Hydrolytic ability of acid protease of Fusarium culmorum and its possible role in phytopathogenesis.
It was found that the acid protease of Fusarium culmorum can hydrolyze various proteins of plant origin including polygalacturonase inhibitor from bean (BPI) and soybean trypsin inhibitor (STI). The highest hydrolysis extent of BPI and STI by the enzyme was only 5% and 3% respectively. The partially hydrolyzed BPI lost its inhibition ability to fungal polyglacturonases. Similarly, the partially hydrolyzed STI lost its inhibition ability to trypsin and fungal alkaline protease. The F. culmorum acid protease showed broad substrate specificity towards synthetic dipeptides.
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases; D004151:Dipeptides; D010450:Endopeptidases / Q000378:metabolism*; D007887:Fabaceae; D005670:Fusarium / Q000201:enzymology* / Q000472:pathogenicity; D007700:Kinetics; D010946:Plants, Medicinal; D011096:Polygalacturonase / Q000037:antagonists & inhibitors; D013379:Substrate Specificity; D014359:Trypsin Inhibitor, Kazal Pancreatic
D004151:Dipeptides; D014359:Trypsin Inhibitor, Kazal Pancreatic; D011096:Polygalacturonase; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases