Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoprotease.
The neutral protease isolated from Bacillus cereus (BRL-70) has been purified by affinity chromatography and characterized. The enzyme exhibits a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, has a molecular weight of 34 000 by ultracentrifugation, and contains one enzymatically essential zinc atom per 34 000 g. These data together with the amino acid composition, response to metal substitution, chemical modification, and substrate specificity all indicate that this protease is monomeric and is a typical bacterial neutral metalloprotease.
D000596:Amino Acids / Q000032:analysis; D001409:Bacillus cereus / Q000201:enzymology*; D007700:Kinetics; D008667:Metalloproteins / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013820:Thermolysin / Q000378:metabolism; D015032:Zinc
D000596:Amino Acids; D008667:Metalloproteins; D010447:Peptide Hydrolases; D013820:Thermolysin; D015032:Zinc