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Journal of Bacteriology, January 2003, p. 679-682, Vol. 185, No. 2
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.2.679-682.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Identification of MpaA, an Amidase in Escherichia coli That Hydrolyzes the {gamma}-D-Glutamyl-meso-Diaminopimelate Bond in Murein Peptides

Tsuyoshi Uehara and James T. Park*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 13 September 2002/ Accepted 17 October 2002

MpaA amidase was identified in Escherichia coli by its amino acid sequence homology with the ENP1 endopeptidase from Bacillus sphaericus. The enzymatic activity of MpaA, i.e., hydrolysis of the {gamma}-D-glutamyl-diaminopimelic acid bond in the murein tripeptide L-alanyl-{gamma}-D-glutamyl-meso-diaminopimelic acid, was demonstrated in the cell extract of a strain expressing mpaA from a multicopy plasmid. An mpaA mpl (murein peptide ligase) double mutant accumulated large amounts of murein tripeptide in its cytoplasm, consistent with the premise that MpaA degrades the tripeptide if its recycling via the peptidoglycan biosynthetic pathway is blocked.

* Corresponding author. Mailing address: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-6753. Fax: (617) 636-0337. E-mail: james.park{at}tufts.edu.

Journal of Bacteriology, January 2003, p. 679-682, Vol. 185, No. 2
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.2.679-682.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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