[Hydrolysis of a Staphylococcus aureus cell wall peptidoglycan by 209 P lysoamidase].
Hydrolysis of Staphylococcus aureus 209 P cell wall peptidoglycan was accompanied by the liberation of 1.3 mol of C-terminal and 1.2 mol of N-terminal glycine per mole of Glu as well as of 0.5 mol of N-terminal and 0.3 mol of C-terminal alanine. Gel chromatography on Sephadex G-25, ion-exchange chromatography on QAE-Sephadex A-50 and paper electrophoresis of S. aureus peptidoglycan hydrolysates gave seven homogeneous fractions; these fractions were structurally defined. Lysoamidase hydrolyzed bonds Mur-Ala, Gly-Gly and Mur-GlcN in the peptidoglycan molecule. Hydrolysis of glycan chains was accompanied by the formation of large fragments, (GlcN-Mur)9 and (GlcN-Mur)28. The lytic effect of lysoamidase on S. aureus peptidoglycan is coupled with bacteriolytic enzymes of lysoamidase: acetmuramyl amidase, glycyl--glycine endopeptidase and acetyl--muramidase.
Severin
A I
AI
Il'chenko
V Ia
VIa
Kulaev
I S
IS
D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D002473:Cell Wall / Q000201:enzymology; D002853:Chromatography, Liquid; D004590:Electrophoresis, Paper; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry*; D010457:Peptidoglycan / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*
D010457:Peptidoglycan; C060332:lysoamidase; D010447:Peptide Hydrolases
Gidroliz peptidoglikana kletochnykh stenok Staphylococcus aureus 209 P lizoamidazoĭ.