Kyowa Hakko Kogyo Co., Ltd.

Kyowa Hakko Bio Co., Ltd.

Kyowa Hakko Food Specialties Co., Ltd.

Junko Ohnishi

Masato Ikeda

Keiko Ochiai

Satoshi Mitsuhashi

Satoshi Nakagawa

Akio Ozaki

Yoshiyuki Yonetani

Mikiro Hayashi

Haruhiko Yokoi

Hiroshi Mizoguchi

The present invention relates to a polypeptide having a modified amino acid sequence of 6-phosphogluconate dehydrogenase (hereinafter abbreviated as GND) derived from a microorganism belonging to the genus, said modification being substitution of the amino acid residue(s) at the position(s) corresponding to the 158th and/or the 361st amino acid(s) of the amino acid sequence shown in SEQ ID NO: 1, and having GND activity; DNA encoding the polypeptide; a recombinant DNA comprising the DNA; a transformant carrying the recombinant DNA; a microorganism carrying the DNA on the chromosome; and a process for producing a useful substance which comprises culturing the transformant or the microorganism in a medium.

Mutant 6-phosphogluconate dehydrogenase

Mutated 6-phosphogluconate dehydrogenase

The present invention provides a polypeptide comprising an amino acid sequence in which at least one amino acid is deleted, substituted or added in an amino acid sequence of isopropylmalate isomerase derived from a microorganism belonging to coryneform bacteria, wherein a coryneform bacterium which produces the polypeptide comprising the amino acid sequence as the sole isopropylmalate isomerase exhibits a partial leucine requirement in a minimal medium; a DNA encoding the polypeptide, a recombinant DNA comprising the DNA, a microorganism transformed with the recombinant DNA, and a process for producing an L-amino acid using the microorganism.

Mutant isopropylmalate isomerase

The present invention relates to a novel aspartokinase derived from a Coryneform bacterium; a DNA encoding the enzyme; a recombinant DNA containing the above DNA; a Coryneform bacterium having the above recombinant DNA or a Coryneform bacterium having the DNA on its chromosome; and a process for producing L-lysine by culturing the above microorganism. Construction has been successfully made of a DNA encoding an aspartokinase freed from concerted feedback inhibition by L-lysine and L-threonine derived from aand has a nucleotide sequence encoding an amino acid sequence wherein the amino acid residue at position 311 is an amino acid other than Thr in the amino acid sequence shown by SEQ ID NO: 18.

Desensitized aspartokinase

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Nagano, Japan

Junko Ohnishi