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Journal of Bacteriology, January 2001, p. 397-400, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.397-400.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Some Lactobacillus L-Lactate Dehydrogenases Exhibit Comparable Catalytic Activities for Pyruvate and Oxaloacetate

Kazuhito Arai,1 Takeo Kamata,1 Hiroyuki Uchikoba,2 Shinya Fushinobu,2 Hiroshi Matsuzawa,2 and Hayao Taguchi1,*

Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510,1 and Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657,2 Japan

Received 23 May 2000/Accepted 6 October 2000

The nonallosteric and allosteric L-lactate dehydrogenases of Lactobacillus pentosus and L. casei, respectively, exhibited broad substrate specificities, giving virtually the same maximal reaction velocity and substrate Km values for pyruvate and oxaloacetate. Replacement of Pro101 with Asn reduced the activity of the L. pentosus enzyme toward these alternative substrates to a greater extent than the activity toward pyruvate.

* Corresponding author. Mailing address: Department of Applied Bioscience, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510, Japan. Phone: 81-471-24-1501, ext. 3407. Fax: 81-471-23-9767. E-mail: htaguchi{at}rs.noda.sut.ac.jp.

Journal of Bacteriology, January 2001, p. 397-400, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.397-400.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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