PMID:10940025
| Citation |
Cheng, Q, Li, H, Merdek, K and Park, JT (2000) Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J. Bacteriol. 182:4836-40 |
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| Abstract |
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. |
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| Keywords |
Acetylglucosaminidase/genetics; Acetylglucosaminidase/metabolism; Acetylglucosaminidase/physiology; Amino Sugars/metabolism; Cell Wall/physiology; Chromosome Mapping; Cytoplasm/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/physiology; Genes, Bacterial; Mutagenesis |
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