5 research outputs found
The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases
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
Rokkatan: Scaling an RTS Game Design
While massively multiplayer online role-playing games involve large numbers of simultaneous players, two other popular game classes -- first person action and real-time strategy games -- are still rarely discussed for massively multiplayer gaming. This paper presents our work on Rokkatan, an online game which implements the common concept of real-time strategy in a scalable multiplayer design. In order to allow hundreds of users to participate in a single game session, Rokkatan uses our proxy-server network architecture which provides the required scalability and responsiveness required for a fast-paced gaming style. An analytical scalability model integrated into Rokkatan allows to forecast the maximum number of simultaneous players. Our experiments demonstrate good prediction quality of the model and high scalability of Rokkatan, which allows several hundreds of users to participate in a single game session
The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases
Datenlage und Herausforderungen empirischer Sozialforschung
Hummels K, Kamp M, Spielhaus R, Stetten L-M, Zick A. Datenlage und Herausforderungen empirischer Sozialforschung. In: Biene J, Daase C, Junk J, Müller H, eds. Salafismus und Dschihadismus in Deutschland. Frankfurt a. M.: Campus; 2016: 43-77
The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases.
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