Isolation and characterization of a peptidase from an oral strain of Corynebacterium matruchotii.
From the cell extract of Corynebacterium matruchotii strain ATCC 14266, a peptidase could be isolated and purified, increasing the specific activity 267 times. This enzyme with a molecular weight of 60,000 was completely inactivated by heating at 50 degrees C for 20 min, its optimum pH was found to be pH 7.5 and the isoelectric point was 4.1. The peptidase was inhibited by diisopropylfluorophosphate, phenylmethanesulfonyl fluoride, tosyl-L-lysine chloromethyl ketone, chymostatin and urea. Among various synthetic substrates tested, only benzoyl-L-arginine-p-nitroanilide and benzoyl-L-arginine ethylester were found to be hydrolyzed by this enzyme. Several proteins investigated were not hydrolyzed, but the enzyme inactivated a peptidic staphylococcal bacteriocin.
D001430:Bacteriocins / Q000378:metabolism; D003352:Corynebacterium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D001430:Bacteriocins; D011480:Protease Inhibitors; D010447:Peptide Hydrolases