Purification and properties of a new aminopeptidase from Escherichia COLI K12.
An aminopeptidase (EC 3.4.11.-) capmable of hydrolyzing L-alanyl-beta-naphthyl-amide and certain other aminoacyl beta-naphthylamides was purified to homogeneity from extracts of Exherichia coli K-12. The enzyme, designated aminopeptidase II, is a monomeric protein of mol. wt. 100 000. It exhibits a broad pH optimum in the range pH 7.0--9.0. Although Zn2+, Fe3+ and Cr3+ are strong inhibitors of enzyme activity, a metal requirement for catalysis could not be firmly established. Neither sulfhydryl reagents nor serine protease inhibitors affected enzyme activity.
D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent; D002455:Cell Division; D002857:Chromium / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D013329:Structure-Activity Relationship
D002413:Cations, Divalent; D002857:Chromium; D007501:Iron; D000626:Aminopeptidases