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Journal of Bacteriology, December 2000, p. 6827-6830, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Comparison of the UDP-N-Acetylmuramate:L-Alanine Ligase Enzymes from Mycobacterium tuberculosis and Mycobacterium leprae

Sebabrata Mahapatra, Dean C. Crick, and Patrick J. Brennan*

Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1677

Received 5 June 2000/Accepted 11 September 2000

In the peptidoglycan of Mycobacterium leprae, L-alanine of the side chain is replaced by glycine. When expressed in Escherichia coli, MurC (UDP-N-acetyl-muramate:L-alanine ligase) of M. leprae showed Km and Vmax for L-alanine and glycine similar to those of Mycobacterium tuberculosis MurC, suggesting that another explanation should be sought for the presence of glycine.

* Corresponding author. Mailing address: Department of Microbiology, Colorado State University, Fort Collins, CO 80523-1677. Phone: (970) 491-6700. Fax: (970) 491-1815. E-mail: pbrennan{at}cvmbs.colostate.edu.

Journal of Bacteriology, December 2000, p. 6827-6830, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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