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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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