Sep 14, 1976

Purification and properties of a new aminopeptidase from Escherichia COLI K12

Biochimica Et Biophysica Acta
L M Yang, R L Somerville


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.

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Mentioned in this Paper

Cations, Divalent
Aminopeptidase II
Alkalescens-Dispar Group
Structure-Activity Relationship
Serine Proteinase Inhibitors
Escherichia coli K12
Sulfhydryl Reagents

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