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J Bacteriol, February 1998, p. 945-949, Vol. 180, No. 4
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Biochemical and Genetic Characterization of trans-2'-Carboxybenzalpyruvate Hydratase-Aldolase from a Phenanthrene-Degrading Nocardioides Strain

Tokuro Iwabuchidagger and Shigeaki Harayama*

Marine Biotechnology Institute, Kamaishi Laboratories, 3-75-1 Heita, Kamaishi, Iwate 026, Japan

Received 11 August 1997/Accepted 6 December 1997

trans-2'-Carboxybenzalpyruvate hydratase-aldolase was purified from a phenanthrene-degrading bacterium, Nocardioides sp. strain KP7, and characterized. The purified enzyme was found to have molecular masses of 38 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 113 kDa by gel filtration chromatography. Thus, the homotrimer of the 38-kDa subunit constituted an active enzyme. The Km and kcat values of this enzyme for trans-2'-carboxybenzalpyruvate were 50 µM and 13 s-1, respectively. trans-2'-Carboxybenzalpyruvate was transformed to 2-carboxybenzaldehyde and pyruvate by the action of this enzyme. The structural gene for this enzyme was cloned and sequenced; the length of this gene was 996 bp. The deduced amino acid sequence of this enzyme exhibited homology to those of trans-2'-hydroxybenzalpyruvate hydratase-aldolases from Pseudomonas putida PpG7 and Pseudomonas sp. strain C18.

* Corresponding author. Mailing address: Marine Biotechnology Institute, Kamaishi Laboratories, 3-75-1 Heita, Kamaishi, Iwate 026, Japan. Phone: 81-193-26-6544. Fax: 81-193-26-6592. E-mail: harayama{at}kamaishi.mbio.co.jp.

dagger Present address: Shiseido Research Center, 1050 Nippa, Kohoku-ku, Yokohama, Kanagawa 223, Japan.




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