[Characterization and separation of exocellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602].
Two exocellular enzymes have been characterized in the culture media of sporulating Bacillus sphaericus 9602 : a gamma-D-glutamyl-(L) meso-diaminopimelate endopeptidase and a L-lysyl-D-alanine carboxypeptidase. These two enzymes and the corresponding membrane-bound peptidases found in Bacillus sphaericus and Bacillus subtilis strains have similar activities. Their separation is described. Both enzymes were precipitated between 25 and 65 per cent (NH4)2SO4 saturation and a first chromatography was carried out on a column of DEAE-cellulose. The separation was performed by chromatography on hydroxyapatite, each enzyme was finally filtered through Ultrogel AcA 34. After separation, the endopeptidase activity and the carboxypeptidase activity increased respectively 93 and 11 fold. Both enzymes have a molecular weight near 200 000. By gel electrophoresis at pH 8.5, they were shown to have different mobilities : the carboxypeptidase is more anionic than the endopeptidase.
D000409:Alanine; D001407:Bacillus / Q000201:enzymology*; D001412:Bacillus subtilis / Q000201:enzymology; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D003960:Diaminopimelic Acid; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008239:Lysine; D008970:Molecular Weight; D013045:Species Specificity
D003960:Diaminopimelic Acid; D002268:Carboxypeptidases; D010450:Endopeptidases; D008239:Lysine; D000409:Alanine
Mise en évidence et séparation d'une gamma-D-glutamyl-(L)meso-diaminopimélate endopeptidase et d'une LD-carboxypeptidase exocellulaires à partir de Bacillus sphaericus 9602