title: Specificity of the action of lysoamidase on Staphylococcus aureus 209P cell walls.
abstract: Specificity of Staphylococcus aureus 209P cell wall hydrolysis by the L1 and L2-bacteriolytic enzymes from lysoamidase lytic complex was studied. L1-peptidase was shown to display both glycyl-glycine endopeptidase and N-acetylmuramyl-L-alanine amidase enzymatic activities on the S. aureus peptidoglycan molecule, whereas L2-peptidase acts as N-acetylmuramyl-L-alanine amidase.
authors.affiliation: Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, 142292, Moscow Region, Russia.
authors.forename: E A
authors.initials: EA
authors.lastname: Begunova
authors.forename: O A
authors.initials: OA
authors.lastname: Stepnaya
authors.forename: V Ya
authors.initials: VY
authors.lastname: Lysanskaya
authors.forename: I S
authors.initials: IS
authors.lastname: Kulaev
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000166:cytology* / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; C060332:lysoamidase; D010447:Peptide Hydrolases