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Applied and Environmental Microbiology, April 1999, p. 1459-1462, Vol. 65, No. 4
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cyclic-Imide-Hydrolyzing Activity of D-Hydantoinase from Blastobacter sp. Strain A17p-4

Chee-Leong Soong, Jun Ogawa, Michinari Honda, and Sakayu Shimizu*

Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

Received 28 September 1998/Accepted 12 January 1999

The cyclic-imide-hydrolyzing activity of a prokaryotic cyclic-ureide-hydrolyzing enzyme, D-hydantoinase, was investigated. The enzyme hydrolyzed cyclic imides with bulky substituents such as 2-methylsuccinimide, 2-phenylsuccinimide, phthalimide, and 3,4-pyridine dicarboximide to the corresponding half-amides. However, simple cyclic imides without substituents, which are substrates of imidase (i.e., succinimide, glutarimide, and sulfur-containing cyclic imides such as 2,4-thiazolidinedione and rhodanine), were not hydrolyzed. The combined catalytic actions of bacterial D-hydantoinase and imidase can cover the function of a single mammalian enzyme, dihydropyrimidinase. Prokaryotic D-hydantoinase also catalyzed the dehydrative cyclization of the half-amide phthalamidic acid to the corresponding cyclic imide, phthalimide. The reversible hydrolysis of cyclic imides shown by prokaryotic D-hydantoinase suggested that, in addition to pyrimidine metabolism, it may also function in cyclic-imide metabolism.

* Corresponding author. Mailing address: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan. Phone: 81-75-753-6115. Fax: 81-75-753-6128. E-mail: sim{at}kais.kyoto-u.ac.jp.

Applied and Environmental Microbiology, April 1999, p. 1459-1462, Vol. 65, No. 4
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Soong, C.-L., Ogawa, J., Sakuradani, E., Shimizu, S. (2002). Barbiturase, a Novel Zinc-containing Amidohydrolase Involved in Oxidative Pyrimidine Metabolism. J. Biol. Chem. 277: 7051-7058 [Abstract] [Full Text]  
  • Kim, G. J., Lee, D. E., Kim, H.-S. (2000). Functional Expression and Characterization of the Two Cyclic Amidohydrolase Enzymes, Allantoinase and a Novel Phenylhydantoinase, from Escherichia coli. J. Bacteriol. 182: 7021-7028 [Abstract] [Full Text]  
  • Soong, C.-L., Ogawa, J., Shimizu, S. (2000). A Novel Amidase (Half-Amidase) for Half-Amide Hydrolysis Involved in the Bacterial Metabolism of Cyclic Imides. Appl. Environ. Microbiol. 66: 1947-1952 [Abstract] [Full Text]  


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