Ajinomoto Co., Ltd.

Ajinomoto Co., Inc., Patent & Licensing Department

Kenzo Yokozeki

Seiichi Hara

Shunichi Suzuki

Isao Abe

Naoto Tonouchi

Masakazu Sugiyama

Norimasa Onishi

Yasuko Jojima

Kunihiko Watanabe

Hiroyuki Nozaki

Yasuhiro Takenaka

Sonoko Suzuki

Ayako Ohno

Shinji Kuroda

Ikuo Kira

Koji Kubota

Kunisuke Izawa

Katsunori Kobayashi

Hideyuki Shirae

Yasuhiro Mihara

Hiroshi Shiragami

Naohiko Yasuda

Shigeru Yamanaka

Koji Mitsugi

Kenichi Hashiguchi

Yasuo Irie

Yoshiteru Hirose

Yuko Tanita

Daisuke Takahashi

Shigeru Nakamori

Yuzuru Eto

Kiyoshi Miwa

Masakazu Nakazawa

Toshihide Yukawa

Chikahiko Eguchi

Toshiya Tanabe

Masaru Otani

Yasuaki Takakura

Masaki Naito

Toshiki Taba

Peter Henderson

Sonoko Takeuchi

Eiji Majima

Hiroshi Matsui

Osamu Kurahashi

Takashi Tanaka

Takashi Tsuji

Konosuke Sano

Yoshimi Kikuchi

Masakazu Sugimoto

Mika Moriya

Seiko Hirano

Atsushi Hayakawa

Tatsuki Kashiwagi

Hisao Iwagami

Kazuhiko Yamada

Masako Izui

Naoki Usui

Ichiro Noda

Fumihide Tamura

Yuki Imabayashi

Takeru Sato

Kazushi Togo

Junko Shinozaki

Maiko Mori

Ryosuke Fudou

Naoko Tsuyoshi

Ryosuke Fudo

Teruhiko Kagawa

Hideo Kano

Hiroaki Takino

Norimasa Oonishi

Norimasa Ohnishi

Chisa Niwa

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 genusand 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.

Enzyme that catalyzes a peptide-forming reaction from a carboxy component and an amine component, microbe producing the same, and a method of producing a dipeptide using the enzyme or microbe

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.

Methods for making 3-indole-pyruvic acid from tryptophan using a tryptophan deaminase

The present invention provides a method of producing optically active amino acids from 5-substituted hydantoin by isolating a hydantoinase gene and an N-carbamyl-L-amino acid hydrolase gene involved in an ability to convert 5-substituted hydantoin or N-carbamylamino acid into optically active amino acids from a microorganism of the genushaving the above ability and by improving gene amplification and transcriptional and translational activities thereby preparing a recombinant wherein the amount of the desired enzymes produced is increased. The hydantoinase gene is, for example, a DNA encoding for a protein having a hydantoinase activity, which has the nucleotide sequence of SEQ ID NO:1. The N-carbamyl-L-amino acid hydrolase gene is, for example, a DNA encoding for a protein having an N-carbamyl-L-amino acid hydrolase activity, which has the nucleotide sequence of SEQ ID NO:3.

DNA encoding hydantoinase, DNA encoding N-carbamyl-L-amino acid hydrolase, recombinant DNA, transformed cell, method of producing protein, and method of producing optically active amino acid

Oxidase gene and method for producing 3-indole-pyruvic acid by utilizing the gene

A method of producing an &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b2;-ester by forming the &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b2;-ester from L-aspartic acid-&#x3b1;,&#x3b2;-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an &#x3b1;-ester site of the L-aspartic acid-&#x3b1;,&#x3b2;-diester through a peptide bond.

Method for producing &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b2;-ester and method for producing &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b1;-methyl ester

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 &#x3b1;-amino acid is reacted with an aldehyde to form a serine derivative:

Method for producing serine derivative and protein used for the same

The present invention provides a method for 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.

Method for producing dipeptides

Method for producing a dipeptide

A method of producing an &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b2;-ester by forming the &#x3b1;-L-aspartyl-L-phenylalanine-&#x3b2;-ester from L-aspartic acid-&#x3b1;&#x3b2;-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an &#x3b1;-ester site of the L-aspartic acid-&#x3b1;&#x3b2;-diester through a peptide bond.

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-&#x3b1;-amino acid of formula (I): (in the formula (I), Ris a hydrocarbon group)is reacted with an aldehyde of formula (II): (in the formula (II), Ris a hydrocarbon)to produce an L-serine derivative of formula (III). .

Method of producing L-serine derivative and enzyme used therefore

A novel protein which has an activity to transport hydantoin compounds is described, as well as a recombinant expressing this transporter protein. Fromstrain 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.

Transporter protein

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Kanagawa, Japan

Kenzo Yokozeki