title: Characterization of the N-Terminal Catalytic Domain of Lytµ1/6, an Endolysin from Streptomyces aureofaciens Phage µ1/6.
abstract: Previous characterization of Lytµ1/6, an endolysin from Streptomyces aureofaciens phage µ1/6, suggested that the N-terminal domain is responsible for the catalytic activity of Lytµ1/6. Mutational analyses (deletions and site-directed mutagenesis) demonstrated that lytic activity of Lytµ1/6 relies on the N-terminal part of about 200 amino acid residues. Various C-terminally truncated versions of Lytµ1/6 failed to cause lysis, indicating the necessity of the CBD for full enzyme activity. Functional analysis of the point mutants suggested that the residues K27, H31, E109, H176, and D184 were essential for lytic activity of the µ1/6 endolysin. Further characterization of the purified Lytµ1/6 revealed that this endolysin is an N-acetylmuramoyl-L-alanine amidase which seems to be unrelated to any of the known conserved catalytic domains of phage endolysins or bacterial autolysins.
authors.affiliation: Institute of Molecular Biology, Laboratory of Prokaryotic Biology, Slovak Academy of Sciences, Bratislava, Slovakia. jarmila.farkasovska@savba.sk.
authors.forename: Jarmila
authors.initials: J
authors.lastname: Farkašovská
authors.affiliation: Institute of Molecular Biology, Laboratory of Prokaryotic Biology, Slovak Academy of Sciences, Bratislava, Slovakia.|Faculty of Natural Sciences, Department of Biology, University of SS. Cyril and Methodius, Trnava, Slovakia.
authors.forename: Andrej
authors.initials: A
authors.lastname: Godány
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D020134:Catalytic Domain; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D017354:Point Mutation; D016415:Sequence Alignment; D013304:Streptomyces aureofaciens / Q000821:virology*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D014764:Viral Proteins; D010450:Endopeptidases; C001143:endolysin