Pseudomonas aeruginosa LasD processes the inactive LasA precursor to the active protease form.
LasA and LasD are staphylolytic proteinases which are secreted by the opportunistic pathogen Pseudomonas aeruginosa. We have previously described the purification and characterization of both LasA and LasD, a 21-kDa protein which shares many of the enzymatic properties of LasA. In this follow-up study we describe the isolation of the 42-kDa precursor of LasA (proLasA) and demonstrate the ability of the purified LasD proteinase to cleave the inactive proLasA to the 20-kDa active form of the proteinase.
Park
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Department of Microbiology, Ohio State University, Columbus, Ohio 43210-1292, USA.
Galloway
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DR
D001426:Bacterial Proteins; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics; D006868:Hydrolysis; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D011498:Protein Precursors / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D012697:Serine Endopeptidases / Q000378:metabolism* / Q000502:physiology
D001426:Bacterial Proteins; D011498:Protein Precursors; D010450:Endopeptidases; C095769:LasD protein, Pseudomonas aeruginosa; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases; C066371:staphylolytic protease