Name

Ply118

Recommended Name ?L-alanyl-D-glutamate peptidase
Alternative Name ?endolysin Ply118
metalloendoprotease
metalloendoproteinase
Uniprot IDQ37976
General Mode of ActionEnzymatic cleavage of peptidoglycan which results in a rapid lysis of the bacterial cell.
phiBIOTICS Family ?Metallopeptidase
Reaction ?1. Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions
    EC: 3.4.24.-
    Corresponding Pfam domain: VanY
    Evidence: experimental (PubMed: 8577256)
Source Organism ?Listeria phage A118
Target Organism ?Listeria monocytogenes
Bacillus megaterium
Disease ?Listeria infections
State ?Tested
Reference ?8577256
11972774


Studies found: 1

Antimicrobial Agent
Study Type
Model
AdministrationRelevant ResultsAdverse Effects and Other IssuesReference ?
Ply118 in vitro
  • set of different serogroups of Listeria monocytogenes strains and closely related Listeria species
 Lytic activity is essentially restricted to the genus Listeria.
CBD (cell wall binding domain) of Ply118 strongly binds to Listeria cells belonging to the serogroup 1/2; generally not recognizing other Gram-positive or Gram-negative bacteria with exception of Bacillus megaterium, thus its not able to lyse them.		 Other Issues
Only full-lenght protein yielded lytic activity.
Any removal of either of the two domains resulted in loss capacity to lyse bacterial cells, demonstrating that both of proposed major domains are necesarry for lytic function of enzyme.		 11972774