Results 41 to 50 of about 14,027 (185)

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

open access: yesScientific 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   +4 more
doaj   +1 more source

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

open access: yesBMC 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   +3 more
doaj   +1 more source

Molecular imaging of glycan chains couples cell-wall polysaccharide architecture to bacterial cell [PDF]

open access: yes, 2018
Biopolymer composite cell walls maintain cell shape and resist forces in plants, fungi and bacteria. Peptidoglycan, a crucial antibiotic target and immunomodulator, performs this role in bacteria.
A Typas   +40 more
core   +2 more sources

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

open access: yesNature 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   +5 more
doaj   +1 more source

Cell wall peptidoglycan in Mycobacterium tuberculosis: An Achilles’ heel for the TB-causing pathogen [PDF]

open access: yes, 2019
Tuberculosis (TB), caused by the intracellular pathogen Mycobacterium tuberculosis, remains one of the leading causes of mortality across the world. There is an urgent requirement to build a robust arsenal of effective antimicrobials, targeting novel ...
Bhakta, S   +6 more
core   +2 more sources

Binding site‐shaped repeated sequences of bacterial wall peptidoglycan hydrolases [PDF]

open access: yesFEBS Letters, 1994
The non‐catalytic C‐terminal regions of the N‐acetylmuramidase (lysozyme) of Clostridium acetobutylicum and N‐acetylmuramoyl(d‐lactyl)‐l‐alanine amidases CwlA of Bacillus subtilis, ORFL3 and CwlL of Bacillus licheniformis were previously reported to have similarities with the amino acid sequence of the non‐catalytic N‐terminal module of the ...
Ghuysen, Jean-Marie   +3 more
openaire   +2 more sources

More than just lysins: peptidoglycan hydrolases tailor the cell wall. [PDF]

open access: yesCurr Opin Microbiol, 2011
Enzymes that degrade the peptidoglycan (PG) cell wall layer called PG hydrolases or autolysins are often thought of as destructive forces. Phages employ them to lyse their host for the release of virion particles and some bacteria secrete them to eliminate (lyse) their competition.
Uehara T, Bernhardt TG.
europepmc   +4 more sources

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

open access: yes, 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

Cell wall elongation mode in Gram-negative bacteria is determined by peptidoglycan architecture [PDF]

open access: yes, 2013
Cellular integrity and morphology of most bacteria is maintained by cell wall peptidoglycan, the target of antibiotics essential in modern healthcare.
Cadby, A.   +4 more
core   +1 more source

Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation [PDF]

open access: yes, 2020
The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Deletion of a gene encoding a putative deacetylase, Agd3, leads to defects in GAG deacetylation, biofilm formation, and ...
A Ghafoor   +84 more
core   +3 more sources

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