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Journal of Bacteriology, August 2002, p. 4321-4325, Vol. 184, No. 15
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.15.4321-4325.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Mutant Analysis Shows that Alanine Racemases from Pseudomonas aeruginosa and Escherichia coli Are Dimeric

Ulrich Strych and Michael J. Benedik*

Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5001

Received 4 February 2002/ Accepted 29 April 2002

Alanine racemases are ubiquitous prokaryotic enzymes providing the essential peptidoglycan precursor D-alanine. We present evidence that the enzymes from Pseudomonas aeruginosa and Escherichia coli function exclusively as homodimers. Moreover, we demonstrate that expression of a K35A Y235A double mutation of dadX in E. coli suppresses bacterial growth in a dominant negative fashion.

* Corresponding author. Mailing address: Department of Biology and Biochemistry, University of Houston, Houston, TX 77204-5001. Phone: (713) 743-8377. Fax: (713) 743-8351. E-mail: benedik{at}uh.edu.

Journal of Bacteriology, August 2002, p. 4321-4325, Vol. 184, No. 15
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.15.4321-4325.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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  • Mustata, G., Briggs, J. M. (2004). Cluster analysis of water molecules in alanine racemase and their putative structural role. Protein Eng Des Sel 17: 223-234 [Abstract] [Full Text]  


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