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Journal of Bacteriology, August 2007, p. 5634-5641, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.00446-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

An Anhydro-N-Acetylmuramyl-L-Alanine Amidase with Broad Specificity Tethered to the Outer Membrane of Escherichia coli{triangledown}

Tsuyoshi Uehara* and James T. Park

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

Received 26 March 2007/ Accepted 11 May 2007

From its amino acid sequence homology with AmpD, we recognized YbjR, now renamed AmiD, as a possible second 1,6-anhydro-N-acetylmuramic acid (anhMurNAc)-L-alanine amidase in Escherichia coli. We have now confirmed that AmiD is an anhMurNAc-L-Ala amidase and demonstrated that AmpD and AmiD are the only enzymes present in E. coli that are able to cleave the anhMurNAc-L-Ala bond. The activity was present only in the outer membrane fraction obtained from an ampD mutant. In contrast to AmpD, which is specific for the anhMurNAc-L-alanine bond, AmiD also cleaved the bond between MurNAc and L-alanine in both muropeptides and murein sacculi. Unlike the periplasmic murein amidases, AmiD did not participate in cell separation. ampG mutants, which are unable to import GlcNAc-anhMurNAc-peptides into the cytoplasm, released mainly peptides into the medium due to AmiD activity, whereas an ampG amiD double mutant released a large amount of intact GlcNAc-anhMurNAc-peptides into the medium.

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

{triangledown} Published ahead of print on 25 May 2007.

Journal of Bacteriology, August 2007, p. 5634-5641, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.00446-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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