Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling.
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.
Cheng
Q
Q
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
Li
H
H
Merdek
K
K
Park
J T
JT
D000118:Acetylglucosaminidase / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D000606:Amino Sugars / Q000378:metabolism; D002473:Cell Wall / Q000502:physiology; D002874:Chromosome Mapping; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D005798:Genes, Bacterial; D016296:Mutagenesis
D000606:Amino Sugars; D000118:Acetylglucosaminidase