This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cheng, Q.
Right arrow Articles by Park, J. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cheng, Q.
Right arrow Articles by Park, J. T.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2000, p. 4836-4840, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Characterization of the beta -N-Acetylglucosaminidase of Escherichia coli and Its Role in Cell Wall Recycling

Qiaomei Cheng, Hongshan Li, Keith Merdek, and James T. Park*

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

Received 17 April 2000/Accepted 2 June 2000

The beta -N-acetylglucosaminidase of Escherichia coli was found to have a novel specificity and to be encoded by a gene (nagZ) that maps at 25.1 min. It corresponds to an open reading frame, ycfO, whose predicted amino acid sequence is 57% identical to that of Vibrio furnissii ExoII. NagZ hydrolyzes the beta -1,4 glycosidic bond between N-acetylglucosamine and anhydro-N-acetylmuramic acid in cell wall degradation products following their importation into the cell during the process for recycling cell wall muropeptides. From amino acid sequence comparisons, the novel beta -N-acetylglucosaminidase appears to be conserved in all 12 gram-negative bacteria whose complete or partial genome sequence data are available.

* 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: jpark{at}opal.tufts.edu.

Journal of Bacteriology, September 2000, p. 4836-4840, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Plumbridge, J. (2009). An Alternative Route for Recycling of N-Acetylglucosamine from Peptidoglycan Involves the N-Acetylglucosamine Phosphotransferase System in Escherichia coli. J. Bacteriol. 191: 5641-5647 [Abstract] [Full Text]  
  • Asgarali, A., Stubbs, K. A., Oliver, A., Vocadlo, D. J., Mark, B. L. (2009). Inactivation of the Glycoside Hydrolase NagZ Attenuates Antipseudomonal {beta}-Lactam Resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 53: 2274-2282 [Abstract] [Full Text]  
  • Park, J. T., Uehara, T. (2008). How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan). Microbiol. Mol. Biol. Rev. 72: 211-227 [Abstract] [Full Text]  
  • Uehara, T., Park, J. T. (2008). Growth of Escherichia coli: Significance of Peptidoglycan Degradation during Elongation and Septation. J. Bacteriol. 190: 3914-3922 [Abstract] [Full Text]  
  • Garcia, D. L., Dillard, J. P. (2008). Mutations in ampG or ampD Affect Peptidoglycan Fragment Release from Neisseria gonorrhoeae. J. Bacteriol. 190: 3799-3807 [Abstract] [Full Text]  
  • Uehara, T., Park, J. T. (2007). An Anhydro-N-Acetylmuramyl-L-Alanine Amidase with Broad Specificity Tethered to the Outer Membrane of Escherichia coli. J. Bacteriol. 189: 5634-5641 [Abstract] [Full Text]  
  • Stubbs, K. A., Balcewich, M., Mark, B. L., Vocadlo, D. J. (2007). Small Molecule Inhibitors of a Glycoside Hydrolase Attenuate Inducible AmpC-mediated beta-Lactam Resistance. J. Biol. Chem. 282: 21382-21391 [Abstract] [Full Text]  
  • Herve, M., Boniface, A., Gobec, S., Blanot, D., Mengin-Lecreulx, D. (2007). Biochemical Characterization and Physiological Properties of Escherichia coli UDP-N-Acetylmuramate:L-Alanyl-{gamma}-D-Glutamyl-meso- Diaminopimelate Ligase. J. Bacteriol. 189: 3987-3995 [Abstract] [Full Text]  
  • Uehara, T., Suefuji, K., Jaeger, T., Mayer, C., Park, J. T. (2006). 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. J. Bacteriol. 188: 1660-1662 [Abstract] [Full Text]  
  • Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M., Park, J. T. (2005). Recycling of the Anhydro-N-Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to N-Acetylglucosamine-Phosphate. J. Bacteriol. 187: 3643-3649 [Abstract] [Full Text]  
  • Stenbak, C. R., Ryu, J.-H., Leulier, F., Pili-Floury, S., Parquet, C., Herve, M., Chaput, C., Boneca, I. G., Lee, W.-J., Lemaitre, B., Mengin-Lecreulx, D. (2004). Peptidoglycan Molecular Requirements Allowing Detection by the Drosophila Immune Deficiency Pathway. J. Immunol. 173: 7339-7348 [Abstract] [Full Text]  
  • Uehara, T., Park, J. T. (2004). The N-Acetyl-D-Glucosamine Kinase of Escherichia coli and Its Role in Murein Recycling. J. Bacteriol. 186: 7273-7279 [Abstract] [Full Text]  
  • Dahl, U., Jaeger, T., Nguyen, B. T., Sattler, J. M., Mayer, C. (2004). Identification of a Phosphotransferase System of Escherichia coli Required for Growth on N-Acetylmuramic Acid. J. Bacteriol. 186: 2385-2392 [Abstract] [Full Text]  
  • Uehara, T., Park, J. T. (2003). Identification of MpaA, an Amidase in Escherichia coli That Hydrolyzes the {gamma}-D-Glutamyl-meso-Diaminopimelate Bond in Murein Peptides. J. Bacteriol. 185: 679-682 [Abstract] [Full Text]  
  • Cheng, Q., Park, J. T. (2002). Substrate Specificity of the AmpG Permease Required for Recycling of Cell Wall Anhydro-Muropeptides. J. Bacteriol. 184: 6434-6436 [Abstract] [Full Text]  
  • Uehara, T., Park, J. T. (2002). Role of the Murein Precursor UDP-N-Acetylmuramyl-L-Ala-{gamma}-D-Glu- meso-Diaminopimelic Acid-D-Ala-D-Ala in Repression of {beta}-Lactamase Induction in Cell Division Mutants. J. Bacteriol. 184: 4233-4239 [Abstract] [Full Text]  
  • Faure, D. (2002). The Family-3 Glycoside Hydrolases: from Housekeeping Functions to Host-Microbe Interactions. Appl. Environ. Microbiol. 68: 1485-1490 [Full Text]  
  • Park, J. T. (2001). Identification of a Dedicated Recycling Pathway for Anhydro-N-Acetylmuramic Acid and N-Acetylglucosamine Derived from Escherichia coli Cell Wall Murein. J. Bacteriol. 183: 3842-3847 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»