Ajinomoto Co., Ltd.

Uno Tagami

Masayuki Sugiki

Takayuki Ito

Wataru Hoshino

Yasuhiro Mihara

Tatsuki Kashiwagi

Tomoko Shimizu

Chihiro Tsuji

Shogo Nakano

Toshimi Mizukoshi

Tomoharu Motoyama

Yuya Kodama

Sohei Ito

Eri Tabuchi

Kenichi Mori

Shunichi Suzuki

Masakazu Sugiyama

Hiroyuki Nozaki

Ayako Sato

Natalia Viktorovna Stoynova

Sergey Vasilievich Smirnov

Yoshinori Tajima

Hideyuki Suzuki

Yasuaki Takakura

Hiroaki Fukada

Kunio Nakata

Elena Viktorovna Sycheva

Hidemi Fujii

Daiki Yahagi

Ayako Sasahara

Mitsunori Tokura

Takashi Oku

Yasuhiro Kashima

Yuki Oda

Hiroomi Ogino

Koki Ishikawa

Erika Watanabe

Misato Okamoto

Eri Higashiura

Erika Yoshida

Elena V Matrosova

Natalia V Geraskina

The present invention provides a 2-OST mutant exhibiting a high activity. Specifically, the present invention provides a 2-O-sulfation enzyme mutant, having a substitution of a leucine residue at position 321 with a basic amino acid residue in any one amino acid sequence of: (a) the amino acid sequence of SEQ ID NO: 2; (b) an amino acid sequence comprising one or several amino acid substitutions, deletions, insertions, or additions in the amino acid sequence of SEQ ID NO: 2; (c) an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO: 2; (d) the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; (e) an amino acid sequence comprising one or several amino acid substitutions, deletions, insertions, or additions in the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; (f) an amino acid sequence having 90% or more identity to the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; and having a 2-O-sulfate transfer activity.

2-O-sulfation enzyme mutant and 3-O-sulfation enzyme mutant, and method for using same

A method for producing an objective protein and a method for producing a disaccharide are provided. An objective protein is produced by culturingin 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.

Method for producing a protein and disaccharide using a

A mutant glutathione synthetase (GSHB) suitable for generating &#x3b3;-Glu-Val-Gly, and a method for producing &#x3b3;-Glu-Val-Gly using the same are provided. &#x3b3;-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.

Mutant glutathione synthetase and method for producing gamma-glutamyl-valyl-glycine

A mutant glutamate-cysteine ligase (GSHA) suitable for generating &#x3b3;-Glu-Val, and a method for producing &#x3b3;-Glu-Val-Gly using the same are provided. &#x3b3;-Glu-Val is produced by using a mutant GSHA having a specific mutation with Glu and Val as raw materials, and &#x3b3;-Glu-Val-Gly is further produced by using &#x3b3;-Glu-Val and Gly as raw materials. &#x3b3;-Glu-Val-Gly is produced by using a mutant GSHA having a specific mutation with Glu, Val, and Gly as raw materials.

Mutant glutamate-cysteine ligase and method for manufacturing gamma glutamyl-valyl-glycine

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.

Modified isoprene synthase

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.

Modified leucine dehydrogenase

The present invention provides a methodology for improving a yield of 2R,4R-Monatin. Specifically, the present invention provides a method for producing 2S,4R-Monatin or a salt thereof, comprising contacting 4R-IHOG with an L-amino acid aminotransferase in the presence of an L-amino acid to form the 2S,4R-Monatin; a method for producing 2R,4R-Monatin or a salt thereof, comprising isomerizing the 2S,4R-Monatin to form the 2R,4R-Monatin; and the like. These production methods may further comprise condensing indole-3-pyruvate and pyruvate to form the 4R-IHOG, and deaminating a tryptophan to form the indole-3-pyruvate.

Method for producing monatin using an L-amino acid aminotransferase

Growing community of inventors

Kawasaki, Japan

Uno Tagami