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doi:10.22028/D291-39226
Titel: | The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases |
VerfasserIn: | Müller, Maraike Calvert, Matthew Hottmann, Isabel Kluj, Robert Maria Teufel, Tim Balbuchta, Katja Engelbrecht, Alicia Selim, Khaled A. Xu, Qingping Borisova, Marina Titz, Alexander Mayer, Christoph |
Sprache: | Englisch |
Titel: | The Journal of Biological Chemistry |
Bandnummer: | 296 |
Verlag/Plattform: | Elsevier |
Erscheinungsjahr: | 2021 |
Freie Schlagwörter: | peptidoglycan hydrolase lysozyme exo-lytic glycosidase N-acetylmuramidase N-acetylglucosaminidase N-acetylmuramoyl amidase cell wall recycling Rossmann-fold |
DDC-Sachgruppe: | 500 Naturwissenschaften |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that catalyze an endo-lytic cleavage of peptidoglycan; i.e., they hydrolyze the β-1,4-glycosidic bonds connecting N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). In contrast, little is known about exo-β-N-acetylmuramidases, which catalyze an exo-lytic cleavage of β-1,4-MurNAc entities from the non-reducing ends of peptidoglycan chains. Such an enzyme was identified earlier in the bacterium Bacillus subtilis, but the corresponding gene has remained unknown so far. We now report that ybbC of B. subtilis, renamed namZ, encodes the reported exo-β-N-acetylmuramidase. A ΔnamZ mutant accumulated specific cell wall fragments and showed growth defects under starvation conditions, indicating a role of NamZ in cell wall turnover and recycling. Recombinant NamZ protein specifically hydrolyzed the artificial substrate para-nitrophenyl β-MurNAc and the peptidoglycan-derived disaccharide MurNAc-β-1,4-GlcNAc. Together with the exo-β-N-acetylglucosaminidase NagZ and the exo-muramoyl-L-alanine amidase AmiE, NamZ degraded intact peptidoglycan by sequential hydrolysis from the non-reducing ends. A structure model of NamZ, built on the basis of two crystal structures of putative orthologs from Bacteroides fragilis, revealed a two-domain structure including a Rossmann-fold-like domain that constitutes a unique glycosidase fold. Thus, NamZ, a member of the DUF1343 protein family of unknown function, is now classified as the founding member of a new family of glycosidases (CAZy GH171; www. cazy.org/GH171.html). NamZ-like peptidoglycan hexosaminidases are mainly present in the phylum Bacteroidetes and less frequently found in individual genomes within Firmicutes (Bacilli, Clostridia), Actinobacteria, and γ-proteobacteria. |
DOI der Erstveröffentlichung: | 10.1016/j.jbc.2021.100519 |
URL der Erstveröffentlichung: | https://doi.org/10.1016/j.jbc.2021.100519 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-392268 hdl:20.500.11880/35350 http://dx.doi.org/10.22028/D291-39226 |
ISSN: | 0021-9258 |
Datum des Eintrags: | 6-Mär-2023 |
Bezeichnung des in Beziehung stehenden Objekts: | Supporting information |
In Beziehung stehendes Objekt: | https://ars.els-cdn.com/content/image/1-s2.0-S0021925821002970-mmc1.pdf |
Fakultät: | NT - Naturwissenschaftlich- Technische Fakultät |
Fachrichtung: | NT - Chemie |
Professur: | NT - Univ.-Prof. Dr. phil. Alexander Titz |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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1-s2.0-S0021925821002970-main.pdf | 2,76 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons