Results 51 to 60 of about 11,815 (217)

Diversity of the lysozyme fold: structure of the catalytic domain from an unusual endolysin encoded by phage Enc34

Scientific Reports, 2022
Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and
Elina Cernooka, Janis Rumnieks, Nikita Zrelovs, Kaspars Tars, Andris Kazaks   +4 more
doaj   +1 more source

The Bifunctional Cell Wall Hydrolase CwlT Is Needed for Conjugation of the Integrative and Conjugative Element ICEBs1 in Bacillus subtilis and B. anthracis [PDF]

, 2014
The mobile genetic element ICEBs1 is an integrative and conjugative element (ICE) found in Bacillus subtilis. One of the ICEBs1 genes, cwlT, encodes a cell wall hydrolase with two catalytic domains, a muramidase and a peptidase.
DeWitt, Tyler, Grossman, Alan Davis
core   +1 more source

Identification of a novel zinc metalloprotease through a global analysis of clostridium difficile extracellular proteins [PDF]

, 2013
Clostridium difficile is a major cause of infectious diarrhea worldwide. Although the cell surface proteins are recognized to be important in clostridial pathogenesis, biological functions of only a few are known.
A Barketi-Klai, A Bateman, A Boetzkes, A Dhalluin, A Molla, A Tasteyre, A Tasteyre, A Tasteyre, A Wright, A Wright, AJ Waligora, B Singh, BR Hoffmann, C Janoir, C Schwan, CB Reynolds, CC Häse, CM Surawicz, D Lyras, D Zhang, Davide Serruto, DC Nelson, DE Voth, DJ Rigden, E Calabi, E Calabi, EJ Kuipers, F Tonello, FH Niesen, Francesca Cantini, G Bensi, GA Dalkas, GM Slynn, H Maeda, I Poilane, Jeffrey T. Rubino, JM Kirby, JR O'Connor, JW Teo, K Mukherjee, K Yokoyama, KR Klimpel, L de la Riva, L Tulli, LG Pacheco, M Cerquetti, M Desvaux, M Miura, M Monot, M Rupnik, M Sebaihia, M Warny, MA Breidenbach, Manuele Martinelli, Maria Scarselli, Massimiliano Biagini, Meera Unnikrishnan, Mikael Skurnik, MJ Rodríguez-Ortega, N Sengupta, Nathalie Norais, NM Hooper, NS Duesbery, O Schneewind, Rosanna Leuzzi, RP Fagan, S Péchiné, S Péchiné, S Ravipaty, SA Kuehne, T Karasawa, T Karjalainen, TC Dingle, Valeria Cafardi   +73 more
core   +12 more sources

Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis

Nature Communications, 2023
The FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a ...
Jianwei Li, Xin Xu, Jian Shi, Juan A. Hermoso, Lok-To Sham, Min Luo   +5 more
doaj   +1 more source

Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases

Current Opinion in Structural Biology, 2017
The major component of bacterial cell wall is peptidoglycan (PG), a complex polymer formed by long glycan chains cross-linked by peptide stems. PG is in constant equilibrium requiring well-orchestrated coordination between synthesis and degradation. The resulting cell-wall fragments can be recycled, act as messengers for bacterial communication, as ...
Alcorlo, Martín, Martínez-Caballero, Siseth, Molina, Rafael, Hermoso, Juan A.   +3 more
openaire   +4 more sources

The PECACE domain: a new family of enzymes with potential peptidoglycan cleavage activity in Gram-positive bacteria

BMC Genomics, 2005
Background The metabolism of bacterial peptidoglycan is a dynamic process, synthases and cleavage enzymes are functionally coordinated. Lytic Transglycosylase enzymes (LT) are part of multienzyme complexes which regulate bacterial division and elongation.
Di Guilmi Anne, Vernet Thierry, Dideberg Otto, Pagliero Estelle   +3 more
doaj   +1 more source

Different walls for rods and balls: the diversity of peptidoglycan [PDF]

, 2014
Peptidoglycan performs the essential role of resisting turgor in the cell walls of most bacteria. It determines cell shape, and its biosynthesis is the target for many important antibiotics.
Braun V., Glauner B., Jonge B.L., Park J., Verwer R.W.   +4 more
core   +1 more source

O-Glycosylation as a Novel Control Mechanism of Peptidoglycan Hydrolase Activity [PDF]

Journal of Biological Chemistry, 2013
Acm2, the major autolysin of Lactobacillus plantarum, is a tripartite protein. Its catalytic domain is surrounded by an O-glycosylated N-terminal region rich in Ala, Ser, and Thr (AST domain), which is of low complexity and unknown function, and a C-terminal region composed of five SH3b peptidoglycan (PG) binding domains.
Wolfgang Egge-Jacobsen, Marie-Pierre Chapot-Chartier, Marie-Pierre Chapot-Chartier, Pascal Hols, Audrey Beaussart, Thomas Rolain, Michiel Kleerebezem, Hervé Degand, Yves F. Dufrêne, Peter A. Bron, Pascal Courtin, Pascal Courtin, Elvis Bernard, Elvis Bernard, Elvis Bernard, Pierre Morsomme   +15 more
openaire   +5 more sources

Phage lytic proteins: Biotechnological applications beyond clinical antimicrobials [PDF]

, 2017
Most bacteriophages encode two types of cell wall lytic proteins: endolysins (lysins) and virion-associated peptidoglycan hydrolases. Both enzymes have the ability to degrade the peptidoglycan of Gram-positive bacteria resulting in cell lysis when they ...
Donovan, David M., García Suárez, María Pilar, Gutiérrez, Diana, Martínez Fernández, Beatriz, Rodríguez González, Ana, Rodríguez, Lorena   +5 more
core   +1 more source

Physiological significance of the peptidoglycan hydrolase, LytM, in Staphylococcus aureus [PDF]

FEMS Microbiology Letters, 2010
Autolysins in bacteria are peptidoglycan hydrolases with roles in growth, turnover and cell lysis. LytM was identified as the only autolysin in a previously reported autolysis-deficient (lyt(-) ) strain of Staphylococcus aureus. Purified LytM has been studied in great detail for its lytic properties and its production is elevated in vancomycin ...
Vineet K. Singh, Mary R. Carlos, Kuldeep Singh   +2 more
openaire   +3 more sources