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Journal of Bacteriology, April 2000, p. 2052-2054, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Purification and Properties of Ornithine Racemase from Clostridium sticklandii

Hao-Ping Chen,1,* Chin-Fen Lin,1 Ya-Jung Lee,2,3 San-San Tsay,4 and Shih-Hsiung Wu3

Department of Biochemistry, China Medical College, Taichung 404,1 Department of Food Science, National Chung-Hsiung University, Taichung 402,2 Department of Botany, National Taiwan University, Taipei 106,4 and Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei 115,3 Taiwan

Received 29 September 1999/Accepted 7 January 2000

Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an Mr of 92,000, with a Km for L-ornithine of 0.77 ± 0.05 mM and a kcat of 980 ± 20 s-1.

* Corresponding author. Mailing address: Department of Biochemistry, China Medical College, Taichung 404, Taiwan. Phone: 886-4-2053366, ext. 8706. Fax: 886-4-2053764. E-mail: hpchen{at}mail.cmc.edu.tw.

Journal of Bacteriology, April 2000, p. 2052-2054, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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