Recommended Name ?prophage LambdaBa02, N-acetylmuramoyl-L-alanine amidase PlyL
Systematic Name ?peptidoglycan amidohydrolase
Alternative Name ?prophage LambdaBa02 endolysin
acetylmuramoyl-alanine amidase
acetylmuramyl-alanine amidase
acetylmuramyl-L-alanine amidase
N-acetylmuramic acid L-alanine amidase
N-acetylmuramyl-L-alanine amidase
N-acetylmuramylalanine amidase
N-acylmuramyl-L-alanine amidase
peptidoglycan amidohydrolase
Uniprot IDQ81WA9
General Mode of ActionEnzymatic cleavage of peptidoglycan which results in a rapid lysis of the bacterial cell.
phiBIOTICS Family ?NAM amidase
Reaction ?1. Catalysis of the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides (R04112)
    Corresponding Pfam domain: Amidase_2
    Evidence: experimental (PubMed: 16103125)
Source Organism ?Bacillus anthracis
Target Organism ?Bacillus anthracis
Bacillus cereus
Disease ?Anthrax (inhalation, cutaneous, intestinal) (Bacillus anthracis)
Gastroenteritis (Bacillus cereus)
State ?Tested
Reference ?16103125

Studies found: 1

Antimicrobial Agent
Study Type
AdministrationRelevant ResultsAdverse Effects and Other IssuesReference ?
PlyL in vitro
  • Bacillus anthracis (Sterne 34F2)
    Bacillus cereus ATCC 4342
    Bacillus megaterium WH320
    Bacillus subtilis 168
    Escherichia coli CFT073
Efficient lytic activity against B. cereus, (efficacy compared to that reported for PlyG on B. anthracis); relatively high lytic activity against B. megaterium and low but detectable lytic activity was established on B. subtilis and B. anthracis. Other Issues
Lytic activity of C' truncated form of the lysin was found to be more active then its full-lenght form, most due to some inhibitory effects of the C-terminal domain on the N-terminal enzymatic domain.