Kaneka Corporation

Daisuke Moriyama

Naoaki Taoka

Tozo Nishiyama

Shinichi Yoshida

Akira Iwasaki

Kohei Mori

Motohisa Washida

Yoshihiko Yasohara

Akira Nishiyama

Noriyuki Kizaki

Nobuo Nagashima

Makoto Ueda

Masutoshi Nojiri

Takahiro Oishi

The present invention has its object to provide a novel polypeptide having amidase activity to selectively hydrolyze S-enantiomer in racemic nipecotamide, a DNA encoding the polypeptide, a vector containing the DNA, a transformant transformed with the vector, and a method for producing an optically active carboxylic acid amide and an optically active carboxylic acid in which a racemic carboxylic acid amide is hydrolyzed with the polypeptide or the transformant.

Amidase, gene for the same, vector, transformant, and method for production of optically active carboxylic acid amide and optically active carboxylic acid by using any one of those items

Water-forming NADH oxidase derived fromshould be further improved in terms of stability for practical use in industrial production. An object of the present invention is to provide an enzyme that is obtained through modification of a water-forming NADH oxidase, which is useful as an NAD+ regeneration system for stereoselective oxidation catalyzed by an oxidoreductase, by protein engineering techniques so that the enzyme can withstand long-term use without exhibiting a reduction of its activity for the regeneration of NAD+, that is, an enzyme having improved stability, and to provide a method for efficiently producing a useful substance such as an optically active alcohol or amino acid. The present invention relates to an enzyme modification method that can improve the stability of water-forming NADH oxidase derived fromby appropriately introducing mutation.

Protein having NADH and/or NADPH oxidase activity

Isolated DNA encoding protein having improved stability

The present invention is to provide a process for efficiently producing an optically active alcohol including (R)-3-hydroxy-3-phenylpropanenitrile. One of the features of the present invention is a polypeptide having an activity of asymmetrically reducing 3-oxo-3-phenylpropanenitrile isolated from a microorganism belonging to the genusto produce (R)-3-hydroxy-3-phenylpropanenitrile, DNA encoding the polypeptide and a transformant of producing the polypeptide. Another feature of the present invention is a process for producing an optically active alcohol such as (R)-3-hydroxy-3-phenylpropanenitrile by reducing a carbonyl compound such as 3-oxo-3-phenylpropanenitrile by use of the polypeptide or the transformant.

Carbonyl reductase, gene therefor and use thereof

An objective of the present application is to provide an industrially practicable method for producing an optically-active 3-amino-2-hydroxypropionic cyclopropylamide derivative or salt thereof from an inexpensive easily-available starting material. The derivative or salt thereof is useful as an intermediate for a medicine. It is also intended by the present application to provide a useful intermediate of the derivative. The objective is attained by the following method. First, an easily-available 2-halo-3-oxopropionic acid derivative is asymmetrically reduced, and then epoxidated to produce an optically-active epoxycarboxylic acid derivative. Next, the derivative is converted into an optically-active epoxyamide derivative by reaction with cyclopropylamine, and then reacted with a nitrile to obtain an optically-active oxazolinamide derivative. Subsequently, selective acid solvolysis of the oxazoline skeleton gives the optically-active 3-amino-2-hydroxypropionic cyclopropylamide derivative or salt thereof.

Process for production of optically active-3-amino-2-hydroxypropionic cyclopropylamide derivatives and salts thereof

The present invention is to provide a process for simply producing an optically active 3-hydroxypropionic ester derivative useful as a medicament intermediate from an inexpensive material. More specifically, the present invention is directed to a process for producing an optically active 3-hydroxypropionic ester derivative comprising reacting an acetic ester derivative available at low cost with a base and a formic ester, thereby converting the acetic ester derivative into a 2-formylacetic ester derivative, and thereafter, stereospecifically reducing the formyl group of the derivative by use of an enzymatic source capable of stereoselectively reducing the formyl group of the derivative.

Process for producing optically active 3-hydroxypropionic ester derivative

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Takasago, Japan

Daisuke Moriyama