Purification and properties of a proline iminopeptidase from Propionibacterium acnes.
Proline iminopeptidase was extracted from the cells of a strain of Propionibacterium acnes and purified. The molecular weight was estimated to be about 120,000 by SDS-polyacrylamide gel electrophoresis. The enzyme showed the highest activity at 50 degrees C-55 degrees C and its optimum pH was found at 7.5-8.0. The enzyme activity was inhibited by p-chloromercuribenzoate, indicating that this peptidase is a SH-enzyme. Especially prolyl-glycyl-glycine but also prolyl-proline bonds were hydrolyzed by this enzyme, glycyl-proline was not split.
D000626:Aminopeptidases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D003773:Dental Plaque / Q000382:microbiology; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011425:Propionibacterium acnes / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
D004791:Enzyme Inhibitors; D000626:Aminopeptidases; C022450:prolyl aminopeptidase