title: Properties and purification of N-acetylmuramyl-L-alanine amidase from Staphylococcus aureus H.
abstract: The principal autolytic enzyme activity of the cell sap of Staphylococcus aureus H has been purified 400-fold. It is an N-acetylmuramyl-l-alanine amidase. This enzyme has a molecular weight of 8 to 10 x 10(5), a pH optimum of 7.3, an ionic strength optimum of 0.16 m and a K(m) of 10(-3)m murein repeating units.
mesh_terms: D000409:Alanine / Q000096:biosynthesis; D000581:Amidohydrolases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D000596:Amino Acids / Q000096:biosynthesis; D000606:Amino Sugars / Q000096:biosynthesis; D001329:Autolysis; D002473:Cell Wall / Q000378:metabolism; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D002852:Chromatography, Ion Exchange; D003593:Cytoplasm / Q000201:enzymology; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010406:Penicillins; D010457:Peptidoglycan / Q000378:metabolism; D013210:Staphylococcus / Q000201:enzymology* / Q000378:metabolism; D013237:Stereoisomerism; D014462:Ultrafiltration
chemical_list: D000596:Amino Acids; D000606:Amino Sugars; D010406:Penicillins; D010457:Peptidoglycan; D000581:Amidohydrolases; D000409:Alanine