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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

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