon group) is reacted with an aldehyde of formula (II): (in the formula (II), R2 is a hydrocarbon) to produce an L-serine derivative of formula (III).