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Journal of Bacteriology, December 2000, p. 6854-6856, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Genetic Analysis of Peptidoglycan Biosynthesis in Mycobacteria: Characterization of a ddlA Mutant of Mycobacterium smegmatis

Aimee E. Belanger,1 Joelle C. Porter,2 and Graham F. Hatfull1,*

Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260,1 and Human Genome Sciences, Rockville, Maryland 208502

Received 31 May 2000/Accepted 22 September 2000

A temperature-sensitive mutant of Mycobacterium smegmatis was characterized that contains a mutation in ddlA, the gene encoding D-alanine:D-alanine ligase. Enzymatic assays using recombinant proteins and D-cycloserine susceptibility indicate that the A365V mutation in the SMEG35 DdlA protein causes a reduction in enzymatic activity in vitro and in vivo.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260. Phone: (412) 624-6975. Fax: (412) 624-4870. E-mail: gfh{at}vms.cis.pitt.edu.

Journal of Bacteriology, December 2000, p. 6854-6856, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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  • Chacon, O., Feng, Z., Harris, N. B., Caceres, N. E., Adams, L. G., Barletta, R. G. (2002). Mycobacterium smegmatisD-Alanine Racemase Mutants Are Not Dependent on D-Alanine for Growth. Antimicrob. Agents Chemother. 46: 47-54 [Abstract] [Full Text]  


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