Intracellular proteases of Bacillus stearothermophilus.
Cell-free extracts of Bacillus stearothermophilus have been shown to exhibit proteolytic activity toward casein as well as specific activity to catalyze the hydrolysis of furylacryloylglycyl-l-leucine amide, furylacryloylglycine, and carbobenzoxyl-glycine-p-nitrophenyl ester, indicating the presence of a neutral proteinase, a carboxypeptidase-like enzyme, and an alkaline proteinase. The neutral proteinase and carboxypeptidase-like activities were separated by gel filtration over Bio-Gel P-60, and both were reversibly inhibited by 1, 10-phenanthroline. The esterase activity was inhibited by diisopropylfluorophosphate, which did not affect other enzymatic activities and was insensitive to 1, 10-phenanthroline and ethylenediaminetetra-acetic acid.
D000596:Amino Acids / Q000378:metabolism; D001322:Autoanalysis; D001407:Bacillus / Q000201:enzymology* / Q000378:metabolism; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism; D002474:Cell-Free System; D002850:Chromatography, Gel; D004151:Dipeptides / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D004950:Esterases / Q000378:metabolism; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D010618:Phenanthrolines / Q000494:pharmacology; D013053:Spectrophotometry
D000596:Amino Acids; D002364:Caseins; D004151:Dipeptides; D010618:Phenanthrolines; D004492:Edetic Acid; D004950:Esterases; D002268:Carboxypeptidases; D010447:Peptide Hydrolases