Developmentally regulated proteases from the basidiomycete Schizophyllum commune.

The basidiomycete Schizophyllum commune produces three chromatographically distinguishable proteases which are capable of attack on a variety of other enzymes from S. commune and other sources. These proteases, which are produced during a specific phase of the development cycle, exhibit typical enzyme kinetic patterns, are active in the neutral to weakly alkaline pH range and are inhibited by phenylmethylsulfonyl fluoride, soybean trypsin inhibitor, and ovomucoid. No pattern of specificity toward the test enzymes could be discerned. The proteases co-purify with the activity which causes the increase in cold lability of S. commune phosphoglucomutase reported previously. In addition, one of the protease enzymes could be purified to the point where it had no significant ability to release trichloroacetic acid products from denatured substrates at pH 3 or pH 7. When undenatured hemoglobin was used as a substrate, the purified protease releases a relatively large molecular weight nonheme peptide. Relatively large peptides are also formed after proteolysis of rabbit muscle phosphoglucomutase. These results suggest that the protease carries out only limited proteolysis.