The study of Escherichia coli proteases. Intracellular serine protease of E. coli-an analogue of bacillus proteases.
Two serine proteases in extracts of Escherichia coli grown to stationary phase were purified to homogeneity using affinity chromatography on gramicidin S-Sepharose 4B. One enzyme was closely related to, if not identical with, the 'trypsin-like' protease II of E. coli. The other was capable of cleaving the subtilisin chromogenic substrate N-carbobenzoxy-L-alanyl-L-alanyl-L-leucine-p-nitroanilide and resembled the intracellular serine proteases of Bacillus spp. The amino acid composition of this E. coli protease was similar to that of the Bacillus licheniformis enzyme. These data indicate a relationship between proteolytic enzymes of evolutionary distant Gram-negative Enterobacteriaceae and Gram-positive spore-forming Bacillus.
D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000201:enzymology; D002847:Chromatography, Agarose; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D012694:Serine; D013379:Substrate Specificity
D000596:Amino Acids; D012694:Serine; D010447:Peptide Hydrolases