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Applied and Environmental Microbiology, June 1999, p. 2781-2783, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Mechanism of Alanine Hyperproduction by Arthrobacter oxydans HAP-1: Metabolic Shift to Fermentation under Nongrowth Aerobic Conditions

Shin-ichi Hashimoto* and Ryoichi Katsumatadagger

Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3-6-6 Asahi-machi, Machida-shi, Tokyo 194-8533, Japan

Received 19 January 1999/Accepted 23 March 1999

Arthrobacter oxydans HAP-1 hyperproduces DL-alanine in a non-growth-associated manner. We found that decreased activities of pyruvate dehydrogenase and of the enzyme catalyzing NADH oxidation in the stationary phase are paralleled by a shift of pyruvate metabolism to alanine synthesis by L-alanine dehydrogenase. We propose that this enzyme functions as an electron sink even under aerobic conditions.

* Corresponding author. Mailing address: Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3-6-6 Asahi-machi, Machida-shi, Tokyo 194-8533, Japan. Phone: 81-427-25-2555. Fax: 81-427-26-8330. E-mail: shashimoto{at}kyowa.co.jp.

dagger Present address: Laboratory of Animal Microbiology, Faculty of Agriculture, Tohoku University, 1-1 Tsutsumidori-Amamiya-machi, Aobaku, Sendai-shi, 981, Japan.

Applied and Environmental Microbiology, June 1999, p. 2781-2783, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.




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