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Applied and Environmental Microbiology, October 1998, p. 4093-4094, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Substrate Selectivity and Biochemical Properties of 4-Hydroxy-2-Keto-Pentanoic Acid Aldolase from Escherichia coli

John R. Pollard, Delphine Rialland, and Timothy D. H. Bugg*

Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom

Received 22 May 1998/Accepted 14 July 1998

4-Hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli was identified as a class I aldolase. The enzyme was found to be highly selective for the acetaldehyde acceptor but would accept alpha -ketobutyric acid or phenylpyruvic acid in place of the pyruvic acid carbonyl donor.

* Corresponding author. Mailing address: Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom. Phone: 01703-593816. Fax: 01703-593781. E-mail: tdb{at}soton.ac.uk.

Applied and Environmental Microbiology, October 1998, p. 4093-4094, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hernaez, M. J., Floriano, B., Rios, J. J., Santero, E. (2002). Identification of a Hydratase and a Class II Aldolase Involved in Biodegradation of the Organic Solvent Tetralin. Appl. Environ. Microbiol. 68: 4841-4846 [Abstract] [Full Text]  
  • Diaz, E., Ferrandez, A., Prieto, M. A., Garcia, J. L. (2001). Biodegradation of Aromatic Compounds by Escherichia coli. Microbiol. Mol. Biol. Rev. 65: 523-569 [Abstract] [Full Text]  


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