Aminopeptidase I activities in several microorganisms.
Aminopeptidase I activity which was found to be localized in the same subcellular fraction and to be similarly heat stable was partially purified by a common procedure from Escherichia coli B, Escherichia coli K12, Enterobacter aerogenes, Salmonella typhimurium, Serratia marcescens Pseudomonas aeruginosa, and Proteus vulgaris. The enzyme preparations were shown to contain a single animopeptidase active toward both leucylleucine and methionylalanylserine by mixed-substrate initial-velocity kinetic analysis. The Km value for leucylleucine was virtually identical for the aminopeptidases of all of the organisms, as was the Km value for methionylalanylserine.
D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D004754:Enterobacter / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D011514:Proteus vulgaris / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D012486:Salmonella typhimurium / Q000201:enzymology; D012706:Serratia marcescens / Q000201:enzymology; D013045:Species Specificity; D013379:Substrate Specificity
D000626:Aminopeptidases