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Originally published In Press as doi:10.1074/jbc.M004797200 on September 7, 2000
J. Biol. Chem., Vol. 275, Issue 50, 39032-39038, December 15, 2000
Characterization of a -N-acetylglucosaminidase of
Escherichia coli and Elucidation of Its Role in
Muropeptide Recycling and -Lactamase Induction*
Walter
Vötsch and
Markus F.
Templin
From the Max-Planck-Institut für Entwicklungsbiologie,
Abteilung Biochemie, Spemannstrasse 35, 72076 Tübingen, Germany
Using the known mapping position the gene
encoding a -1,4-N-acetylglucosaminidase needed for
the degradation of muropeptides could be identified. nagZ
encodes a cytosolic enzyme active on N-actylglucosamyl- -1,4-(1,6)-anhydromuramic acid
containing muropeptides. These degradation products of the
peptidoglycan are formed during the enlargement of the murein sacculus
as a consequence of a growth mechanism, which couples the controlled
degradation of the cell wall polymer with the insertion of new
material. NagZ is needed for the formation of monosaccharides from the
released disaccharides during the cytosolic steps of the
muropeptide-recycling pathway. The formation of intracellular
1,6-anhydro-N-acetylmuramyl-peptides is important for the
expression control of the inducible -lactamases of the AmpC type. A
mutant lacking active NagZ cannot establish AmpC mediated -lactam
resistance. The biochemical characterization of the enzyme showed its
activity on different muropeptides and inhibitors of enzyme activity
could be identified. This observation might be important for designing
inhibitors of NagZ that could prevent the establishment of -lactam
resistance of Enterobacteria possessing inducible
-lactamases.
*
This work was supported by European Commission Project
BIOU-CT96-0122.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Present address: NMI,
an der Universität Tübingen, Markwiesenstr. 55, 72770 Reutlingen, Germany. Tel.: 49-7121-51530-802; Fax: 49-7121-51530-16; E-mail: Templin@nmi.de.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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