Evidence for extrusion of unfolded extracellular enzyme polypeptide chains through membranes of Bacillus amyloliquefaciens.
The production of extracellular alpha-amylase and protease by protoplasts of Bacillus amyloliquefaciens has been achieved. The production of enzymically active protease was totally dependent on a high concentration of either Mg2+, Ca2+, or spermidine, but production of active alpha-amylase was not. This cation dependence of protease production was seen immediately upon addition of lysozyme to intact cells. The cations could prevent the inactivation of protease and alter the cytoplasmic membrane configuration of protoplasts. Production of active alpha-amylase and protease by protoplasts was totally inhibited by proteolytic enzymes such as trypsin, alpha-chymotrypsin, or the organism's purified extracellular protease. The evidence suggests that these degradative enzymes act specifically on the emerging polypeptide of the extracellular enzyme and that the polypeptide emerges in a conformation different from that of the native molecule.
D000681:Amylases / Q000096:biosynthesis / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000096:biosynthesis; D002118:Calcium / Q000494:pharmacology; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002918:Chymotrypsin / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D008274:Magnesium / Q000494:pharmacology; D009113:Muramidase / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000096:biosynthesis / Q000378:metabolism*; D011487:Protein Conformation; D011523:Protoplasts / Q000187:drug effects / Q000201:enzymology; D013095:Spermidine / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
D001426:Bacterial Proteins; D000681:Amylases; D009113:Muramidase; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin; D008274:Magnesium; D002118:Calcium; D013095:Spermidine