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Journal of Bacteriology, February 2006, p. 1660-1662, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1660-1662.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

MurQ Etherase Is Required by Escherichia coli in Order To Metabolize Anhydro-N-Acetylmuramic Acid Obtained either from the Environment or from Its Own Cell Wall

Tsuyoshi Uehara,1* Kyoko Suefuji,1 Tina Jaeger,2 Christoph Mayer,2 and James T. Park1

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111,1 Fachbereich Biologie, University of Konstanz, 78457 Konstanz, Germany2

Received 11 August 2005/ Accepted 30 November 2005

MurQ is an N-acetylmuramic acid-phosphate (MurNAc-P) etherase that converts MurNAc-P to N-acetylglucosamine-phosphate and is essential for growth on MurNAc as the sole source of carbon (T. Jaegar, M. Arsic, and C. Mayer, J. Biol. Chem. 280:30100-30106, 2005). Here we show that MurQ is the only MurNAc-P etherase in Escherichia coli and that MurQ and AnmK kinase are required for utilization of anhydro-MurNAc derived either from cell wall murein or imported from 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.

Journal of Bacteriology, February 2006, p. 1660-1662, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1660-1662.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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