Structural and catalytic properties of peptidase N from Escherichia coli K-12

摘要: Abstract Escherichia coli K-12 strains contain a single cytosolic activity, peptidase N, capable of hydrolyzing alanine-p-nitroanilide. The enzyme is monomeric, acidic protein with molecular weight 87,000, containing sulfhydryl group essential for activity. Substrate specificity studies show preference hydrophobic peptides and requirement free α-amino groups. Peptidase N has no measurable endoproteolytic activity on protein, large peptide, or signal peptide substrates. These results suggest that aminopeptidase whose physiological role as yet still unclear. It likely to be involved in the late stages turnover events degradation specific cellular components such attenuator peptides.